|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
5-549 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1087.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 164
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 165 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 243
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 244 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDsVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 323
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 324 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 404 FDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdlQAICSMGINL 483
Cdd:PRK00133 401 FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PFV_A 484 FRVLMTYLKPVLPKLTERAEAFLN-TELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEE 549
Cdd:PRK00133 479 FRALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEA 545
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
5-543 |
0e+00 |
|
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: 870.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 164
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 165 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 243
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 244 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWkKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 323
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 324 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 404 FDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdLQAICSM 479
Cdd:COG0143 398 FDGKVpepgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PFV_A 480 GINLFRVLMTYLKPVLPKLTERAEAFLN---TELTWDGIQQPLL-GHKVNPFKALYNRIDMRQVEALV 543
Cdd:COG0143 477 LLEALRILAILLKPFLPETAEKILEQLGlegDELTWEDAGWPLPaGHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
7-535 |
0e+00 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 781.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 7 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 86
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 87 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 166
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 167 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 242
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 243 PNAPGKYFYVWLDAPIGYMGSfknLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 322
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISS---LGILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 323 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINK 402
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 403 RFDGVLASELA----DPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICS 478
Cdd:TIGR00398 397 YFNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVCS 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
1PFV_A 479 MginLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRID 535
Cdd:TIGR00398 477 M---LIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
7-396 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 619.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 7 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 86
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 87 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 166
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 167 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPN 244
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 245 APGKYFYVWLDAPIGYMGSFKNLCdkrGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHG 324
Cdd:pfam09334 240 AEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PFV_A 325 YVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 396
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR-NRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
6-371 |
7.02e-147 |
|
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: 425.02 E-value: 7.02e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 6 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFA 85
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 86 GFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 165
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 166 spteliepksvvsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 242
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 243 PNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSvsfdeYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 322
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGNS-----WWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
1PFV_A 323 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDID 371
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
5-549 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1087.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 164
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 165 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 243
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 244 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDsVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 323
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 324 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 404 FDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdlQAICSMGINL 483
Cdd:PRK00133 401 FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PFV_A 484 FRVLMTYLKPVLPKLTERAEAFLN-TELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKEE 549
Cdd:PRK00133 479 FRALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEA 545
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
5-543 |
0e+00 |
|
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: 870.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 164
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 165 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 243
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 244 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWkKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 323
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 324 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 403
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 404 FDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdLQAICSM 479
Cdd:COG0143 398 FDGKVpepgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1PFV_A 480 GINLFRVLMTYLKPVLPKLTERAEAFLN---TELTWDGIQQPLL-GHKVNPFKALYNRIDMRQVEALV 543
Cdd:COG0143 477 LLEALRILAILLKPFLPETAEKILEQLGlegDELTWEDAGWPLPaGHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
7-535 |
0e+00 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 781.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 7 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 86
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 87 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 166
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 167 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 242
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 243 PNAPGKYFYVWLDAPIGYMGSfknLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 322
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISS---LGILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 323 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINK 402
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 403 RFDGVLASELA----DPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICS 478
Cdd:TIGR00398 397 YFNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVCS 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
1PFV_A 479 MginLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRID 535
Cdd:TIGR00398 477 M---LIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
7-396 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 619.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 7 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 86
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 87 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 166
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 167 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPN 244
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 245 APGKYFYVWLDAPIGYMGSFKNLCdkrGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHG 324
Cdd:pfam09334 240 AEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PFV_A 325 YVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 396
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR-NRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
6-371 |
7.02e-147 |
|
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: 425.02 E-value: 7.02e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 6 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFA 85
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 86 GFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 165
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 166 spteliepksvvsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 242
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 243 PNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSvsfdeYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 322
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGNS-----WWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
1PFV_A 323 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDID 371
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
6-372 |
5.22e-127 |
|
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: 374.06 E-value: 5.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 6 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGI-------------TPEQM 72
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 73 IGEMSQEHQTDFAGFNISYD--NYHSTHSEENRQLSELIYSRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkcks 150
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 151 pdqygdncevcgatyspteliepksvvsgatpvmRDSEHFFFDLPSFSEMLQAWTRSGA-LQEQVANKMQEWFESGLQqW 229
Cdd:cd00668 137 ----------------------------------RITEQWFFDMPKFKEKLLKALRRGKiVPEHVKNRMEAWLESLLD-W 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 230 DISRDApYFGFEIPNapgKYFYVWLDAPIGYMGSFKNLCDKRgdsvsfdeyWKKDSTAELYHFIGKDIVYFHSLFWPAML 309
Cdd:cd00668 182 AISRQR-YWGTPLPE---DVFDVWFDSGIGPLGSLGYPEEKE---------WFKDSYPADWHLIGKDILRGWANFWITML 248
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
1PFV_A 310 EGSNFR-KPSNLFVHGYVTVN-GAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDL 372
Cdd:cd00668 249 VALFGEiPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLA-PYGDDIRL 312
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
5-535 |
1.72e-103 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 320.68 E-value: 1.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckspdqygdnCEVCGAT 164
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 165 YSPTELIEPKSV--VSGATPVMRDSEHFFFDLPSFSEMLQAW--TRSGALQ-EQVANKMQEWFESGLQQWDISR---DAp 236
Cdd:PRK11893 132 YTESELIEDGYRcpPTGAPVEWVEEESYFFRLSKYQDKLLELyeANPDFIQpASRRNEVISFVKSGLKDLSISRtnfDW- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 237 yfGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDStaelyHFIGKDIVYFHSLFWPAMLEGSNFRK 316
Cdd:PRK11893 211 --GIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELLAELFNKYWPADV-----HLIGKDILRFHAVYWPAFLMAAGLPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 317 PSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRyYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 396
Cdd:PRK11893 284 PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVR-YFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 397 AGFINKRFDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEgrDAD 472
Cdd:PRK11893 363 LSMIAKNFDGKVpepgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTD--PER 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1PFV_A 473 LQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTE---------LTWDGIQQpllGHKVNPFKALYNRID 535
Cdd:PRK11893 441 LATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEedenrdfaaLSWGRLAP---GTTLPKPEPIFPRLE 509
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
5-507 |
9.31e-81 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 268.96 E-value: 9.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHI-QADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 83
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 84 FAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKSPDQYGDNCEVC 161
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 162 GATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQ-VANKMQ---EWFESGLQQWDISRD--- 234
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGwSQNAIQttnAWLRDGLKPRCITRDlkw 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 235 ---APYFGFEipnapGKYFYVWLDAPIGYMGSFKNLcdkrgdSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEG 311
Cdd:PLN02610 257 gvpVPLEKYK-----DKVFYVWFDAPIGYVSITACY------TPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 312 S--NFRKPSNLFVHGYVTVNGAKMSKSRG----------TFIKASTWlnhfdadslRYYYtakLSSR--IDDIDLNLEDF 377
Cdd:PLN02610 326 TgeNWTMMKTISVTEYLNYEGGKFSKSKGvgvfgndakdTNIPVEVW---------RYYL---LTNRpeVSDTLFTWADL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 378 VQRVNADIVNKVVNLASRNAGFI----NKRFDGVL--ASELADPQLYKTFtdaAEVIG-------EAWESREFGKAVREI 444
Cdd:PLN02610 394 QAKLNSELLNNLGNFINRVLSFIakppGAGYGSVIpdAPGAESHPLTKKL---AEKVGklveqyvEAMEKVKLKQGLKTA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PFV_A 445 MALADLANRYVDEQAPWVVAKQegrDADLQAI---CSMGinLFRVLMTYLKPVLPKLTERAEAFLN 507
Cdd:PLN02610 471 MSISSEGNAYLQESQFWKLYKE---DKPSCAIvvkTSVG--LVYLLACLLEPFMPSFSKEVLKQLN 531
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
5-551 |
1.30e-78 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 259.73 E-value: 1.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 5 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 84
Cdd:PRK12267 4 KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 85 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI-KNR-------------TISQLYDPEKgmflpdrfvkgtCPKCKS 150
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIyKGEyegwycvscetffTESQLVDGGK------------CPDCGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 151 PdqygdncevcgatyspTELIEPKSvvsgatpvmrdsehFFFDLPSFSEMLQAWTRSGA---LQEQVANKMQEWF-ESGL 226
Cdd:PRK12267 152 E----------------VELVKEES--------------YFFRMSKYQDRLLEYYEENPdfiQPESRKNEMINNFiKPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 227 QQWDISRDAPYFGFEIPNAPGKYFYVWLDA------PIGYMGSfknlcdkrgDSVSFDEYWKKDstaelYHFIGKDIVYF 300
Cdd:PRK12267 202 EDLSISRTSFDWGIPVPFDPKHVVYVWIDAllnyitALGYGSD---------DDELFKKFWPAD-----VHLVGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 301 HSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYytakLSSRI---DDIDLNLEDF 377
Cdd:PRK12267 268 HAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY----LLREVpfgSDGDFSPEAL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 378 VQRVNADIVNKVVNLASRNAGFINKRFDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR 453
Cdd:PRK12267 344 VERINSDLANDLGNLLNRTVAMINKYFDGEIpapgNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 454 YVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTER---------AEAFLNTELTWDGIQqplLGHKV 524
Cdd:PRK12267 424 YIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKifeqlgleeELTSWESLLEWGGLP---AGTKV 500
|
570 580
....*....|....*....|....*..
1PFV_A 525 NPFKALYNRIDMRQVEALVEASKEEVK 551
Cdd:PRK12267 501 AKGEPLFPRIDVEEEIAYIKEQMEGSA 527
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
4-501 |
2.94e-55 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 196.47 E-value: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 4 AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 83
Cdd:PLN02224 68 ADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 84 FAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkspDQYGDNcevcga 163
Cdd:PLN02224 148 WKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDE------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 164 tyspTELIEPKSVVSGATP-VMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVA---NKMQEWFESGLQQWDISRDAPYFG 239
Cdd:PLN02224 203 ----KELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSyrlNEVQSWIKSGLRDFSISRALVDWG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 240 FEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDstaelYHFIGKDIVYFHSLFWPAMLEGSNFRKPSN 319
Cdd:PLN02224 279 IPVPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPAS-----LHLIGKDILRFHAVYWPAMLMSAGLELPKM 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 320 LFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRiDDIDLNLEDFVQRVNADIVNKVVNLASRNAGF 399
Cdd:PLN02224 354 VFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 400 INKRFDGVLASELADPQLYKTFTDAAEVIGEA----WESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQA 475
Cdd:PLN02224 433 LKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKaqtnYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAA 512
|
490 500
....*....|....*....|....*..
1PFV_A 476 I-CSMGINLFRVLMTYLKPVLPKLTER 501
Cdd:PLN02224 513 KdLVIILEVMRVIAVALSPIAPCLSLR 539
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
374-506 |
4.43e-40 |
|
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA synthetases (MetRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon (CAU). MetRS catalyzes the transfer of methionine to the 3'-end of its tRNA.
Pssm-ID: 153411 [Multi-domain] Cd Length: 129 Bit Score: 141.86 E-value: 4.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 374 LEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLAselADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR 453
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTE---EDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1PFV_A 454 YVDEQAPWVVAKQEGRDAdLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFL 506
Cdd:cd07957 78 YIDETAPWKLAKEEDPER-LATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
6-358 |
9.36e-20 |
|
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: 90.00 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 6 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQM----IGEMSQehQ 81
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWteynIKKMKE--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 82 TDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkCKSPDQYGDNcevc 161
Cdd:cd00812 79 LKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW-------------------CKLLDQWFLK---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 162 gatYSPTELIEpksvvsgatpvmrdsehfffDLPSFSEMLQAWTrsgalqEQVANKMQEWFesglqqwDISRDApYFGFE 241
Cdd:cd00812 136 ---YSETEWKE--------------------KLLKDLEKLDGWP------EEVRAMQENWI-------GCSRQR-YWGTP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 242 IPnapgkYFYV---WLDAPIgYMGSF---KNLCDKRGDSVSFD----EYWkkdSTAELYHFiGKDIVYFH---SLFWPAM 308
Cdd:cd00812 179 IP-----WTDTmesLSDSTW-YYARYtdaHNLEQPYEGDLEFDreefEYW---YPVDIYIG-GKEHAPNHllySRFNHKA 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
1PFV_A 309 L--EGSNFRK-PSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 358
Cdd:cd00812 249 LfdEGLVTDEpPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLY 301
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
14-358 |
4.05e-15 |
|
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: 76.50 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMS--------------- 77
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMGiaefnakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 78 ---QEHQTDFAGFNISYDNYHSTHSEEnrqlseliysrlkengFIKN--RTISQLYdpEKGMflpdrfvkgtcpkckspd 152
Cdd:cd00818 90 vdeQEEQFQRLGVWVDWENPYKTMDPE----------------YMESvwWVFKQLH--EKGL------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 153 qygdncevcgatyspteliepksVVSGATPVM-----RDSEHFFFDLPSF-SEMLQAWTRSGALQEQVANKMQEWFEsGL 226
Cdd:cd00818 134 -----------------------LYRGYKVVPwpliyRATPQWFIRVTKIkDRLLEANDKVNWIPEWVKNRFGNWLE-NR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 227 QQWDISRDApYFGFEIP----NAPGKY--------FYVWLDApiGYMGSFKNlcDKRGDSVSFDEYWKKDSTAElyhfiG 294
Cdd:cd00818 190 RDWCISRQR-YWGTPIPvwycEDCGEVlvrrvpdvLDVWFDS--GSMPYAQL--HYPFENEDFEELFPADFILE-----G 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 295 KDIV--YFHSLfwpaMLEGS-NFRKPS--NLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 358
Cdd:cd00818 260 SDQTrgWFYSL----LLLSTaLFGKAPykNVIVHGFVlDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
14-372 |
5.34e-15 |
|
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: 76.90 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEHQ 81
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 82 TDFA------GFNISYDNYHSTHSEENRQLSELIYSRLKENGFIknrtisqlydpEKGMFLPDRfvkgtCPKCKSPDQyg 155
Cdd:cd00817 90 GKIReqlkrlGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLI-----------YRDNRLVNW-----CPKLRTAIS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 156 dNCEVCGATYSPtelIEPKSvvsgatpvmrdSEHFFFDLPSFSEMLQAWTRSGALQ---EQVANKMQEWFESgLQQWDIS 232
Cdd:cd00817 152 -DIEVCSRSGDV---IEPLL-----------KPQWFVKVKDLAKKALEAVKEGDIKfvpERMEKRYENWLEN-IRDWCIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 233 RDApYFGFEIPnapgkyfyVWLDAPIGY--------------MGSFKNLCDK---RGDSVSFDE------------YWKK 283
Cdd:cd00817 216 RQL-WWGHRIP--------AWYCKDGGHwvvareedeaidkaAPEACVPCGGeelKQDEDVLDTwfssslwpfstlGWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 284 DsTAELYHFI-------GKDIVYfhslFWPA--MLEGSNF--RKP-SNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHF 350
Cdd:cd00817 287 E-TKDLKKFYptsllvtGHDIIF----FWVArmIMRGLKLtgKLPfKEVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGY 361
|
410 420
....*....|....*....|..
1PFV_A 351 DADSLRyYYTAKLSSRIDDIDL 372
Cdd:cd00817 362 GADALR-FTLASAATQGRDINL 382
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
14-79 |
8.67e-12 |
|
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: 68.18 E-value: 8.67e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITpEQMIGEMSQE 79
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIK-KKDIEKVGIA 120
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
14-119 |
1.55e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 64.06 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNF-ICADDaHGTPIMLKAQ-QLGITP----------------EQMIGE 75
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcreltDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1PFV_A 76 MSQEHQTdfAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI 119
Cdd:PRK13208 126 FRELWRR--LGLSVDWSLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
14-151 |
1.67e-10 |
|
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: 63.58 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMSQEHQTDFAGFNISYd 92
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVeKKLGIKEKKTRHKYGREEFREKCREWKME- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1PFV_A 93 nYHSTHSEENRQLSELI-----YSRLKEnGFIKN--RTISQLYDpeKGMFLPDRFVKGTCPKCKSP 151
Cdd:pfam00133 111 -YADEIRKQFRRLGRSIdwdreYFTMDP-ELEAAvwEVFVRLHD--KGLIYRGKKLVNWSPALNTA 172
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
14-119 |
9.78e-10 |
|
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: 61.23 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEH- 80
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESg 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
1PFV_A 81 -----QTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI 119
Cdd:TIGR00422 122 gtiknQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLI 165
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
14-64 |
1.28e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 60.94 E-value: 1.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQ 64
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
319-359 |
5.38e-06 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 47.57 E-value: 5.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
1PFV_A 319 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 359
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
291-376 |
1.18e-05 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 47.36 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 291 HFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY-YTAKLSSRID 368
Cdd:pfam01406 211 HGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFlLSVHYRSPLD 290
|
....*...
1PFV_A 369 DIDLNLED 376
Cdd:pfam01406 291 FSEELLEQ 298
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
294-398 |
1.24e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 48.33 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 294 GKDIVYFHSLF-------------WPAMLEgsnfrkpsnlfVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYT 360
Cdd:PRK12300 537 GKDLIPNHLTFfifnhvaifpeekWPRGIV-----------VNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT 605
|
90 100 110 120
....*....|....*....|....*....|....*....|
1PFV_A 361 --AKLSSridDIDLNlEDFVQRVnADIVNKVVNLASRNAG 398
Cdd:PRK12300 606 ssAELLQ---DADWR-EKEVESV-RRQLERFYELAKELIE 640
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
316-359 |
1.67e-05 |
|
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: 47.40 E-value: 1.67e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
1PFV_A 316 KPSNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 359
Cdd:COG0215 248 PFARYWMHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
18-45 |
3.37e-05 |
|
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: 46.97 E-value: 3.37e-05
10 20
....*....|....*....|....*....
1PFV_A 18 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 45
Cdd:COG0525 48 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 75
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
18-45 |
4.20e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 46.64 E-value: 4.20e-05
10 20
....*....|....*....|....*....
1PFV_A 18 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 45
Cdd:PRK05729 49 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 76
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
13-45 |
7.84e-05 |
|
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: 45.43 E-value: 7.84e-05
10 20 30
....*....|....*....|....*....|...
1PFV_A 13 LPYANGSIHLGHMLEHIQADVWVRYQRMRGHEV 45
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
14-99 |
8.52e-05 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which 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.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 42.85 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFI-CADDAHGTPIMLKAQQLGITP---EQMIGEMSQ--EHQTDFAGF 87
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIaLIDDAGGLIGDPANKKGENAKafvERWIERIKEdvEYMFLQAAD 85
|
90
....*....|..
1PFV_A 88 NISYDNYHSTHS 99
Cdd:cd00802 86 FLLLYETECDIH 97
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
14-141 |
2.36e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 44.04 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 14 PYANGS-IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLG----ITPEQMIGEMSQEHQTdfAGFN 88
Cdd:PLN02563 119 PYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGthpkITTLKNIARFRSQLKS--LGFS 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
1PFV_A 89 ISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFV 141
Cdd:PLN02563 197 YDWDREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV 249
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
300-456 |
9.58e-04 |
|
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: 41.99 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 300 FHSLFWPA-MLEGSN-FRkpsNLFVHGYVtV--NGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAklSSRIDDIdlnle 375
Cdd:COG0060 571 FYSSLLTStALFGRApYK---NVLTHGFV-LdeDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS--SDYWGDL----- 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 376 dfvqRVNADIVNkvvnlasRNAGFINK-----RFdgvLASELA--DPQ----------------LYKTFTDAAEVIgEAW 432
Cdd:COG0060 640 ----RFSDEILK-------EVRDVYRRlrntyRF---LLANLDdfDPAedavpyedlpeldrwiLSRLNELIKEVT-EAY 704
|
170 180
....*....|....*....|....*.
1PFV_A 433 ESREFGKAVREIMALA--DLANRYVD 456
Cdd:COG0060 705 DNYDFHRAYRALHNFCveDLSNWYLD 730
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
294-500 |
1.18e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 41.63 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 294 GKDIVYFhslfWPA--MLEGSNFRK--P-SNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRI 367
Cdd:PRK05729 480 GFDIIFF----WVArmIMMGLHFTGqvPfKDVYIHGLVrDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAA-LASPG 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 368 DDIDLNLEdfvqRVNadivnkvvnlASRNagFINK-----RF----DGVLASELADPQLYKTFTD----------AAEVI 428
Cdd:PRK05729 555 RDIRFDEE----RVE----------GYRN--FANKlwnasRFvlmnLEGADVGELPDPEELSLADrwilsrlnrtVAEVT 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1PFV_A 429 gEAWESREFGKAVREIMALA--DLANRYVdEqapwvVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTE 500
Cdd:PRK05729 619 -EALDKYRFDEAARALYEFIwnEFCDWYL-E-----LAKPVLQEAAKRATRATLAYVLEQILRLLHPFMPFITE 685
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
14-76 |
1.34e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 41.63 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
1PFV_A 14 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEM 76
Cdd:PLN02882 47 PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIdKKLGIKRRDDVLKM 110
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
20-151 |
5.14e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 39.85 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 20 IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQL---------------GItPEQMIGEM-------- 76
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIargdpetielykslyGI-PEEELEKFkdpeyive 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1PFV_A 77 --SQEHQTDF--AGFNIsyD---NYHSThSEENRQLSELIYSRLKENGFIknrtisqlydpekgmflpdrfVKGT----- 144
Cdd:PRK12300 80 yfSEEAKEDMkrIGYSI--DwrrEFTTT-DPEYSKFIEWQFRKLKEKGLI---------------------VKGShpvry 135
|
....*..
1PFV_A 145 CPKCKSP 151
Cdd:PRK12300 136 CPNDNNP 142
|
|
| |
