NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1511892312|gb|AYV33256|]
View 

isoleucine--tRNA ligase, partial [Lactiplantibacillus plantarum]

Protein Classification

isoleucine--tRNA ligase( domain architecture ID 1015576)

isoleucine--tRNA ligase catalyzes the attachment of isoleucine to tRNA(Ile)

CATH:  3.90.740.10
EC:  6.1.1.5
Gene Ontology:  GO:0004822|GO:0006428|GO:0000049|GO:0005524|GO:0002161|GO:0008270
SCOP:  4000856

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IleS super family cl33754
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 1-215 3.30e-127

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


The actual alignment was detected with superfamily member COG0060:

Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 380.97  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAED-GTAIMDEV 79
Cdd:COG0060   407 CKTPLIYRATPQWFISMDKLRDRALEAIEKVNWIPEWGEGRFGNMLENRPDWCISRQRYWGVPIPIWVCEDcGELHRTEE 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKD-LLPDGYTNEHSpNGTFTKETDIMDVWFDSGSSHQGVLAERSYLDYPADLYLEGSD 158
Cdd:COG0060   487 VIGSVAELLEEEGADAWFELDLHRpFLDETLKCPKC-GGTMRRVPDVLDVWFDSGSMHFAVLENREELHFPADFYLEGSD 565

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:COG0060   566 QTRGWFYSSLLTSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVIDKYG 622
 
Name Accession Description Interval E-value
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 1-215 3.30e-127

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 380.97  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAED-GTAIMDEV 79
Cdd:COG0060   407 CKTPLIYRATPQWFISMDKLRDRALEAIEKVNWIPEWGEGRFGNMLENRPDWCISRQRYWGVPIPIWVCEDcGELHRTEE 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKD-LLPDGYTNEHSpNGTFTKETDIMDVWFDSGSSHQGVLAERSYLDYPADLYLEGSD 158
Cdd:COG0060   487 VIGSVAELLEEEGADAWFELDLHRpFLDETLKCPKC-GGTMRRVPDVLDVWFDSGSMHFAVLENREELHFPADFYLEGSD 565

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:COG0060   566 QTRGWFYSSLLTSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVIDKYG 622
ileS TIGR00392
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ...
 1-215 5.67e-102

isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273054 [Multi-domain]  Cd Length: 861  Bit Score: 313.54  E-value: 5.67e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDEVT 80
Cdd:TIGR00392 412 TKTPVIYRATEQWFIKTKDIKDQMLEQIKKVNWVPEWGEGRFGNWLENRPDWCISRQRYWGIPIPIWYCEDTGEPIVVGS 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  81 INHVADLFGKYGSNVWFERDAKDLLPDGYTNEHSPnGTFTKETDIMDVWFDSGSSHQGVLAERSYLD-----YPADLYLE 155
Cdd:TIGR00392 492 IEELIELIELKGIDAWFEDLHRDFLDKITLKSGDG-GEYRRVPDVLDVWFDSGSMPYASIHYPFENEkfkevFPADFILE 570

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 156 GSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:TIGR00392 571 GSDQTRGWFYSSLAIGTALFGQAPYKNVITHGFTLDEKGRKMSKSLGNVVDPLKVINKYG 630
PLN02843 PLN02843
isoleucyl-tRNA synthetase
 1-211 3.29e-96

isoleucyl-tRNA synthetase


Pssm-ID: 215452 [Multi-domain]  Cd Length: 974  Bit Score: 300.53  E-value: 3.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFY-AEDGTAIMDEV 79
Cdd:PLN02843  418 TKKPTIFRATEQWFASVEGFRQAALDAIDKVKWIPAQGENRIRAMVSGRSDWCISRQRTWGVPIPVFYhVETKEPLMNEE 497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKDLLPDGYTNEHSpngTFTKETDIMDVWFDSGSSHQGVLAERSYLDYPADLYLEGSDQ 159
Cdd:PLN02843  498 TIAHVKSIVAQKGSDAWWYMDVEDLLPEKYRDKAS---DYEKGTDTMDVWFDSGSSWAGVLGSREGLSYPADLYLEGSDQ 574

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1511892312 160 YRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVI 211
Cdd:PLN02843  575 HRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVI 626
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 1-215 1.82e-85

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 264.27  E-value: 1.82e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAED-GTAIMDEV 79
Cdd:pfam00133 368 SGTPIIPRATPQWFVRMDELADQALEAVEKVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPAWVSKDtEEVVCRGE 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKDLLPDGytnehspNGTFTKETDIMDVWFDSGSSHQGVL------AERSYLDYPADLY 153
Cdd:pfam00133 448 LFELVAGRFEEEGSIKWLHREAKDKLGYG-------KGTLEQDEDVLDTWFSSGSWPFSTLgwpfvnTEEFKKFFPADML 520

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511892312 154 LEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:pfam00133 521 LEGSDQTRGWFYRMIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYG 582
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 4-215 4.49e-80

catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 242.52  E-value: 4.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   4 PIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDevtinh 83
Cdd:cd00818   144 PLIYRATPQWFIRVTKIKDRLLEANDKVNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPVWYCEDCGEVLV------ 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  84 vadlfgkygsnvwferdakdllpdgytnehspngtfTKETDIMDVWFDSGSSHQGVL-----AERSYLDYPADLYLEGSD 158
Cdd:cd00818   218 ------------------------------------RRVPDVLDVWFDSGSMPYAQLhypfeNEDFEELFPADFILEGSD 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00818   262 QTRGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYG 318
 
Name Accession Description Interval E-value
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
 1-215 3.30e-127

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 380.97  E-value: 3.30e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAED-GTAIMDEV 79
Cdd:COG0060   407 CKTPLIYRATPQWFISMDKLRDRALEAIEKVNWIPEWGEGRFGNMLENRPDWCISRQRYWGVPIPIWVCEDcGELHRTEE 486

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKD-LLPDGYTNEHSpNGTFTKETDIMDVWFDSGSSHQGVLAERSYLDYPADLYLEGSD 158
Cdd:COG0060   487 VIGSVAELLEEEGADAWFELDLHRpFLDETLKCPKC-GGTMRRVPDVLDVWFDSGSMHFAVLENREELHFPADFYLEGSD 565

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:COG0060   566 QTRGWFYSSLLTSTALFGRAPYKNVLTHGFVLDEDGRKMSKSLGNVVDPQEVIDKYG 622
ileS TIGR00392
isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ...
 1-215 5.67e-102

isoleucyl-tRNA synthetase; The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. This model may recognize IleS from every species, including eukaryotic cytosolic and mitochondrial forms. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273054 [Multi-domain]  Cd Length: 861  Bit Score: 313.54  E-value: 5.67e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDEVT 80
Cdd:TIGR00392 412 TKTPVIYRATEQWFIKTKDIKDQMLEQIKKVNWVPEWGEGRFGNWLENRPDWCISRQRYWGIPIPIWYCEDTGEPIVVGS 491

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  81 INHVADLFGKYGSNVWFERDAKDLLPDGYTNEHSPnGTFTKETDIMDVWFDSGSSHQGVLAERSYLD-----YPADLYLE 155
Cdd:TIGR00392 492 IEELIELIELKGIDAWFEDLHRDFLDKITLKSGDG-GEYRRVPDVLDVWFDSGSMPYASIHYPFENEkfkevFPADFILE 570

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 156 GSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:TIGR00392 571 GSDQTRGWFYSSLAIGTALFGQAPYKNVITHGFTLDEKGRKMSKSLGNVVDPLKVINKYG 630
PLN02843 PLN02843
isoleucyl-tRNA synthetase
 1-211 3.29e-96

isoleucyl-tRNA synthetase


Pssm-ID: 215452 [Multi-domain]  Cd Length: 974  Bit Score: 300.53  E-value: 3.29e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFY-AEDGTAIMDEV 79
Cdd:PLN02843  418 TKKPTIFRATEQWFASVEGFRQAALDAIDKVKWIPAQGENRIRAMVSGRSDWCISRQRTWGVPIPVFYhVETKEPLMNEE 497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKDLLPDGYTNEHSpngTFTKETDIMDVWFDSGSSHQGVLAERSYLDYPADLYLEGSDQ 159
Cdd:PLN02843  498 TIAHVKSIVAQKGSDAWWYMDVEDLLPEKYRDKAS---DYEKGTDTMDVWFDSGSSWAGVLGSREGLSYPADLYLEGSDQ 574

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1511892312 160 YRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVI 211
Cdd:PLN02843  575 HRGWFQSSLLTSVATKGKAPYKSVLTHGFVLDEKGFKMSKSLGNVVDPRLVI 626
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 1-215 1.82e-85

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 264.27  E-value: 1.82e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAED-GTAIMDEV 79
Cdd:pfam00133 368 SGTPIIPRATPQWFVRMDELADQALEAVEKVQFVPKSGEKRYFNWLANIQDWCISRQRWWGHPIPAWVSKDtEEVVCRGE 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  80 TINHVADLFGKYGSNVWFERDAKDLLPDGytnehspNGTFTKETDIMDVWFDSGSSHQGVL------AERSYLDYPADLY 153
Cdd:pfam00133 448 LFELVAGRFEEEGSIKWLHREAKDKLGYG-------KGTLEQDEDVLDTWFSSGSWPFSTLgwpfvnTEEFKKFFPADML 520

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511892312 154 LEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:pfam00133 521 LEGSDQTRGWFYRMIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYG 582
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
 4-215 4.49e-80

catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 242.52  E-value: 4.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   4 PIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDevtinh 83
Cdd:cd00818   144 PLIYRATPQWFIRVTKIKDRLLEANDKVNWIPEWVKNRFGNWLENRRDWCISRQRYWGTPIPVWYCEDCGEVLV------ 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  84 vadlfgkygsnvwferdakdllpdgytnehspngtfTKETDIMDVWFDSGSSHQGVL-----AERSYLDYPADLYLEGSD 158
Cdd:cd00818   218 ------------------------------------RRVPDVLDVWFDSGSMPYAQLhypfeNEDFEELFPADFILEGSD 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00818   262 QTRGWFYSLLLLSTALFGKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYG 318
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
 2-215 3.47e-47

catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. Enzymes in this subfamily share an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids. MetRS has a significantly shorter insertion, which lacks the editing function.


Pssm-ID: 185674 [Multi-domain]  Cd Length: 312  Bit Score: 157.58  E-value: 3.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   2 KKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPifyaedgtaimdevti 81
Cdd:cd00668   131 RGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAWLESLLDWAISRQRYWGTPLP---------------- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  82 nhvadlfgkygsnvwferdakdllpdgytnehspngtftkeTDIMDVWFDSGSSHQGVLAERS-----YLDYPADLYLEG 156
Cdd:cd00668   195 -----------------------------------------EDVFDVWFDSGIGPLGSLGYPEekewfKDSYPADWHLIG 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1511892312 157 SDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00668   234 KDILRGWANFWITMLVALFGEIPPKNLLVHGFVLDEGGQKMSKSKGNVIDPSDVVEKYG 292
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
 1-215 1.17e-40

catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. ValRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 185677 [Multi-domain]  Cd Length: 382  Bit Score: 142.39  E-value: 1.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   1 TKKPIIFRATPQWFASVGDMRDEILKSM--DDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAImde 78
Cdd:cd00817   159 SGDVIEPLLKPQWFVKVKDLAKKALEAVkeGDIKFVPERMEKRYENWLENIRDWCISRQLWWGHRIPAWYCKDGGHW--- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  79 vtinhVADLfgkygsnvwfERDAKDLLPDGYTNEHSPNGTFTKETDIMDVWFDSGSSHQGVLA---ERSYLD--YPADLY 153
Cdd:cd00817   236 -----VVAR----------EEDEAIDKAAPEACVPCGGEELKQDEDVLDTWFSSSLWPFSTLGwpeETKDLKkfYPTSLL 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511892312 154 LEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00817   301 VTGHDIIFFWVARMIMRGLKLTGKLPFKEVYLHGLVRDEDGRKMSKSLGNVIDPLDVIDGYG 362
valS PRK13208
valyl-tRNA synthetase; Reviewed
 2-215 1.05e-39

valyl-tRNA synthetase; Reviewed


Pssm-ID: 237306 [Multi-domain]  Cd Length: 800  Bit Score: 144.18  E-value: 1.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   2 KKPIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGKKRLYNMIRD-RGDWVISRQRVWGVPLPIFYAEDGTAImdevt 80
Cdd:PRK13208  347 DTPLEILVTRQWFIKVLDLKEELLERGKEINWYPEHMRVRLENWIEGlNWDWCISRQRYFGTPIPVWYCKDCGHP----- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  81 inHVADLfGKYGSNVWFErdakdlLPDGYTNEHSPNGTFTKETDIMDVWFDSGSSHQ---GVLAERSYLD--YPADLYLE 155
Cdd:PRK13208  422 --ILPDE-EDLPVDPTKD------EPPGYKCPQCGSPGFEGETDVMDTWATSSITPLivtGWERDEDLFEkvFPMDLRPQ 492

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 156 GSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PRK13208  493 GHDIIRTWLFYTILRAYLLTGKLPWKNIMISGMVLDPDGKKMSKSKGNVVTPEELLEKYG 552
valS TIGR00422
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ...
 10-215 1.33e-32

valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273070 [Multi-domain]  Cd Length: 861  Bit Score: 124.02  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  10 TPQWFASVGDMRDEILKSMDD--VEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAImdevtinHVADL 87
Cdd:TIGR00422 355 SKQWFVKVEKLADKALEAAEEgeIKFVPKRMEKRYLNWLRNIKDWCISRQLIWGHRIPVWYCKECGEV-------YVAKE 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  88 fgkygsnvwferdakDLLPDGYTNEhSPNGTFTKETDIMDVWFDSGSS-------HQGVLAERSYldYPADLYLEGSDQY 160
Cdd:TIGR00422 428 ---------------EPLPDDKTNT-GPSVELEQDTDVLDTWFSSSLWpfstlgwPDETKDLKKF--YPTDLLVTGYDII 489

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1511892312 161 RGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:TIGR00422 490 FFWVARMIFRSLALTGQVPFKEVYIHGLVRDEQGRKMSKSLGNVIDPLDVIEKYG 544
PLN02882 PLN02882
aminoacyl-tRNA ligase
 4-215 1.95e-32

aminoacyl-tRNA ligase


Pssm-ID: 215477 [Multi-domain]  Cd Length: 1159  Bit Score: 123.68  E-value: 1.95e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312    4 PIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGK-KRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAImdeVTIN 82
Cdd:PLN02882   418 PLIYRAVPSWFVKVEEIKDRLLENNKQTYWVPDYVKeKRFHNWLENARDWAVSRSRFWGTPLPIWISDDGEEV---VVIG 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   83 HVADLFGKYGSNVW-FERDAKDLL--PDGYTNEHSPngtFTKETDIMDVWFDSGSSHQGVL------AERSYLDYPADLY 153
Cdd:PLN02882   495 SIAELEKLSGVKVTdLHRHFIDHItiPSSRGPEFGV---LRRVDDVFDCWFESGSMPYAYIhypfenKELFEKNFPADFV 571

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1511892312  154 LEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PLN02882   572 AEGLDQTRGWFYTLMVLSTALFDKPAFKNLICNGLVLAEDGKKMSKSLKNYPDPNEVIDKYG 633
PTZ00427 PTZ00427
isoleucine-tRNA ligase, putative; Provisional
 4-215 1.83e-31

isoleucine-tRNA ligase, putative; Provisional


Pssm-ID: 173617 [Multi-domain]  Cd Length: 1205  Bit Score: 120.84  E-value: 1.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312    4 PIIFRATPQWFASVGDMRDEILKSMDDVEFFPEWGK-KRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDEVTIN 82
Cdd:PTZ00427   522 PLIYRAIPAWFIRVSNSTNELVKNNETTYWIPAHIKeKKFHNWIKDAKDWCISRNRYWGTPIPIWADEKMETVICVESIK 601

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   83 HVADLFGKygsnvwfeRDAKDL---LPDGYTNEHSPNGTFTKE---TDIMDVWFDSGSS-----HQGVLAERSYLD--YP 149
Cdd:PTZ00427   602 HLEELSGV--------KNINDLhrhFIDHIEIKNPKGKTYPKLkriPEVFDCWFESGSMpyakvHYPFSTEKEDFHkiFP 673

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1511892312  150 ADLYLEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PTZ00427   674 ADFIAEGLDQTRGWFYTLLVISTLLFDKAPFKNLICNGLVLASDGKKMSKRLKNYPDPLYILDKYG 739
valS PRK05729
valyl-tRNA synthetase; Reviewed
 10-215 8.31e-19

valyl-tRNA synthetase; Reviewed


Pssm-ID: 235582 [Multi-domain]  Cd Length: 874  Bit Score: 84.00  E-value: 8.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  10 TPQWFASVGDMRDEILKSM--DDVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGtaimdevtinhvadl 87
Cdd:PRK05729  357 SDQWFVKMKPLAKPALEAVenGEIKFVPERWEKTYFHWMENIQDWCISRQLWWGHRIPAWYDEDG--------------- 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  88 fgkygsNVWFERDAKdllpdgytnEHSPNGTFTKETDIMDVWFDSGsshqgvLAERSYLDYPADlylegSDQYRGWF-NS 166
Cdd:PRK05729  422 ------EVYVGREEP---------EAREKALLTQDEDVLDTWFSSA------LWPFSTLGWPEK-----TEDLKRFYpTS 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1511892312 167 SLITS-------VA--------VSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PRK05729  476 VLVTGfdiiffwVArmimmglhFTGQVPFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYG 539
PLN02381 PLN02381
valyl-tRNA synthetase
 11-214 9.46e-19

valyl-tRNA synthetase


Pssm-ID: 215214 [Multi-domain]  Cd Length: 1066  Bit Score: 84.18  E-value: 9.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   11 PQWFASVGDMRDEILKSMDD-----VEFFP-----EWgkKRLYNMIRDrgdWVISRQRVWGVPLPIFYA--EDgtaimDE 78
Cdd:PLN02381   469 PQWFVNCSSMAKQALDAAIDgenkkLEFIPkqylaEW--KRWLENIRD---WCISRQLWWGHRIPAWYVtlED-----DQ 538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   79 VTInhvadlFGKYGSNVWFERDAKDLLPDGYTNEHSPNGTFTKETDIMDVWFDSGSSHQGVLAERSYLD-----YPADLY 153
Cdd:PLN02381   539 LKE------LGSYNDHWVVARNESDALLEASQKFPGKKFELSQDPDVLDTWFSSGLFPLSVLGWPDDTDdlkafYPTSVL 612

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511892312  154 LEGSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQM 214
Cdd:PLN02381   613 ETGHDILFFWVARMVMMGMQLGGDVPFRKVYLHPMIRDAHGRKMSKSLGNVIDPLEVINGI 673
PLN02943 PLN02943
aminoacyl-tRNA ligase
 12-215 1.88e-18

aminoacyl-tRNA ligase


Pssm-ID: 215509 [Multi-domain]  Cd Length: 958  Bit Score: 83.07  E-value: 1.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  12 QWFASVGDMRDEILKSMDDVEF--FPEWGKKrLYNM-IRDRGDWVISRQRVWGVPLPIFYAEDGTAIMDEVTINHVADLF 88
Cdd:PLN02943  409 QWFVTMEPLAEKALKAVENGELtiIPERFEK-IYNHwLSNIKDWCISRQLWWGHRIPVWYIVGKDCEEDYIVARSAEEAL 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  89 G----KYGSNVwferdakdllpdgytnehspngTFTKETDIMDVWFDSG---SSHQG---VLAERSYLDYPADLYLEGSD 158
Cdd:PLN02943  488 EkareKYGKDV----------------------EIYQDPDVLDTWFSSAlwpFSTLGwpdVSAEDFKKFYPTTVLETGHD 545

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 159 QYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PLN02943  546 ILFFWVARMVMMGIEFTGTVPFSYVYLHGLIRDSQGRKMSKTLGNVIDPLDTIKEFG 602
ValS COG0525
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ...
 10-215 3.63e-16

Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440291 [Multi-domain]  Cd Length: 877  Bit Score: 76.24  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  10 TPQWFASVGDMRDEILKSM--DDVEFFPEWGKKRLYN-M--IRDrgdWVISRQRVWGVPLPIFYAEDGtaimdevtinhv 84
Cdd:COG0525   356 SDQWFVKMKPLAKPAIEAVedGEIKFVPERWEKTYFHwMenIRD---WCISRQLWWGHRIPAWYCPDG------------ 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  85 adlfgkygsNVWFERDAKDLLPdgytneHSPNGTFTKETDIMDVWFDSG----SShqgvlaersyLDYPadlylEGSDQY 160
Cdd:COG0525   421 ---------EVYVARTEPEACA------KAGSVNLTQDEDVLDTWFSSAlwpfST----------LGWP-----EKTEDL 470

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511892312 161 RGWF-NSSLITS-------VA--------VSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:COG0525   471 KYFYpTSVLVTGfdiiffwVArmimmglhFTGEVPFKDVYIHGLVRDEQGRKMSKSKGNVIDPLDLIDKYG 541
valS PRK14900
valyl-tRNA synthetase; Provisional
 8-215 1.00e-14

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 72.33  E-value: 1.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312    8 RATPQWFASVGDMRDEILKSMDD--VEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFYAEDGtaimdEVTInhva 85
Cdd:PRK14900   370 LLSDQWYVRIEPLARPAIEAVEQgrTRFIPEQWTNTYMAWMRNIHDWCISRQLWWGHQIPAWYCPDG-----HVTV---- 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   86 dlfgkygsnvwfERDAKDLLPDgytnehSPNGTFTKETDIMDVWFDSG---SSHQGVLAERSYLD--YPADLYLEGSDQY 160
Cdd:PRK14900   441 ------------ARETPEACST------CGKAELRQDEDVLDTWFSSGlwpFSTMGWPEQTDTLRtfYPTSVMETGHDII 502

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1511892312  161 RGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PRK14900   503 FFWVARMMMMGLHFMGEVPFRTVYLHPMVRDEKGQKMSKTKGNVIDPLVITEQYG 557
PTZ00419 PTZ00419
valyl-tRNA synthetase-like protein; Provisional
 11-212 8.08e-13

valyl-tRNA synthetase-like protein; Provisional


Pssm-ID: 240411 [Multi-domain]  Cd Length: 995  Bit Score: 66.57  E-value: 8.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  11 PQWFASVGDMRDEILKSMD--DVEFFPEWGKKRLYNMIRDRGDWVISRQRVWGVPLPIFyaedgtaimdEVTINhvADLF 88
Cdd:PTZ00419  402 PQWYVNCKDMAKRAVEAVRngELKIIPSSHENVWYHWLENIQDWCISRQLWWGHRIPAY----------RVISK--GPET 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  89 GKYGSNVWF--------ERDAKDLLPDgytNEHSPngTFTKETDIMDVWFDSGS---SHQGVLAERSYLD--YPADLYLE 155
Cdd:PTZ00419  470 DPSDEEPWVvarseeeaLEKAKKKFGL---SEEDF--ELEQDEDVLDTWFSSGLfpfSTLGWPDQTDDLQrfFPTSLLET 544

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1511892312 156 GSDQYRGWFNSSLITSVAVSGHAPYKQVLSQGFTLDNQGRKMSKSLGNTIAPADVIK 212
Cdd:PTZ00419  545 GSDILFFWVARMVMMSLHLTDKLPFKTVFLHAMVRDSQGEKMSKSKGNVIDPLEVIE 601
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
 12-215 1.52e-12

catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173906 [Multi-domain]  Cd Length: 314  Bit Score: 64.96  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  12 QWFA--SVGDMRDEILKSMDDVEFFPEwgkkRLYNMIRDrgdWV-ISRQRVWGVPLPIfyaedgTAIMDEVTinhvadlf 88
Cdd:cd00812   131 QWFLkySETEWKEKLLKDLEKLDGWPE----EVRAMQEN---WIgCSRQRYWGTPIPW------TDTMESLS-------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  89 gkyGSNVWFERdakdllpdgYTNEHSPNGTFTKETDIMDvwfdsgsshqgvlAERSYLdYPADLYLEGSDQ-------YR 161
Cdd:cd00812   190 ---DSTWYYAR---------YTDAHNLEQPYEGDLEFDR-------------EEFEYW-YPVDIYIGGKEHapnhllySR 243

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1511892312 162 gwFNSSLITSVAVSGHAPYKQVLSQGFTLDNqGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00812   244 --FNHKALFDEGLVTDEPPKGLIVQGMVLLE-GEKMSKSKGNVVTPDEAIKKYG 294
LeuS COG0495
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ...
 51-215 3.10e-11

Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440261 [Multi-domain]  Cd Length: 826  Bit Score: 61.99  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  51 DWVISRQRVWGVPLPIFYAEDGTAIM--DE---VTINHVADLFGKYGS---------NVWFERDakdllpdgytnehspN 116
Cdd:COG0495   421 DWLISRQRYWGEPIPIIHCEDCGVVPvpEDqlpVELPEDVDFDPTGGSplarapewvNVTCPKC---------------G 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 117 GTFTKETDIMDVWFDS----------GSSHQGVLAERsyLDY--PADLYlegsdqyrgwfnsslitsvaVSG--HA---- 178
Cdd:COG0495   486 GPARRETDTMDTFVDSswyylrytdpHNDEAPFDPEA--ANYwlPVDQY--------------------IGGieHAilhl 543

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1511892312 179 --------------------PYKQVLSQG--FTLDNQGR------KMSKSLGNTIAPADVIKQMG 215
Cdd:COG0495   544 lyarfftkvlrdlglvsfdePFKRLLTQGmvLEVGKDGVviggieKMSKSKGNVVDPDEIIEKYG 608
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
 125-215 1.81e-07

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 50.65  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 125 IMDVWFDS--------GSSHQGVLAERSYLDY-PADLYLEGSDQYRgwfnSSLITSVAVSGHAPY---KQVLSQGFtLDN 192
Cdd:PRK11893  221 VIYVWFDAltnyltalGYPDDEELLAELFNKYwPADVHLIGKDILR----FHAVYWPAFLMAAGLplpKRVFAHGF-LTL 295

                          90       100
                  ....*....|....*....|...
gi 1511892312 193 QGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PRK11893  296 DGEKMSKSLGNVIDPFDLVDEYG 318
PLN02563 PLN02563
aminoacyl-tRNA ligase
 38-215 4.59e-06

aminoacyl-tRNA ligase


Pssm-ID: 178177 [Multi-domain]  Cd Length: 963  Bit Score: 46.74  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  38 GKKRLYNMIRDrgdWVISRQRVWGVPLPIFYAEDGTAIMDEVtinhvadlfgkygsnvwfERDAKDLLPDgyTNEHSPNG 117
Cdd:PLN02563  496 GKKKVNYKLRD---WLFARQRYWGEPIPVVFLEDSGEPVPVP------------------ESDLPLTLPE--LDDFTPTG 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 118 T----------------------FTKETDIMDVW----------FDSGSSHQGVLAERSYLDYPADLYLEGSDQ------ 159
Cdd:PLN02563  553 TgepplakavswvntvdpssgkpARRETNTMPQWagscwyylrfMDPKNSNALVDKEKEKYWMPVDLYVGGAEHavlhll 632

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 160 YRGWFNSSLITSVAVSGHAPYKQVLSQGFTL---------DNQGR----------------------------------- 195
Cdd:PLN02563  633 YARFWHKVLYDIGVVSTKEPFQCLVNQGMILgeveytafkDSDGEyvsadtadrlgelqqekipeekviksgdsfvlkdd 712

                         250       260       270
                  ....*....|....*....|....*....|
gi 1511892312 196 ----------KMSKSLGNTIAPADVIKQMG 215
Cdd:PLN02563  713 psirliarahKMSKSRGNVVNPDDVVSEYG 742
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
 175-215 1.56e-05

Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 45.10  E-value: 1.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1511892312 175 SGHAPYKQVLSQGFtLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:COG0143   307 AGLPLPKKVFAHGF-LTVEGEKMSKSRGNVIDPDDLLDRYG 346
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
 6-215 4.95e-05

catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.


Pssm-ID: 173907 [Multi-domain]  Cd Length: 319  Bit Score: 43.29  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312   6 IFRATPQWFASVGDMRDEILKSMDDVEFF--PEWGKKRLYNMIRDR-GDWVISRQRV-WGVPLPIFyaedgtaimDEVTI 81
Cdd:cd00814   133 EWREEEHYFFRLSKFQDRLLEWLEKNPDFiwPENARNEVLSWLKEGlKDLSITRDLFdWGIPVPLD---------PGKVI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312  82 nhvadlfgkYgsnVWFerDAkdllPDGYTnehspngTFTKEtdimdvWFDSGSShqgvlaERSYLDY-PADLYLEGSD-- 158
Cdd:cd00814   204 ---------Y---VWF--DA----LIGYI-------SATGY------YNEEWGN------SWWWKDGwPELVHFIGKDii 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1511892312 159 ----QYrgwFNSSLITSvavsGHAPYKQVLSQGFtLDNQGRKMSKSLGNTIAPADVIKQMG 215
Cdd:cd00814   247 rfhaIY---WPAMLLGA----GLPLPTRIVAHGY-LTVEGKKMSKSRGNVVDPDDLLERYG 299
PLN02224 PLN02224
methionine-tRNA ligase
 128-215 1.66e-04

methionine-tRNA ligase


Pssm-ID: 177869 [Multi-domain]  Cd Length: 616  Bit Score: 42.01  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1511892312 128 VWFDSGSSHQGVLAERS---------YLDYPADLYLEGSDQYRgwFNSSLITSVAVS-GHAPYKQVLSQGFtLDNQGRKM 197
Cdd:PLN02224  291 VWFDALLGYISALTEDNkqqnletavSFGWPASLHLIGKDILR--FHAVYWPAMLMSaGLELPKMVFGHGF-LTKDGMKM 367

                          90
                  ....*....|....*...
gi 1511892312 198 SKSLGNTIAPADVIKQMG 215
Cdd:PLN02224  368 GKSLGNTLEPFELVQKFG 385
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 179-215 1.35e-03

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 39.01  E-value: 1.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1511892312 179 PYKQVLSQGFTLDNqGRKMSKSLGNTIAPADVIKQMG 215
Cdd:PRK12267  283 LPKKVFAHGWWLMK-DGKMSKSKGNVVDPEELVDRYG 318
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
 194-213 4.11e-03

Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439985 [Multi-domain]  Cd Length: 465  Bit Score: 37.39  E-value: 4.11e-03
                          10        20
                  ....*....|....*....|
gi 1511892312 194 GRKMSKSLGNTIAPADVIKQ 213
Cdd:COG0215   263 GEKMSKSLGNFFTVRDLLKK 282
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH