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Conserved domains on  [gi|312985388|gb|ADR30837|]
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phosphoglucomutase, partial [Oenococcus oeni]

Protein Classification

phosphohexomutase domain-containing protein( domain architecture ID 1562470)

phosphohexomutase domain-containing protein catalyzes catalyzes the reversible conversion of 1-phospho to 6-phosphohexose, with various sugars including glucose, mannose, glucosamine, and N-acetylglucosamine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
phosphohexomutase super family cl38939
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 2-176 3.61e-75

The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


The actual alignment was detected with superfamily member cd05799:

Pssm-ID: 476822  Cd Length: 487  Bit Score: 232.78  E-value: 3.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   2 PHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHIKKVA----GGIKKIG 77
Cdd:cd05799   82 LRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEaldsGLIKYIG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  78 SEIDKEYLNQVKTIPINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEQFKPDGTFPTVKYPNPEFHE 157
Cdd:cd05799  162 EEIDDAYLEAVKKLLVNPELNEG--KDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPG 239

                        170       180
                 ....*....|....*....|...
gi 312985388 158 VFKIS----ESYGADVELAVDPD 176
Cdd:cd05799  240 ALDLAielaKKVGADLILATDPD 262
 
Name Accession Description Interval E-value
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 2-176 3.61e-75

This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100092  Cd Length: 487  Bit Score: 232.78  E-value: 3.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   2 PHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHIKKVA----GGIKKIG 77
Cdd:cd05799   82 LRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEaldsGLIKYIG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  78 SEIDKEYLNQVKTIPINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEQFKPDGTFPTVKYPNPEFHE 157
Cdd:cd05799  162 EEIDDAYLEAVKKLLVNPELNEG--KDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPG 239

                        170       180
                 ....*....|....*....|...
gi 312985388 158 VFKIS----ESYGADVELAVDPD 176
Cdd:cd05799  240 ALDLAielaKKVGADLILATDPD 262
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
1-176 2.22e-41

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 144.19  E-value: 2.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVtDIFHIKKVAGGIKKIGSEI 80
Cdd:COG1109   76 GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE-DFRRAEAEEIGKVTRIEDV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  81 DKEYLNQVKTIpINRDLIKKwgdKLTISFTPLYGAGGDLGSKALKEAGFnKILTVKEQfkPDGTFPTVkYPNPE---FHE 157
Cdd:COG1109  155 LEAYIEALKSL-VDEALRLR---GLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNH-NPNPEpenLED 226

                        170
                 ....*....|....*....
gi 312985388 158 VFKISESYGADVELAVDPD 176
Cdd:COG1109  227 LIEAVKETGADLGIAFDGD 245
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 4-176 1.28e-33

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 124.80  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQL-PP---KPADEIVRERQ---EVTDIFHikkvAGGIKKI 76
Cdd:PTZ00150 128 PTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIiPPhdkNISAKILSNLEpwsSSWEYLT----ETLVEDP 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  77 GSEIDKEYLNQVKTI--PINRDlikkwGDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEQFKPDGTFPTVKYPNPE 154
Cdd:PTZ00150 204 LAEVSDAYFATLKSEynPACCD-----RSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPE 278

                        170       180
                 ....*....|....*....|....*..
gi 312985388 155 -----FHEVFKISESYGADVELAVDPD 176
Cdd:PTZ00150 279 egkgaLKLSMETAEAHGSTVVLANDPD 305
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
1-53 1.03e-21

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 85.35  E-value: 1.03e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312985388    1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEI 53
Cdd:pfam02878  75 GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKI 127
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 4-176 1.65e-21

phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]


Pssm-ID: 274906  Cd Length: 443  Bit Score: 89.88  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388    4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVR----ERQEVTDIFHIKKVaggikKIGSE 79
Cdd:TIGR03990  73 PTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEiaesGDFERADWDEIGTV-----TSDED 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   80 IDKEYLNQVKTIpINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGfNKILTVKEQfkPDGTFPT-VKYPNPE-FHE 157
Cdd:TIGR03990 148 AIDDYIEAILDK-VDVEAIRK--KGFKVVVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFPGrNPEPTPEnLKD 221

                         170
                  ....*....|....*....
gi 312985388  158 VFKISESYGADVELAVDPD 176
Cdd:TIGR03990 222 LSALVKATGADLGIAHDGD 240
 
Name Accession Description Interval E-value
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 2-176 3.61e-75

This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100092  Cd Length: 487  Bit Score: 232.78  E-value: 3.61e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   2 PHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHIKKVA----GGIKKIG 77
Cdd:cd05799   82 LRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEaldsGLIKYIG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  78 SEIDKEYLNQVKTIPINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEQFKPDGTFPTVKYPNPEFHE 157
Cdd:cd05799  162 EEIDDAYLEAVKKLLVNPELNEG--KDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPG 239

                        170       180
                 ....*....|....*....|...
gi 312985388 158 VFKIS----ESYGADVELAVDPD 176
Cdd:cd05799  240 ALDLAielaKKVGADLILATDPD 262
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
1-176 2.22e-41

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 144.19  E-value: 2.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVtDIFHIKKVAGGIKKIGSEI 80
Cdd:COG1109   76 GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE-DFRRAEAEEIGKVTRIEDV 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  81 DKEYLNQVKTIpINRDLIKKwgdKLTISFTPLYGAGGDLGSKALKEAGFnKILTVKEQfkPDGTFPTVkYPNPE---FHE 157
Cdd:COG1109  155 LEAYIEALKSL-VDEALRLR---GLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNH-NPNPEpenLED 226

                        170
                 ....*....|....*....
gi 312985388 158 VFKISESYGADVELAVDPD 176
Cdd:COG1109  227 LIEAVKETGADLGIAFDGD 245
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 4-176 1.28e-33

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 124.80  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQL-PP---KPADEIVRERQ---EVTDIFHikkvAGGIKKI 76
Cdd:PTZ00150 128 PTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIiPPhdkNISAKILSNLEpwsSSWEYLT----ETLVEDP 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  77 GSEIDKEYLNQVKTI--PINRDlikkwGDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEQFKPDGTFPTVKYPNPE 154
Cdd:PTZ00150 204 LAEVSDAYFATLKSEynPACCD-----RSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPE 278

                        170       180
                 ....*....|....*....|....*..
gi 312985388 155 -----FHEVFKISESYGADVELAVDPD 176
Cdd:PTZ00150 279 egkgaLKLSMETAEAHGSTVVLANDPD 305
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 1-130 5.19e-23

This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.


Pssm-ID: 100093  Cd Length: 461  Bit Score: 94.54  E-value: 5.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHIKKVAGGIKKIgsEI 80
Cdd:cd05800   75 RPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETI--DP 152

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 312985388  81 DKEYLNQVKTIpINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFN 130
Cdd:cd05800  153 KPDYLEALRSL-VDLEAIRE--AGLKVVVDPMYGAGAGYLEELLRGAGVD 199
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
1-53 1.03e-21

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 85.35  E-value: 1.03e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312985388    1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEI 53
Cdd:pfam02878  75 GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKI 127
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 4-176 1.65e-21

phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]


Pssm-ID: 274906  Cd Length: 443  Bit Score: 89.88  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388    4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVR----ERQEVTDIFHIKKVaggikKIGSE 79
Cdd:TIGR03990  73 PTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEiaesGDFERADWDEIGTV-----TSDED 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   80 IDKEYLNQVKTIpINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGfNKILTVKEQfkPDGTFPT-VKYPNPE-FHE 157
Cdd:TIGR03990 148 AIDDYIEAILDK-VDVEAIRK--KGFKVVVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFPGrNPEPTPEnLKD 221

                         170
                  ....*....|....*....
gi 312985388  158 VFKISESYGADVELAVDPD 176
Cdd:TIGR03990 222 LSALVKATGADLGIAHDGD 240
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 4-177 1.46e-19

This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100096  Cd Length: 445  Bit Score: 84.67  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHIKKVAGGIKKIGSEIdKE 83
Cdd:cd05803   75 PTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAI-AE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  84 YLNQV-KTIPINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEqfkPDGTFPTVKYPNPE-FHEVFKI 161
Cdd:cd05803  154 HIDKVlALVDVDVIKIRE--RNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCE---PTGLFPHTPEPLPEnLTQLCAA 228

                        170
                 ....*....|....*.
gi 312985388 162 SESYGADVELAVDPDS 177
Cdd:cd05803  229 VKESGADVGFAVDPDA 244
PGM_PMM_II pfam02879
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
83-176 7.84e-19

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;


Pssm-ID: 427033  Cd Length: 102  Bit Score: 76.95  E-value: 7.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   83 EYLNQVKTIPinrDLIKKWGDKLTISFTPLYGAGGDLGSKALKEAGFNkilTVKEQFKPDGTFPTvKYPNPEFHEVFKIS 162
Cdd:pfam02879   1 AYIDHLLELV---DSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCD---VVEENCEPDPDFPT-RAPNPEEPEALALL 73

                          90
                  ....*....|....*...
gi 312985388  163 ----ESYGADVELAVDPD 176
Cdd:pfam02879  74 ielvKSVGADLGIATDGD 91
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 1-176 9.80e-19

The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100086 [Multi-domain]  Cd Length: 355  Bit Score: 81.63  E-value: 9.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHLH-TYAGIMITASHNSKEYNGYKLYGEDGGQLpPKPADEIVRERQEVTDIFhikkVAGGIKKIGSE 79
Cdd:cd03084   12 GDDITPETAVALGQAIgSTGGIMITASHNPPEDNGIKFVDPDGEPI-ASEEEKAIEDLAEKEDEP----SAVAYELGGSV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  80 ----IDKEYLNQVKTIpINRDLIKKwgDKLTISFTPLYGAGGDLGSKALKEAGFNKILTVKEqfkPDGTFPtVKYPNPEF 155
Cdd:cd03084   87 kavdILQRYFEALKKL-FDVAALSN--KKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCE---PDGNFG-NINPDPGS 159

                        170       180
                 ....*....|....*....|....*
gi 312985388 156 ----HEVFKISESYGADVELAVDPD 176
Cdd:cd03084  160 etnlKQLLAVVKAEKADFGVAFDGD 184
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 1-176 3.45e-17

This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100089  Cd Length: 439  Bit Score: 78.00  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHlHTYAGIMITASHNSKEYNGYKLYGEDGGQLPpkPADEIVRERQEVTDIFHIKK--VAGGIKKIGS 78
Cdd:cd03087   68 GIVPTPALQYAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFS--REQEEEIEEIIFSERFRRVAwdEVGSVRREDS 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  79 EIDkEYLNQV-KTIPInrdlikKWGDKLTISFTPLYGAGGDLGSKALKEAGfNKILTVKEQfkPDGTFPTVK-YPNPE-F 155
Cdd:cd03087  145 AID-EYIEAIlDKVDI------DGGKGLKVVVDCGNGAGSLTTPYLLRELG-CKVITLNAN--PDGFFPGRPpEPTPEnL 214

                        170       180
                 ....*....|....*....|.
gi 312985388 156 HEVFKISESYGADVELAVDPD 176
Cdd:cd03087  215 SELMELVRATGADLGIAHDGD 235
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 4-154 5.22e-16

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 74.47  E-value: 5.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   4 PTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLygedggQLPPKPADEivrerQEVTDIFHI--KKVAGGIKKIGSEID 81
Cdd:cd03089   74 PTPVLYFATFHLDADGGVMITASHNPPEYNGFKI------VIGGGPLSG-----EDIQALRERaeKGDFAAATGRGSVEK 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312985388  82 KEYLNQ-VKTIpinRDLIKKWGDKLTISFTPLYGAGGDLGSKALKEAGFnkilTVKEQFK-PDGTFPTvKYPNPE 154
Cdd:cd03089  143 VDILPDyIDRL---LSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGC----EVIPLFCePDGTFPN-HHPDPT 209
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 1-144 1.08e-12

GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100095  Cd Length: 434  Bit Score: 64.81  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIvrERQeVTDIFHIKKVAGGIKKIGSEI 80
Cdd:cd05802   72 GVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEI--EAL-IDKELELPPTGEKIGRVYRID 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312985388  81 D--KEYLNQVK-TIPiNRDLikkwgDKLTISFTPLYGAGGDLGSKALKEAGFNkilTVKEQFKPDGT 144
Cdd:cd05802  149 DarGRYIEFLKsTFP-KDLL-----SGLKIVLDCANGAAYKVAPEVFRELGAE---VIVINNAPDGL 206
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 1-53 2.04e-10

phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 130522  Cd Length: 443  Bit Score: 58.53  E-value: 2.04e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 312985388    1 GPHPTPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEI 53
Cdd:TIGR01455  73 GPLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAI 125
PRK15414 PRK15414
phosphomannomutase;
5-176 4.17e-08

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 51.48  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   5 TPELSFAVMHLHTYAGIMITASHNSKEYNGYKLYGEdGGQlpPKPADEIVRERQ---EVTDIFHIKKVA-GGIKKIG--- 77
Cdd:PRK15414  77 TEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRE-GAR--PISGDTGLRDVQrlaEANDFPPVDETKrGRYQQINlrd 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  78 SEIDK--EYLNQVKTIPinrdlikkwgdkLTISFTPLYGAGGDLgSKALkEAGFnKILTVKEQF-----KPDGTFPTvKY 150
Cdd:PRK15414 154 AYVDHlfGYINVKNLTP------------LKLVINSGNGAAGPV-VDAI-EARF-KALGAPVELikvhnTPDGNFPN-GI 217

                        170       180       190
                 ....*....|....*....|....*....|
gi 312985388 151 PNPEFHEVFKISES----YGADVELAVDPD 176
Cdd:PRK15414 218 PNPLLPECRDDTRNavikHGADMGIAFDGD 247
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 19-154 2.56e-07

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 49.28  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388  19 AGIMITASHNSKEYNGYKLYGEDGGQLPPKPADEIVRERQEVTDIFHikkvaGGIKKIGSEIDKEyLNQVKTIPIN---- 94
Cdd:PLN02371 170 APIMITASHLPYNRNGLKFFTKDGGLGKPDIKDILERAARIYKEWSD-----EGLLKSSSGASSV-VCRVDFMSTYakhl 243

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312985388  95 RDLIKKWGDKLTISFTPLY----------GAGGDLGSKALKEAGFNkilTVKEQF-KPDGTFPTvKYPNPE 154
Cdd:PLN02371 244 RDAIKEGVGHPTNYETPLEgfkivvdagnGAGGFFAEKVLEPLGAD---TSGSLFlEPDGMFPN-HIPNPE 310
glmM PRK10887
phosphoglucosamine mutase; Provisional
 1-53 2.41e-06

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 46.28  E-value: 2.41e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 312985388   1 GPHPTPelsfAVMHL----HTYAGIMITASHNSKEYNGYKLYGEDGGQLPpkpaDEI 53
Cdd:PRK10887  74 GPMPTP----AVAYLtrtlRAEAGIVISASHNPYYDNGIKFFSADGTKLP----DEV 122
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 20-47 1.33e-05

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 44.24  E-value: 1.33e-05
                         10        20
                 ....*....|....*....|....*...
gi 312985388  20 GIMITASHNSKEYNGYKLYGEDGGQLPP 47
Cdd:PLN02895  61 GLMITASHNPVSDNGVKIVDPSGGMLPQ 88
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 20-47 1.39e-05

PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100088  Cd Length: 513  Bit Score: 44.12  E-value: 1.39e-05
                         10        20
                 ....*....|....*....|....*...
gi 312985388  20 GIMITASHNSKEYNGYKLYGEDGGQLPP 47
Cdd:cd03086   38 GVMITASHNPVEDNGVKIVDPDGEMLEE 65
ManB cd03088
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ...
 1-42 2.26e-05

ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100090  Cd Length: 459  Bit Score: 43.73  E-value: 2.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 312985388   1 GPHPTPELSFAVMHlHTYAGIMITASHNSKEYNGYKLYGEDG 42
Cdd:cd03088   71 GAVPTPALALYAMK-RGAPAIMVTGSHIPADRNGLKFYRPDG 111
PRK07564 PRK07564
phosphoglucomutase; Validated
 4-118 1.25e-04

phosphoglucomutase; Validated


Pssm-ID: 236050  Cd Length: 543  Bit Score: 41.28  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   4 PTPELSFAV-----MHLHTYAGIMITASHNSKEYNGYKLYGEDGGqlppkPADEivrerqEVTD-IFHIKKV---AG--G 72
Cdd:PRK07564 117 PTPAVSHAIlkyngRGGGLADGIVITPSHNPPEDGGIKYNPPNGG-----PADT------DVTDaIEARANEllaYGlkG 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 312985388  73 IKKIGSE----------ID--KEYLNQVKTIpINRDLIKKWGdkLTISFTPLYGAGGD 118
Cdd:PRK07564 186 VKRIPLDralasmtvevIDpvADYVEDLENV-FDFDAIRKAG--LRLGVDPLGGATGP 240
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 19-45 3.22e-04

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 40.41  E-value: 3.22e-04
                         10        20
                 ....*....|....*....|....*..
gi 312985388  19 AGIMITASHNSKEYNGYKLYGEDGGQL 45
Cdd:PTZ00302  77 VGVMITASHNPIQDNGVKIIDPDGGML 103
PGM_like3 cd05801
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 1-116 1.23e-03

This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100094 [Multi-domain]  Cd Length: 522  Bit Score: 38.38  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312985388   1 GPHPTPELSFAVM---HLHTYA---GIMITASHNSKEYNGYKLYGEDGGqlppkPADeivrerqevTDIFH-IKKVAG-- 71
Cdd:cd05801   97 GYTPTPVISHAILtynRGRTEGladGIVITPSHNPPEDGGFKYNPPHGG-----PAD---------TDITRwIEKRANal 162

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312985388  72 ------GIKKIGSE------------IDKEYLNQVKTIpINRDLIKKWGDKLTISftPLYGAG 116
Cdd:cd05801  163 langlkGVKRIPLEaalasgythrhdFVTPYVADLGNV-IDMDAIRKSGLRLGVD--PLGGAS 222
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 5-37 1.41e-03

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 38.42  E-value: 1.41e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 312985388   5 TPELSFAVMHLHTyAGIMITASHNSKEYNGYKL 37
Cdd:PRK09542  74 TDQLYFASGLLDC-PGAMFTASHNPAAYNGIKL 105
 
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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