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Conserved domains on  [gi|491949535|ref|WP_005687018|]
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2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase [Lacticaseibacillus rhamnosus]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 9-234 2.34e-114

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member TIGR03532:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 231  Bit Score: 326.71  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535    9 IISTIANSKKTTPVKVYLKGKLADLHFPKSVHAFIGKHTGTVIGDWTEIQPVLKT--AKLDDYYVEAAGRNTGVPLLDIK 86
Cdd:TIGR03532   4 IIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEAnkDKIKDYRIENDRRNSAIPLLDLK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535   87 TTNARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTI 166
Cdd:TIGR03532  84 NINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKPVVI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535  167 GDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTEAKTVLLDELRKL 234
Cdd:TIGR03532 164 EDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 9-234 2.34e-114

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 326.71  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535    9 IISTIANSKKTTPVKVYLKGKLADLHFPKSVHAFIGKHTGTVIGDWTEIQPVLKT--AKLDDYYVEAAGRNTGVPLLDIK 86
Cdd:TIGR03532   4 IIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEAnkDKIKDYRIENDRRNSAIPLLDLK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535   87 TTNARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTI 166
Cdd:TIGR03532  84 NINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKPVVI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535  167 GDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTEAKTVLLDELRKL 234
Cdd:TIGR03532 164 EDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 89-211 5.66e-45

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 147.14  E-value: 5.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGD 168
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491949535 169 HVMTGANAVVLEGVTVGEGAVIAAGAVVI---------------NDVPAH-TVVAGVPA 211
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTqstpiydretgeiyyGRVPPGsVVVAGSLP 139
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 68-232 5.88e-37

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 130.70  E-value: 5.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  68 DYYVEAAGRNTGVplldikttnaRIEPGAIIRDQVLIGDNaVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIG 147
Cdd:PRK11830  92 AGWDEARFKEAGV----------RVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 148 AGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGaVVIN----------------DVPAHTVV-AG-V 209
Cdd:PRK11830 161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMG-VFLGqstkiydretgevhygRVPAGSVVvPGsL 239

                        170       180       190
                 ....*....|....*....|....*....|...
gi 491949535 210 PAK----------VIKKVNDQTEAKTVLLDELR 232
Cdd:PRK11830 240 PSKdggyslycavIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 80-232 4.22e-36

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 128.31  E-value: 4.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  80 VPLL--DIKTTNARIEPGAIIRDQVLIGDNaVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVE 157
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 158 PPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVV-----IND----------VPAH-TVVAGV-----------P 210
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLtastkIYDrvtgevyygrVPAGsVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 491949535 211 AKVIKKVNDQTEAKTVLLDELR 232
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-84 1.52e-30

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 108.02  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535    5 DTEKIISTIANSKKTTPVKVYLKGKLADLHFP-KSVHAFIGKHTGTVIGDWTEIQPVLK--TAKLDDYYVEAAGRNTGVP 81
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEanKDKIEDYHIENDRRNSAIP 80


                  ...
gi 491949535   82 LLD 84
Cdd:pfam08503  81 LLD 83
 
Name Accession Description Interval E-value
DapD_Ac TIGR03532
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the ...
 9-234 2.34e-114

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase; This enzyme is part of the diaminopimelate pathway of lysine biosynthesis. Alternate name: tetrahydrodipicolinate N-acetyltransferase. Note that IUBMB lists this alternate name as the accepted name. Unfortunately, the related succinyl transferase acting on the same substrate (EC:2.3.1.117, TIGR00695) uses the opposite standard. We have decided to give these two enzymes names which more clearly indicated that they act on the same substrate.


Pssm-ID: 132571 [Multi-domain]  Cd Length: 231  Bit Score: 326.71  E-value: 2.34e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535    9 IISTIANSKKTTPVKVYLKGKLADLHFPKSVHAFIGKHTGTVIGDWTEIQPVLKT--AKLDDYYVEAAGRNTGVPLLDIK 86
Cdd:TIGR03532   4 IIRYIGNAKKSTPVKVYVKGDLEQVDFPESIKKFGSGHSGVLFGEWEDIEPFIEAnkDKIKDYRIENDRRNSAIPLLDLK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535   87 TTNARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTI 166
Cdd:TIGR03532  84 NINARIEPGAIIRDQVIIGDNAVIMMGAVINIGAEIGEGTMIDMNAVLGGRATVGKNVHIGAGAVLAGVIEPPSAKPVVI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535  167 GDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTEAKTVLLDELRKL 234
Cdd:TIGR03532 164 EDNVLIGANAVILEGVRVGKGAVVAAGAIVTEDVPPNTVVAGVPAKVIKQVDEKTKDKTELEDDLRKL 231
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 89-211 5.66e-45

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 147.14  E-value: 5.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGD 168
Cdd:cd03350    1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491949535 169 HVMTGANAVVLEGVTVGEGAVIAAGAVVI---------------NDVPAH-TVVAGVPA 211
Cdd:cd03350   81 DVFIGANCEVVEGVIVGKGAVLAAGVVLTqstpiydretgeiyyGRVPPGsVVVAGSLP 139
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 68-232 5.88e-37

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 130.70  E-value: 5.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  68 DYYVEAAGRNTGVplldikttnaRIEPGAIIRDQVLIGDNaVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIG 147
Cdd:PRK11830  92 AGWDEARFKEAGV----------RVVPGAVVRRGAYIAPN-VVLMPSYVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 148 AGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGaVVIN----------------DVPAHTVV-AG-V 209
Cdd:PRK11830 161 GGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMG-VFLGqstkiydretgevhygRVPAGSVVvPGsL 239

                        170       180       190
                 ....*....|....*....|....*....|...
gi 491949535 210 PAK----------VIKKVNDQTEAKTVLLDELR 232
Cdd:PRK11830 240 PSKdggyslycavIVKKVDAKTRSKTSINELLR 272
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 80-232 4.22e-36

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 128.31  E-value: 4.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  80 VPLL--DIKTTNARIEPGAIIRDQVLIGDNaVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVE 157
Cdd:COG2171   86 VPLKfdYFKPAGVRIVPGARVRLGAYLAPG-VVLMPSFVNIGAYVDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 158 PPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVV-----IND----------VPAH-TVVAGV-----------P 210
Cdd:COG2171  165 PLQAAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLtastkIYDrvtgevyygrVPAGsVVVPGSlpgkdgdyglyC 244

                        170       180
                 ....*....|....*....|..
gi 491949535 211 AKVIKKVNDQTEAKTVLLDELR 232
Cdd:COG2171  245 AVIVKRRDEKTRSKTSLNELLR 266
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
104-222 3.08e-33

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.89  E-value: 3.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 104 IGDNAVIMMGAIINIG-AEIGAGTMIDMGAVL--GGRAIVGKHCHIGAGTVLAGV--------VEPPSAKPVTIGDHVMT 172
Cdd:COG0110   11 IGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGnhpiddpaTFPLRTGPVTIGDDVWI 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491949535 173 GANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTE 222
Cdd:COG0110   91 GAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 92-210 1.31e-31

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 114.50  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  92 IEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGvveppsakPVTIGDHVM 171
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAF 158

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491949535 172 TGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVP 210
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 92-211 1.38e-31

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 114.51  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535   92 IEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGvveppsakPVTIGDHVM 171
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVF 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 491949535  172 TGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPA 211
Cdd:TIGR03570 162 IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
DapH_N pfam08503
Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus ...
 5-84 1.52e-30

Tetrahydrodipicolinate succinyltransferase N-terminal; This domain is found at the N-terminus of tetrahydrodipicolinate N-succinyltransferase (DapH) which catalyzes the acylation of L-2-amino-6-oxopimelate to 2-N-succinyl-6-oxopimelate in the meso-diaminopimelate/lysine biosynthetic pathway of bacteria, blue-green algae, and plants. The N-terminal domain as defined here contains three alpha-helices and two twisted hairpin loops.


Pssm-ID: 430036  Cd Length: 83  Bit Score: 108.02  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535    5 DTEKIISTIANSKKTTPVKVYLKGKLADLHFP-KSVHAFIGKHTGTVIGDWTEIQPVLK--TAKLDDYYVEAAGRNTGVP 81
Cdd:pfam08503   1 DAYEIIKYIKNAKKKTPVKVYVKGDLLGEDLEfEEIKVFGSGDFGVLFGDWKEIKPFLEanKDKIEDYHIENDRRNSAIP 80


                  ...
gi 491949535   82 LLD 84
Cdd:pfam08503  81 LLD 83
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 116-216 1.42e-27

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 103.24  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:COG1045   68 IHPGATIGRGFFIDhgTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGAN 147

                         90       100
                 ....*....|....*....|...
gi 491949535 194 AVVINDVPAHTVVAGVPAKVIKK 216
Cdd:COG1045  148 SVVLKDVPPGSTVVGVPARIVKR 170
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 104-215 2.15e-25

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 96.03  E-value: 2.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 104 IGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSA-------KPVTIGDHVMTGANA 176
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKiyrkwelKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491949535 177 VVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIK 215
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 121-214 7.33e-25

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 94.45  E-value: 7.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 121 EIGAGTMIDMGAVLGGRA--IVGKHCHIGAGTVLAGV-----------VEPPSAKPVTIGDHVMTGANAVVLEGVTVGEG 187
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVTIYDHnhdiddperpiEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 491949535 188 AVIAAGAVVINDVPAHTVVAGVPAKVI 214
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 121-216 9.46e-25

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 95.30  E-value: 9.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 121 EIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVL--------------------------AGVVEPPSAKPVTIGDHVMT 172
Cdd:cd03349    3 SVGDYSYGSgpDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypfyifggeweddAKFDDWPSKGDVIIGNDVWI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491949535 173 GANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKK 216
Cdd:cd03349   83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 117-214 1.56e-24

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 95.18  E-value: 1.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 117 NIgaEIGAGTMIDMGAVL--GGRAIVGKHCHIGAGTVLAGV---VEPPS-------AKPVTIGDHVMTGANAVVLEGVTV 184
Cdd:cd03357   62 NI--HIGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIYTAghpLDPEErnrgleyAKPITIGDNVWIGGGVIILPGVTI 139

                         90       100       110
                 ....*....|....*....|....*....|
gi 491949535 185 GEGAVIAAGAVVINDVPAHTVVAGVPAKVI 214
Cdd:cd03357  140 GDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 116-210 1.46e-22

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 88.27  E-value: 1.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:cd03354    5 IHPGAKIGPGLFIDhgTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGAN 84

                         90
                 ....*....|....*..
gi 491949535 194 AVVINDVPAHTVVAGVP 210
Cdd:cd03354   85 AVVTKDVPANSTVVGVP 101
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 110-212 3.06e-22

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 89.27  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  110 IMMGAIINIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEG 187
Cdd:TIGR01172  58 VLTGVDIHPGARIGRGVFIDhgTGVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGEN 137

                          90       100
                  ....*....|....*....|....*
gi 491949535  188 AVIAAGAVVINDVPAHTVVAGVPAK 212
Cdd:TIGR01172 138 AKIGANSVVLKDVPPGATVVGVPAR 162
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 89-220 3.94e-21

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 86.23  E-value: 3.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIIN-----IgaEIGAGTMIDMGAVL----GGRAIVGKHCHIGAGTVLAGVvepp 159
Cdd:COG0663   16 SAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvgpI--RIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGAILHGC---- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491949535 160 sakpvTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVIND--VPAHTVVAGVPAKVIKKVNDQ 220
Cdd:COG0663   90 -----TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEE 147
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 89-220 2.54e-20

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 83.62  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAII-----NIgaEIGAGTMIDMGAVL----GGRAIVGKHCHIGAGTVLAGVvepp 159
Cdd:cd04645    5 SAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnPI--RIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGC---- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491949535 160 sakpvTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVIND--VPAHTVVAGVPAKVIKKVNDQ 220
Cdd:cd04645   79 -----TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDE 136
PLN02739 PLN02739
serine acetyltransferase
 111-234 8.70e-20

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 86.63  E-value: 8.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 111 MMGAIINIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGA 188
Cdd:PLN02739 203 VFGIDIHPAARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGA 282

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491949535 189 VIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTEAKTVLLDELRKL 234
Cdd:PLN02739 283 MVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYDATREF 328
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 161-217 6.08e-18

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 78.32  E-value: 6.08e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491949535 161 AKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKV 217
Cdd:PRK10092 127 GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 89-212 5.45e-17

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 76.29  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAII------------------NIGA-------EIGAGTMIDMGAVlgGRAIVGKH 143
Cdd:cd03352   43 DCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgggwvkipQLGGviigddvEIGANTTIDRGAL--GDTVIGDG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 144 ------------CHIGAGTVLAGVVEppSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPA 211
Cdd:cd03352  121 tkidnlvqiahnVRIGENCLIAAQVG--IAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPA 198


                 .
gi 491949535 212 K 212
Cdd:cd03352  199 Q 199
cysE PRK11132
serine acetyltransferase; Provisional
 116-216 1.33e-15

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 73.96  E-value: 1.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:PRK11132 144 IHPAAKIGRGIMLDhaTGIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223

                         90       100
                 ....*....|....*....|...
gi 491949535 194 AVVINDVPAHTVVAGVPAKVIKK 216
Cdd:PRK11132 224 SVVLQPVPPHTTAAGVPARIVGK 246
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 163-220 1.86e-15

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 72.34  E-value: 1.86e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535 163 PVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQ 220
Cdd:PRK09527 131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDR 188
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 104-214 2.40e-15

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 69.56  E-value: 2.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 104 IGDNAVIMMGAIINIGAEIgagtmidmgaVLGGRAIVGKHCHIGAGT-----VLAGVVeppsAKPVTIGDHVMTGANAVV 178
Cdd:cd05825    6 IGDNSWIGEGVWIYNLAPV----------TIGSDACISQGAYLCTGShdyrsPAFPLI----TAPIVIGDGAWVAAEAFV 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491949535 179 LEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVI 214
Cdd:cd05825   72 GPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PLN02357 PLN02357
serine acetyltransferase
 116-214 1.43e-14

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 71.84  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:PLN02357 229 IHPGAKIGQGILLDhaTGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAG 308

                         90       100
                 ....*....|....*....|.
gi 491949535 194 AVVINDVPAHTVVAGVPAKVI 214
Cdd:PLN02357 309 SVVLKDVPPRTTAVGNPARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 116-214 1.53e-14

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 71.21  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMID--MGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:PLN02694 163 IHPAAKIGKGILFDhaTGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAG 242

                         90       100
                 ....*....|....*....|.
gi 491949535 194 AVVINDVPAHTVVAGVPAKVI 214
Cdd:PLN02694 243 SVVLIDVPPRTTAVGNPARLV 263
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 89-212 2.47e-14

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 70.82  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLA----GVVEPPSAKP- 163
Cdd:COG1044  114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGadgfGFAPDEDGGWv 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 164 -------VTIGDHVMTGANA---------------------------------------------------VVLEG---- 181
Cdd:COG1044  194 kipqlgrVVIGDDVEIGANTtidrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgiagstkigdnVVIGGqvgi 273

                        170       180       190
                 ....*....|....*....|....*....|....
gi 491949535 182 ---VTVGEGAVIAAGAVVINDVPAHTVVAGVPAK 212
Cdd:COG1044  274 aghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 120-196 2.82e-14

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 65.73  E-value: 2.82e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949535 120 AEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 88-215 3.39e-14

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 70.83  E-value: 3.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  88 TNARIEPGAIIRDqVLIGDNAVIMMGAIIniGAEIGAGTMID------MGAVLG-------------------------- 135
Cdd:COG1207  289 EGVVIGPNCTLKD-STIGDGVVIKYSVIE--DAVVGAGATVGpfarlrPGTVLGegvkignfvevknstigegskvnhls 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 136 --GRAIVGKHCHIGAGTVLA---GVveppsAK-PVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHT-VVAG 208
Cdd:COG1207  366 yiGDAEIGEGVNIGAGTITCnydGV-----NKhRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGAlAIAR 440


                 ....*..
gi 491949535 209 VPAKVIK 215
Cdd:COG1207  441 ARQRNIE 447
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 89-213 5.83e-14

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 68.89  E-value: 5.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGG------------RAIVGKH------------- 143
Cdd:COG1043   19 NVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEepqdlkykgeptRLEIGDNntirefvtihrgt 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 144 ------------------------CHIGAGTV------LAGvveppsakPVTIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:COG1043   99 vqgggvtrigddnllmayvhvahdCVVGNNVIlannatLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGG 170

                        170       180
                 ....*....|....*....|
gi 491949535 194 AVVINDVPAHTVVAGVPAKV 213
Cdd:COG1043  171 SGVVKDVPPYVLAAGNPARL 190
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-216 6.27e-14

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 70.34  E-value: 6.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVImmGAIINI-GAEIGAGTMIDMGAVLGGrAIVGKHCHIGAGTVLA---GVveppSAKPV 164
Cdd:PRK14360 319 GVKIGPYAHLRPEAQIGSNCRI--GNFVEIkKSQLGEGSKVNHLSYIGD-ATLGEQVNIGAGTITAnydGV----KKHRT 391

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491949535 165 TIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKK 216
Cdd:PRK14360 392 VIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 89-233 9.61e-14

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 69.01  E-value: 9.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAII------------------NIGA-------EIGAGTMIDMGAVlgGRAIVGK- 142
Cdd:PRK00892 154 DCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandrggwvkipQLGRviigddvEIGANTTIDRGAL--DDTVIGEg 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 143 -----------HCHIGAGTVLAGVVepPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAH-TVVAGVP 210
Cdd:PRK00892 232 vkidnlvqiahNVVIGRHTAIAAQV--GIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPgEYSSGIP 309

                        170       180
                 ....*....|....*....|...
gi 491949535 211 AKVIKKVNDQTeAKTVLLDELRK 233
Cdd:PRK00892 310 AQPNKEWLRTA-ARLRRLDELRK 331
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 92-220 2.50e-13

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 65.47  E-value: 2.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  92 IEPGAIIRDQVLIGDNAVIMMGAII--NIGA-EIGAGTMIDMGAVLGGR----AIVGKHCHIGAGTVLAGVveppsakpv 164
Cdd:cd04745    9 VHPTAVLIGDVIIGKNCYIGPHASLrgDFGRiVIRDGANVQDNCVIHGFpgqdTVLEENGHIGHGAILHGC--------- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535 165 TIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVIN--DVPAHTVVAGVPAKVIKKVNDQ 220
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSDE 137
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 158-222 5.03e-13

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 65.28  E-value: 5.03e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491949535 158 PPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKKVNDQTE 222
Cdd:PRK09677 125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETK 189
PRK10502 PRK10502
putative acyl transferase; Provisional
 90-215 7.19e-13

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 64.59  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQV--------LIGDNAVIMMGAIINIGAEIgagtmidmgavlggraIVGKHCHIGAGTVLAGVVEPPS- 160
Cdd:PRK10502  52 AKIGKGVVIRPSVritypwklTIGDYAWIGDDVWLYNLGEI----------------TIGAHCVISQKSYLCTGSHDYSd 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491949535 161 ------AKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIK 215
Cdd:PRK10502 116 phfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 89-213 1.08e-12

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 65.53  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGG-----------------------------RA- 138
Cdd:cd03351   17 NVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEapqdlkykgeptrleigdnntirefvtihRGt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 139 -------------------------IVGKHCHIGAGTVLAGVVEppsakpvtIGDHVMTGANAVVLEGVTVGEGAVIAAG 193
Cdd:cd03351   97 aqgggvtrignnnllmayvhvahdcVIGNNVILANNATLAGHVE--------IGDYAIIGGLSAVHQFCRIGRHAMVGGG 168

                        170       180
                 ....*....|....*....|
gi 491949535 194 AVVINDVPAHTVVAGVPAKV 213
Cdd:cd03351  169 SGVVQDVPPYVIAAGNRARL 188
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 89-206 3.92e-12

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 62.82  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVlIGDNAVIMM-----GAIINIGAEIG------AGTMIDMGAVLG---------------------- 135
Cdd:cd03353   39 DCVIGPNCVIKDST-IGDGVVIKAssvieGAVIGNGATVGpfahlrPGTVLGEGVHIGnfveikkstigegskanhlsyl 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491949535 136 GRAIVGKHCHIGAGTVLA---GVveppsAK-PVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVV 206
Cdd:cd03353  118 GDAEIGEGVNIGAGTITCnydGV-----NKhRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
89-213 7.66e-12

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 63.19  E-value: 7.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGG------------RAIVGKH------------- 143
Cdd:PRK05289  20 NVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEdpqdlkykgeptRLVIGDNntirefvtinrgt 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 144 ------------------------CHIGAGTVLAGVVepPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVIND 199
Cdd:PRK05289 100 vqgggvtrigdnnllmayvhvahdCVVGNHVILANNA--TLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQD 177

                        170
                 ....*....|....
gi 491949535 200 VPAHTVVAGVPAKV 213
Cdd:PRK05289 178 VPPYVLAEGNPARL 191
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 92-196 8.00e-12

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 63.62  E-value: 8.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  92 IEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVlggraiVGKHCHIGAGTVLagvveppsakpvtigdhvm 171
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAV------IGDGVKIGADCRL------------------- 157

                         90       100
                 ....*....|....*....|....*
gi 491949535 172 tGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:PRK00892 158 -HANVTIYHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 90-196 2.99e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 61.96  E-value: 2.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVlggraiVGKHCHIGAGTVLagvveppsakpvtigdh 169
Cdd:COG1044   97 PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV------IGDGVVIGDDCVL----------------- 153

                         90       100
                 ....*....|....*....|....*..
gi 491949535 170 vmtGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:COG1044  154 ---HPNVTIYERCVIGDRVIIHSGAVI 177
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 89-196 7.72e-11

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 58.75  E-value: 7.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGA------IINIGAEIGAGTMIDMGAVLG--------------------------- 135
Cdd:cd05636    5 EGTVEEGVTIKGPVWIGEGAIVRSGAyiegpvIIGKGCEIGPNAYIRGYTVLGdgcvvgnsvevknsiimdgtkvphlny 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535 136 -GRAIVGKHCHIGAGTVLAGVVEPPSAKPVT----------------IGDHVMTGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:cd05636   85 vGDSVLGENVNLGAGTITANLRFDDKPVKVRlkgervdtgrrklgaiIGDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 89-214 7.86e-11

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 59.97  E-value: 7.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535   89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGG------------RAIVGKHCHI---------- 146
Cdd:TIGR01852  16 NVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGvpqdlkykgektRLIIGDNNTIrefvtinrgt 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  147 --GAGTVLAG---------------VVE--------PPSAKPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVP 201
Cdd:TIGR01852  96 asGGGVTRIGnnnllmayshiahdcVVGnhvilannATLAGHVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVP 175

                         170
                  ....*....|...
gi 491949535  202 AHTVVAGVPAKVI 214
Cdd:TIGR01852 176 PYCLAEGNRARLR 188
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-205 2.00e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 59.74  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGdNAVIMMGAIINIGAEIGAGTMIdmgavlgGRAIVGKHCHIGAGTVLAGVVEPPSAKPVtIGDH 169
Cdd:PRK14356 334 ARLRPGAVLEEGARVG-NFVEMKKAVLGKGAKANHLTYL-------GDAEIGAGANIGAGTITCNYDGVNKHRTV-IGEG 404

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491949535 170 VMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTV 205
Cdd:PRK14356 405 AFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 64-214 3.76e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 59.18  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  64 AKLDDYYVEAAGRNtGVPLLDIKTT----------NARIEPGAIIRDQVLIGDNAVI---------------------MM 112
Cdd:PRK14352 243 AELNRRIVEAWMRA-GVTIVDPATTwidvdvtigrDVVIHPGTQLLGRTTIGEDAVVgpdttltdvtvgegasvvrthGS 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 113 GAIINIGAEIGAGTMIDMGAVLG----------------------------GRAIVGKHCHIGAGTVLA---GVveppSA 161
Cdd:PRK14352 322 ESEIGAGATVGPFTYLRPGTVLGeegklgafvetknatigrgtkvphltyvGDADIGEHSNIGASSVFVnydGV----NK 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491949535 162 KPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHT-VVAGVPAKVI 214
Cdd:PRK14352 398 HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGAlAVSEGPQRNI 451
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 122-222 5.69e-10

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 56.07  E-value: 5.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 122 IGAGTMIDMGAVLGG--RAI-VGKHCHIGAGTVlagvVEPPSAK--------PVTIGDHVM-----------------TG 173
Cdd:cd03359   24 LNGKTIIQSDVIIRGdlATVsIGRYCILSEGCV----IRPPFKKfskgvaffPLHIGDYVFigencvvnaaqigsyvhIG 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491949535 174 ANAVVLEGVTVGEGAVIAAGAVVIND--VPAHTVVAGVPAKVIKKVNDQTE 222
Cdd:cd03359  100 KNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPECTQ 150
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-203 5.80e-10

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 58.30  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGdNAVIMMGAIINIGAEIGAGTMIdmgavlgGRAIVGKHCHIGAGTVlagVVEPPSAK--PVTI 166
Cdd:PRK14354 328 FAHLRPGSVIGEEVKIG-NFVEIKKSTIGEGTKVSHLTYI-------GDAEVGENVNIGCGTI---TVNYDGKNkfKTII 396

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491949535 167 GDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAH 203
Cdd:PRK14354 397 GDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-215 1.00e-09

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 57.56  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGdNAVIMMGAIINIGAEIGAGTMIdmgavlgGRAIVGKHCHIGAGTVLA---GVveppsAKPVT- 165
Cdd:PRK14353 316 ARLRPGAELGEGAKVG-NFVEVKNAKLGEGAKVNHLTYI-------GDATIGAGANIGAGTITCnydGF-----NKHRTe 382

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491949535 166 IGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIK 215
Cdd:PRK14353 383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
PLN02296 PLN02296
carbonate dehydratase
 89-223 1.09e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 57.06  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAII-----NIgaEIGAGTMIDMGAVLggraivgkhcHIgAGTVLAGVVEPpsakp 163
Cdd:PLN02296  58 DAFVAPSASVIGDVQVGRGSSIWYGCVLrgdvnSI--SVGSGTNIQDNSLV----------HV-AKTNLSGKVLP----- 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491949535 164 VTIGDHVMTGANAV-----------------VLEGVTVGEGAVIAAGAVVIND--VPAHTVVAGVPAKVIKKVNDQTEA 223
Cdd:PLN02296 120 TIIGDNVTIGHSAVlhgctvedeafvgmgatLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTEEEIA 198
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 50-206 6.80e-09

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 55.42  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  50 VIGDWTEIQP--VLKTAKLDdyyvEAAgrnTGVPLldikttnARIEPGAIIRDQVLIGdNAVIMMGAIINIGAEIGAGTM 127
Cdd:PRK09451 302 VIGDDCEISPysVVEDANLG----AAC---TIGPF-------ARLRPGAELAEGAHVG-NFVEMKKARLGKGSKAGHLTY 366

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491949535 128 IdmgavlgGRAIVGKHCHIGAGTVLAGVVEPPSAKPVtIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVV 206
Cdd:PRK09451 367 L-------GDAEIGDNVNIGAGTITCNYDGANKFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 128-200 3.40e-08

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.83  E-value: 3.40e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949535 128 IDMGAVLGGRAIVGKHCHIGAGTVL-AGVVeppsakpvtIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDV 200
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIgAGVV---------IGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 88-213 5.63e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 51.95  E-value: 5.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  88 TNARIEPGAIIRD------------QVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVL------GGRAIVGKHCHIGAG 149
Cdd:PRK12461  52 KNNKIHQGAVVGDepqdftykgeesRLEIGDRNVIREGVTIHRGTKGGGVTRIGNDNLLmayshvAHDCQIGNNVILVNG 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949535 150 TVLAGvveppsakPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKV 213
Cdd:PRK12461 132 ALLAG--------HVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNV 187
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 92-220 6.07e-08

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 51.35  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  92 IEPGAIIR-DQVLIGDnavIMMGAIINIGAE-----------IGAGTMIDMGAVLGGRA----IVGKHCHIGAGTVLAGV 155
Cdd:PRK13627  13 VHPTAFVHpSAVLIGD---VIVGAGVYIGPLaslrgdygrliVQAGANLQDGCIMHGYCdtdtIVGENGHIGHGAILHGC 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949535 156 VeppsakpvtIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDV--PAHTVVAGVPAKVIKKVNDQ 220
Cdd:PRK13627  90 V---------IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVSDD 147
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-216 6.24e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.46  E-value: 6.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  95 GAIIRDQVLIGDNAVIMMGAIINIGAEIG-----AGTMIDMGA-----VLGGRAIVGKHCHIGAGTVLAGVvEPPSAKPV 164
Cdd:PRK14357 306 KSVIEDDVSVGPFSRLREGTVLKKSVKIGnfveiKKSTIGENTkaqhlTYLGDATVGKNVNIGAGTITCNY-DGKKKNPT 384

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491949535 165 TIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVPAHTVVAGVPAKVIKK 216
Cdd:PRK14357 385 FIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 90-220 8.77e-08

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 49.88  E-value: 8.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGDNAVIMMGAI-------INIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVveppsak 162
Cdd:cd04650    7 AYVHPTSYVIGDVVIGELTSVWHYAVirgdndsIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGA------- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 163 pvTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVI--NDVPAHTVVAGVPAKVIKKVNDQ 220
Cdd:cd04650   80 --KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEE 137
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 91-187 4.51e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 49.25  E-value: 4.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  91 RIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGvvEPPSAKPVTIGDHV 170
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGD--EPQDFTYKGEESRL 78

                         90
                 ....*....|....*..
gi 491949535 171 MTGANAVVLEGVTVGEG 187
Cdd:PRK12461  79 EIGDRNVIREGVTIHRG 95
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 47-201 8.90e-07

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 49.21  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  47 TGTVIGDWTEIQP--VLKTAKLddyyveAAGRNTGvPLldikttnARIEPGAIIRDQVLIGdNAVIMMGAIINIGaeIGA 124
Cdd:PRK14358 304 TDSVLHEGAVIKPhsVLEGAEV------GAGSDVG-PF-------ARLRPGTVLGEGVHIG-NFVETKNARLDAG--VKA 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 125 GTMIDMGAVlggraIVGKHCHIGAGTVLA---GVVEPPSakpvTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDVP 201
Cdd:PRK14358 367 GHLAYLGDV-----TIGAETNVGAGTIVAnfdGVNKHQS----KVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVP 437
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 88-202 2.93e-06

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 46.08  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  88 TNARIEPGAIIRDQVLIGDNAVIMMGAIIN----IGAEIGAGTMIDMGAVL----GGRAIVGKHCHIGAGTVLAGvvepp 159
Cdd:cd00710    7 PSAYVHPTAVVIGDVIIGDNVFVGPGASIRadegTPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHG----- 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491949535 160 sakPVTIGDHVMTGANAVVLEGvTVGEGAVIAAGAVVIN-DVPA 202
Cdd:cd00710   82 ---PAYIGDNCFIGFRSVVFNA-KVGDNCVIGHNAVVDGvEIPP 121
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 118-211 3.29e-06

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 47.44  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  118 IGAEIGAGTMIDmGAVLGGRAIV--GKHCHIGAGTVLA------GVVeppSAKPVTIGDHVMTGANAVVLEGVTVGEGAV 189
Cdd:TIGR02353 596 LGVKIGRGVYID-GTDLTERDLVtiGDDSTLNEGSVIQthlfedRVM---KSDTVTIGDGATLGPGAIVLYGVVMGEGSV 671

                          90       100
                  ....*....|....*....|....
gi 491949535  190 IAAGAVVI--NDVPAHTVVAGVPA 211
Cdd:TIGR02353 672 LGPDSLVMkgEEVPAHTRWRGNPA 695
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 116-196 5.56e-06

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 46.56  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLagvveppsaKPVTIGDhvmtgaNAVVLEgvTVGEGAVIAAGAV 195
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL---------KDSTIGD------GVVIKY--SVIEDAVVGAGAT 325


                 .
gi 491949535 196 V 196
Cdd:COG1207  326 V 326
LbH_THP_succinylT_putative cd04649
Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP ...
 89-196 8.98e-06

Putative 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (THP succinyltransferase), C-terminal left-handed parallel alpha-helix (LbH) domain: This group is composed of mostly uncharacterized proteins containing an N-terminal domain of unknown function and a C-terminal LbH domain with similarity to THP succinyltransferase LbH. THP succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is trimeric and displays the left-handed parallel alpha-helix (LbH) structural motif encoded by the hexapeptide repeat motif.


Pssm-ID: 100054  Cd Length: 147  Bit Score: 44.33  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDmGAVLGGrAIVGKHCHIGAGTVLAGVVEPPSAKPVTIGD 168
Cdd:cd04649    1 GVRIADADRVRLGAYLAEGTTVMHEGFVNFNAGTLGNCMVE-GRISSG-VIVGKGSDVGGGASIMGTLSGGGNNVISIGK 78

                         90       100
                 ....*....|....*....|....*...
gi 491949535 169 HVMTGANAVVleGVTVGEGAVIAAGAVV 196
Cdd:cd04649   79 RCLLGANSGI--GISLGDNCIVEAGLYV 104
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 88-170 2.30e-05

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 44.68  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  88 TNARIEPGAIIRDqvligdnaVIMMGaiiniGAEIGAGTMIDmgavlggRAIVGKHCHIGAGTVLaGVVEPPSAKPVTIG 167
Cdd:COG0448  308 RGVRVESGAVVEN--------SVIMP-----GVVIGEGAVIE-------NAIIDKNVVIPPGVVI-GEDPEEDRKRFTVS 366


                 ...
gi 491949535 168 DHV 170
Cdd:COG0448  367 SGI 369
PRK10191 PRK10191
putative acyl transferase; Provisional
 111-213 2.76e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 42.95  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 111 MMGAIINIGAEIGAGTMIDMG--AVLGGRAIVGKHCHIGAGTVLAGVVEPPSAKPVtIGDHVMTGANAVVLEGVTVGEGA 188
Cdd:PRK10191  39 FFGYEIQAAATIGRRFTIHHGyaVVINKNVVAGDDFTIRHGVTIGNRGADNMACPH-IGNGVELGANVIILGDITIGNNV 117

                         90       100
                 ....*....|....*....|....*
gi 491949535 189 VIAAGAVVINDVPAHTVVAGVPAKV 213
Cdd:PRK10191 118 TVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-202 2.98e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGdNAVIMMGAIINIGAEIGAGTMIdmgavlgGRAIVGKHCHIGAGTVLAGVVEPPSAKPVtIGDH 169
Cdd:PRK14355 333 AHLRPGTELSAHVKIG-NFVETKKIVMGEGSKASHLTYL-------GDATIGRNVNIGCGTITCNYDGVKKHRTV-IEDD 403

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491949535 170 VMTGANAVVLEGVTVGEGAVIAAGAVVINDVPA 202
Cdd:PRK14355 404 VFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPP 436
PLN02472 PLN02472
uncharacterized protein
 102-234 1.84e-04

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 41.49  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 102 VLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLagvveppsaKPVTIGDHVMTGANAVVLEG 181
Cdd:PLN02472  91 VLRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPAETLIDRYVTIGAYSLL---------RSCTIEPECIIGQHSILMEG 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491949535 182 VTVGEGAVIAAGAVVI--NDVPAHTVVAGVPAKVIKKV-NDQTEAKTVLLDELRKL 234
Cdd:PLN02472 162 SLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLtNEETLEIPKLAVAINDL 217
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 126-196 3.25e-04

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.77  E-value: 3.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491949535 126 TMIDMGAVLGGRAIVGKHCHIGAGTvlagVVEPpsakPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:COG1043    2 AMIHPTAIVDPGAKLGENVEIGPFC----VIGP----DVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
163-192 5.35e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 5.35e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 491949535  163 PVTIGDHVMTGANAVVLEGVTVGEGAVIAA 192
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 159-200 1.02e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 39.62  E-value: 1.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 491949535 159 PSAKpvtIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDV 200
Cdd:COG1044  107 PSAK---IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 121-212 1.07e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 39.73  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  121 EIGAGTMIDMGAVLGGRAIVGKHCHIGagtvlagvveppsakPVTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVIND- 199
Cdd:TIGR02353 133 TIGAGTIVRKEVMLLGYRAERGRLHTG---------------PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGq 197

                          90
                  ....*....|....
gi 491949535  200 -VPAHTVVAGVPAK 212
Cdd:TIGR02353 198 sIPDGERWHGSPAQ 211
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 164-200 1.23e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.54  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 491949535 164 VTIGDHVMTGANAVVLEGVTVGEGAVIAAGAVVINDV 200
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-190 1.35e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  90 ARIEPGAIIRDQVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLAGVVeppsakpvtIGDH 169
Cdd:PRK14355 239 ARVLRRRINRELMLAGVTLIDPETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCR---------IGDD 309

                         90       100
                 ....*....|....*....|.
gi 491949535 170 VMTGANAvVLEGVTVGEGAVI 190
Cdd:PRK14355 310 VTVKAGS-VLEDSVVGDDVAI 329
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
164-196 1.40e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 35.11  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 491949535  164 VTIGDHVMTGANAVVleGVTVGEGAVIAAGAVV 196
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 89-150 1.81e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.87  E-value: 1.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949535  89 NARIEPGAIIRDQVLIGDNAVIMMGAII----------NIGAEIGAGTMIDM------GAVlgGRAIVGKHCHIGAGT 150
Cdd:cd05635   17 DAVIEPFAVIEGPVYIGPGSRVKMGARIygnttigptcKIGGEVEDSIIEGYsnkqhdGFL--GHSYLGSWCNLGAGT 92
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
119-148 2.98e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 491949535  119 GAEIGAGTMIDMGAVLGGRAIVGKHCHIGA 148
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-200 3.63e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.89  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 116 INIGAEIGAGTMIDMGAVLGGRAIVGKHCHIGAGTVLagvveppsaKPVTIGDHVmTGANAVVLE-----GVTVGEGAVI 190
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI---------VDSTIGDGV-TITNSVIEEskvgdNVTVGPFAHL 331

                         90
                 ....*....|
gi 491949535 191 AAGAVVINDV 200
Cdd:PRK14354 332 RPGSVIGEEV 341
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 88-190 3.76e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 35.90  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  88 TNARIEPGAIIRDQVLIGDnavimmgaiinigAEIGAGTMIDmgavlggRAIVGKHCHIGAGTVLAGVVEPPSAKPVTIG 167
Cdd:cd04651   33 RGVRVGSGSVVEDSVIMPN-------------VGIGRNAVIR-------RAIIDKNVVIPDGVVIGGDPEEDRARFYVTE 92

                         90       100
                 ....*....|....*....|...
gi 491949535 168 DHVmtganavvlegVTVGEGAVI 190
Cdd:cd04651   93 DGI-----------VVVGKGMVI 104
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 89-186 4.05e-03

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 36.83  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  89 NARIEPGAIIRD----QVLIGDNAVIMMGAIINIGAEIGAGTMIDMGAVLgGRAIVGKHCHIGAGTVLAGvVEPPSAKPV 164
Cdd:cd00710   48 NVNIQDGVVIHAlegySVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVV-FNAKVGDNCVIGHNAVVDG-VEIPPGRYV 125

                         90       100
                 ....*....|....*....|..
gi 491949535 165 TIGDHVMTGANAVVLEGVTVGE 186
Cdd:cd00710  126 PAGAVITSQTQADALPDVTDSA 147
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 91-190 5.29e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 37.56  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535  91 RIEPGAIIRDqvligdnaVIMMGA----------------IINIGaeIGAGTMIDmgavlggRAIVGKHCHIGAGTVLAG 154
Cdd:PRK02862 332 RIESGCTIED--------TLVMGAdfyesseereelrkegKPPLG--IGEGTTIK-------RAIIDKNARIGNNVRIVN 394

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491949535 155 VVEPPSAKPVTIGDHVMTGAnAVVLEGVTVGEGAVI 190
Cdd:PRK02862 395 KDNVEEADREDQGFYIRDGI-VVVVKNAVIPDGTVI 429
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 122-196 6.36e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.48  E-value: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949535 122 IGAGTMIDMGAVLGGrAIVGKHCHIGAGTVLAGVVeppSAKPVTIGD-----HVMTGANAVVLEGVTVGEGAVIAAGAVV 196
Cdd:cd05787    2 IGRGTSIGEGTTIKN-SVIGRNCKIGKNVVIDNSY---IWDDVTIEDgctihHSIVADGAVIGKGCTIPPGSLISFGVVI 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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