|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
6-677 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 1308.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDF 85
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 86 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 166 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 244
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 245 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDtVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 324
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 325 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFIAKR 404
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 405 FDGVLSAELADPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDAdlQAICTMGLNM 484
Cdd:PRK00133 401 FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 485 FRVLMTWLKPVLPQLAARAEAFLN-TELTWDAIQQPLLSHKVNTFKALYNRIEMKQVEALVEASKEEVKAATAP--VTGP 561
Cdd:PRK00133 479 FRALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEAAAAKAAAaaAAAP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 562 LADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYpDPQVLIGRQTVMVANLAPRK 641
Cdd:PRK00133 559 LAEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIKSAY-DPEELVGKLVVMVANLAPRK 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 556489810 642 MRFGISEGMVMAAGPGGKDIFLLSPDEGAKPGQQVK 677
Cdd:PRK00133 638 MKFGVSEGMVLAAGPGGGDLFLLEPDEGAKPGMRVK 673
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
6-544 |
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: 876.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDF 85
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 86 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 166 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 244
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 245 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTVSFDEYWkKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH 324
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 325 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFIAKR 404
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 405 FDGVLSA----ELADPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDAdLQAICTM 480
Cdd:COG0143 398 FDGKVPEpgelTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556489810 481 GLNMFRVLMTWLKPVLPQLAARAEAFLN---TELTWDAIQQPLLS-HKVNTFKALYNRIEMKQVEALV 544
Cdd:COG0143 477 LLEALRILAILLKPFLPETAEKILEQLGlegDELTWEDAGWPLPAgHKIGKPEPLFPRIEDEQIEALL 544
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
8-536 |
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: 770.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 8 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDFAG 87
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 88 FDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 167
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 168 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 243
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 244 PNAPGKYFYVWLDAPIGYMGSfknLCDKRGDTVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFV 323
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISS---LGILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 324 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFIAK 403
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 404 RFDGVLSAELA----DPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADLQAICt 479
Cdd:TIGR00398 397 YFNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVC- 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 556489810 480 mgLNMFRVLMTWLKPVLPQLAARAEAFLNTELTWDAIQQPLLSHKVNTFKALYNRIE 536
Cdd:TIGR00398 476 --SMLIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
8-397 |
0e+00 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 628.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 8 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDFAG 87
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 88 FDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 167
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 168 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPN 245
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 246 APGKYFYVWLDAPIGYMGSFKNLCDKRGDtvsFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVHG 325
Cdd:pfam09334 240 AEGKVFYVWLDAPIGYISATKELSGNEEK---WKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556489810 326 YVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 397
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR-NRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
7-372 |
2.49e-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: 430.80 E-value: 2.49e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDFA 86
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 87 GFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 166
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 167 spteliepksvvsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 243
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 244 PNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDtvsfdEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFV 323
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGN-----SWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 556489810 324 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDID 372
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
6-677 |
7.47e-130 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 397.63 E-value: 7.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDF 85
Cdd:PRK12267 4 KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 86 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFI-KNR-------------TISQLYDPEKgmflpdrfvkgtCPKCKS 151
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIyKGEyegwycvscetffTESQLVDGGK------------CPDCGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 152 PdqygdncevcgatyspTELIEPKSvvsgatpvmrdsehFFFDLPSFSEMLQAWTRSGA---LQEQVANKMQEWF-ESGL 227
Cdd:PRK12267 152 E----------------VELVKEES--------------YFFRMSKYQDRLLEYYEENPdfiQPESRKNEMINNFiKPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 228 QQWDISRDAPYFGFEIPNAPGKYFYVWLDA------PIGYMGSfknlcdkrgDTVSFDEYWKKDstaelYHFIGKDIVYF 301
Cdd:PRK12267 202 EDLSISRTSFDWGIPVPFDPKHVVYVWIDAllnyitALGYGSD---------DDELFKKFWPAD-----VHLVGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 302 HSLFWPAMLEGSNFRKPTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYytakLSSRI---DDIDLNLEDF 378
Cdd:PRK12267 268 HAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY----LLREVpfgSDGDFSPEAL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 379 VQRVNADIVNKVVNLASRNAGFIAKRFDGVLSA----ELADPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANR 454
Cdd:PRK12267 344 VERINSDLANDLGNLLNRTVAMINKYFDGEIPApgnvTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 455 YVDEQAPWVVAKQEGRDADLQAICTMGLNMFRVLMTWLKPVLPQLAAR---------AEAFLNTELTWDAIQQPllsHKV 525
Cdd:PRK12267 424 YIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKifeqlgleeELTSWESLLEWGGLPAG---TKV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 526 NTFKALYNRIEmkqVEALVEASKEEVKAATAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDL 605
Cdd:PRK12267 501 AKGEPLFPRID---VEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLEAEKVEKSDKLLKLQVDL 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556489810 606 GGEK-RNVFSGIRSAYPdPQVLIGRQTVMVANLAPRKMRFGISEGMVMAAGPGGKdIFLLSPDEGAKPGQQVK 677
Cdd:PRK12267 578 GEEEpRQIVSGIAKFYP-PEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGK-LTLLTVDKEVPNGSKVK 648
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
7-373 |
5.56e-123 |
|
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: 367.90 E-value: 5.56e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGI-------------SPEQM 73
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 74 IAEMSQEHQTDFAGFDISYD--NYHSTHSDENRELSELIYTRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkcks 151
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 152 pdqygdncevcgatyspteliepksvvsgatpvmRDSEHFFFDLPSFSEMLQAWTRSGA-LQEQVANKMQEWFESGLQqW 230
Cdd:cd00668 137 ----------------------------------RITEQWFFDMPKFKEKLLKALRRGKiVPEHVKNRMEAWLESLLD-W 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 231 DISRDApYFGFEIPNapgKYFYVWLDAPIGYMGSFKNLCDKRgdtvsfdeyWKKDSTAELYHFIGKDIVYFHSLFWPAML 310
Cdd:cd00668 182 AISRQR-YWGTPLPE---DVFDVWFDSGIGPLGSLGYPEEKE---------WFKDSYPADWHLIGKDILRGWANFWITML 248
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556489810 311 EGSNFR-KPTNLFVHGYVTVN-GAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDL 373
Cdd:cd00668 249 VALFGEiPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLA-PYGDDIRL 312
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
6-538 |
3.53e-106 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 331.85 E-value: 3.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTDF 85
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 86 AGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckspdqygdnCEVCGAT 165
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 166 YSPTELIEPKSV--VSGATPVMRDSEHFFFDLPSFSEMLQAW--TRSGALQ-EQVANKMQEWFESGLQQWDISR---DAp 237
Cdd:PRK11893 132 YTESELIEDGYRcpPTGAPVEWVEEESYFFRLSKYQDKLLELyeANPDFIQpASRRNEVISFVKSGLKDLSISRtnfDW- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 238 yfGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTVSFDEYWKKDStaelyHFIGKDIVYFHSLFWPAMLEGSNFRK 317
Cdd:PRK11893 211 --GIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELLAELFNKYWPADV-----HLIGKDILRFHAVYWPAFLMAAGLPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 318 PTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRyYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 397
Cdd:PRK11893 284 PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVR-YFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 398 AGFIAKRFDGVLSA----ELADPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEgrDAD 473
Cdd:PRK11893 363 LSMIAKNFDGKVPEpgalTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTD--PER 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556489810 474 LQAICTMGLNMFRVLMTWLKPVLPQLAARAEAFLNTE----LTWDAIQQPLLSHKVNTFK--ALYNRIEMK 538
Cdd:PRK11893 441 LATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEedenRDFAALSWGRLAPGTTLPKpePIFPRLEEE 511
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
6-677 |
3.85e-97 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 316.72 E-value: 3.85e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 6 KKILVTCALPYANGSIHLGHMLEHI-QADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTD 84
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 85 FAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKSPDQYGDNCEVC 162
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 163 GATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQ-VANKMQ---EWFESGLQQWDISRD--- 235
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGwSQNAIQttnAWLRDGLKPRCITRDlkw 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 236 ---APYFGFEipnapGKYFYVWLDAPIGYMGSFKNLcdkrgdTVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEG 312
Cdd:PLN02610 257 gvpVPLEKYK-----DKVFYVWFDAPIGYVSITACY------TPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 313 S--NFRKPTNLFVHGYVTVNGAKMSKSRG----------TFIKASTWlnhfdadslRYYYtakLSSR--IDDIDLNLEDF 378
Cdd:PLN02610 326 TgeNWTMMKTISVTEYLNYEGGKFSKSKGvgvfgndakdTNIPVEVW---------RYYL---LTNRpeVSDTLFTWADL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 379 VQRVNADIVNKVVNLASRNAGFIAKR----FDGVLsAELADPELYKTFTDAAAAVG-------EAWESREFGKAIREIMA 447
Cdd:PLN02610 394 QAKLNSELLNNLGNFINRVLSFIAKPpgagYGSVI-PDAPGAESHPLTKKLAEKVGklveqyvEAMEKVKLKQGLKTAMS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 448 LADVANRYVDEQAPWVVAKQegrDADLQAI---CTMGLnmFRVLMTWLKPVLPQLAARAEAFLNTELT------------ 512
Cdd:PLN02610 473 ISSEGNAYLQESQFWKLYKE---DKPSCAIvvkTSVGL--VYLLACLLEPFMPSFSKEVLKQLNLPPEslslsdekgeva 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 513 -----WDAIQQpllSHKVNTFKALYNRIEMKQVEALVE----------------------------------ASKEEVKA 553
Cdd:PLN02610 548 rakrpWELVPA---GHKIGTPEPLFKELKDEEVEAYREkfagsqadraaraeaaeakklakqlkkkalsdggKKKQGKKA 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 554 ATAPVTGPLADDPIqetitfdDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQvLIGRQTV 632
Cdd:PLN02610 625 GGGGKSKAAAEREI-------DVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGApRTVVSGLVKYIPLEE-MQNRKVC 696
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 556489810 633 MVANLAPRKMRFGISEGMVMAAGPG-GKDIFLLSPDEGAKPGQQVK 677
Cdd:PLN02610 697 VLCNLKPAAMRGIKSQAMVLAASNSdHTKVELVEPPESAAVGERVT 742
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
541-677 |
1.31e-58 |
|
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273059 [Multi-domain] Cd Length: 137 Bit Score: 193.80 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 541 EALVEASKEE-VKAATAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSA 619
Cdd:TIGR00399 1 DKKIEELKLKgAKKKEKKDEGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAGY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 556489810 620 YPdPQVLIGRQTVMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDEGAKPGQQVK 677
Cdd:TIGR00399 81 YT-PEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK 137
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-572 |
6.99e-55 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 198.01 E-value: 6.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 5 AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQMIAEMSQEHQTD 84
Cdd:PLN02224 68 ADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 85 FAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkspDQYGDNcevcga 164
Cdd:PLN02224 148 WKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDE------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 165 tyspTELIEPKSVVSGATP-VMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVA---NKMQEWFESGLQQWDISRDAPYFG 240
Cdd:PLN02224 203 ----KELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSyrlNEVQSWIKSGLRDFSISRALVDWG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 241 FEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDTVSFDEYWKKDstaelYHFIGKDIVYFHSLFWPAMLEGSNFRKPTN 320
Cdd:PLN02224 279 IPVPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPAS-----LHLIGKDILRFHAVYWPAMLMSAGLELPKM 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 321 LFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRiDDIDLNLEDFVQRVNADIVNKVVNLASRNAGF 400
Cdd:PLN02224 354 VFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 401 IAKR------FDGVLSAElaDPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANRYVDEQAPWVVAKQEGRDADL 474
Cdd:PLN02224 433 LKKNcestlvEDSTVAAE--GVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 475 QAI-CTMGLNMFRVLMTWLKPVLPQLAARAEAFLN------TELTWDAIQQPLLS--HKVNTFKALYNRIEMKQvealvE 545
Cdd:PLN02224 511 AAKdLVIILEVMRVIAVALSPIAPCLSLRIYSQLGysedqfNSITWSDTKWGGLKggQVMEQASPVFARIELNP-----E 585
|
570 580
....*....|....*....|....*..
gi 556489810 546 ASKEEVKAATAPVTGPLADDPIQETIT 572
Cdd:PLN02224 586 KEEDEKKPKVGKKTGKAKVKVVEQTPT 612
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
571-677 |
7.84e-50 |
|
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.
Pssm-ID: 239199 [Multi-domain] Cd Length: 105 Bit Score: 168.83 E-value: 7.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 571 ITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPdPQVLIGRQTVMVANLAPRKMRFGISEGM 650
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYP-PEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100
....*....|....*....|....*..
gi 556489810 651 VMAAGPGGKdIFLLSPDEGAKPGQQVK 677
Cdd:cd02800 80 ILAAEDGGK-LKLLTPDEEVEPGSRVS 105
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
375-507 |
2.87e-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: 143.78 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 375 LEDFVQRVNADIVNKVVNLASRNAGFIAKRFDGvlsAELADPELYKTFTDAAAAVGEAWESREFGKAIREIMALADVANR 454
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGG---LTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 556489810 455 YVDEQAPWVVAKQEGRDAdLQAICTMGLNMFRVLMTWLKPVLPQLAARAEAFL 507
Cdd:cd07957 78 YIDETAPWKLAKEEDPER-LATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
562-677 |
2.01e-29 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 124.58 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 562 LADDPIQETITFDDFAKVD----LRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQV---LIGRQTVMV 634
Cdd:COG0073 21 LAEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYAGDKVpeaLVGAQVPGV 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 556489810 635 ANLAPRKMRFGISEGMVMAA---GPGGKDIFLLSPDEGAKPGQQVK 677
Cdd:COG0073 101 VNLKPRKIRGVESEGMLCSAeelGLGEDHDGILELPEDAPPGDDAE 146
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
581-675 |
7.83e-29 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 110.41 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 581 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQvLIGRQTVMVANLAPRKMRFGISEGMVMAAGP-GG 658
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEpRQIVSGAVNVYPPEE-LVGRLVVVVANLKPAKLRGVESEGMILSAEElDG 79
|
90
....*....|....*..
gi 556489810 659 KDIFLLSPDEGAKPGQQ 675
Cdd:pfam01588 80 GSVGLLEPPADVPPGTK 96
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
581-676 |
9.77e-28 |
|
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.
Pssm-ID: 239066 [Multi-domain] Cd Length: 99 Bit Score: 107.22 E-value: 9.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 581 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQVLIGRQTVMVANLAPRKMRFGISEGMVMAA---GP 656
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKpRQIVSGAANVYP-PEELVGKKVVVAVNLKPKKLRGVESEGMLLSAeelGL 79
|
90 100
....*....|....*....|
gi 556489810 657 GGKDIFLLSPDEGAKPGQQV 676
Cdd:cd02153 80 EEGSVGILELPEDAPVGDRI 99
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
571-676 |
3.81e-22 |
|
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.
Pssm-ID: 239197 [Multi-domain] Cd Length: 107 Bit Score: 91.53 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 571 ITFDDFAKVDLRVALIENAE-FVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQVLIGRQTVMVANLAPRKMRFGISEG 649
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEdFPEARKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*..
gi 556489810 650 MVMAAGPGGKDIFLLSPDEGAKPGQQV 676
Cdd:cd02798 81 LVLGADDEGGEVVLLVPDREVPNGAKV 107
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-359 |
1.10e-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: 93.47 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPEQM----IAEMSQehQ 82
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWteynIKKMKE--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 83 TDFAGFDISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkCKSPDQYGDNcevc 162
Cdd:cd00812 79 LKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW-------------------CKLLDQWFLK---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 163 gatYSPTELIEpksvvsgatpvmrdsehfffDLPSFSEMLQAWTrsgalqEQVANKMQEWFesglqqwDISRDApYFGFE 242
Cdd:cd00812 136 ---YSETEWKE--------------------KLLKDLEKLDGWP------EEVRAMQENWI-------GCSRQR-YWGTP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 243 IPnapgkYFYV---WLDAPIgYMGSF---KNLCDKRGDTVSFD----EYWkkdSTAELYHFiGKDIVYFH---SLFWPAM 309
Cdd:cd00812 179 IP-----WTDTmesLSDSTW-YYARYtdaHNLEQPYEGDLEFDreefEYW---YPVDIYIG-GKEHAPNHllySRFNHKA 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 556489810 310 L--EGSNFRK-PTNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 359
Cdd:cd00812 249 LfdEGLVTDEpPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLY 301
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
574-676 |
2.03e-19 |
|
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.
Pssm-ID: 239198 [Multi-domain] Cd Length: 105 Bit Score: 83.82 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 574 DDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPDPQvLIGRQTVMVANLAPRKMRfGI-SEGMV 651
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEpRTIVSGLVKFVPLEQ-MQNRLVVVLCNLKPRKMR-GVkSQGMV 78
|
90 100
....*....|....*....|....*.
gi 556489810 652 MAAGPGGKDIF-LLSPDEGAKPGQQV 676
Cdd:cd02799 79 LCASNADHEKVeLLEPPEGAKPGERV 104
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
569-676 |
5.96e-18 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 79.87 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 569 ETITFDDFAKVDLRVALIENAEFVEGSDKL-LRLTLDLGGEkrnvfSGIR--SA----YPDPQVLIGRQTVMVANLAPRK 641
Cdd:PRK10089 2 ETITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEE-----IGVKqsSAqitpHYTPEELIGKQVVAVVNFPPKQ 76
|
90 100 110
....*....|....*....|....*....|....*
gi 556489810 642 MRFGISEGMVMAAGPGGKDIFLLSPDEGAKPGQQV 676
Cdd:PRK10089 77 IAGFMSEVLVLGFEDEDGEVVLLTPDRPVPNGVKL 111
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
15-359 |
7.25e-16 |
|
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: 79.20 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGISPEQMIAEMS--------------- 78
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMGiaefnakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 79 ---QEHQTDFAGFDISYDNYHSTHSDENRElSELiytrlkengfiknRTISQLYdpEKGMflpdrfvkgtcpkckspdqy 155
Cdd:cd00818 90 vdeQEEQFQRLGVWVDWENPYKTMDPEYME-SVW-------------WVFKQLH--EKGL-------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 156 gdncevcgatyspteliepksVVSGATPVM-----RDSEHFFFDLPSF-SEMLQAWTRSGALQEQVANKMQEWFEsGLQQ 229
Cdd:cd00818 134 ---------------------LYRGYKVVPwpliyRATPQWFIRVTKIkDRLLEANDKVNWIPEWVKNRFGNWLE-NRRD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 230 WDISRDApYFGFEIP----NAPGKY--------FYVWLDApiGYMGSFKNlcDKRGDTVSFDEYWKKDSTAElyhfiGKD 297
Cdd:cd00818 192 WCISRQR-YWGTPIPvwycEDCGEVlvrrvpdvLDVWFDS--GSMPYAQL--HYPFENEDFEELFPADFILE-----GSD 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556489810 298 IV--YFHSLfwpaMLEGS-NFRKP--TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 359
Cdd:cd00818 262 QTrgWFYSL----LLLSTaLFGKApyKNVIVHGFVlDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
15-373 |
7.52e-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: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGISPE-----------QMIAEMSQEHQ 82
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 83 TDFA------GFDISYDNYHSTHSDENRELSELIYTRLKENGFIknrtisqlydpEKGMFLPDRfvkgtCPKCKSPDQyg 156
Cdd:cd00817 90 GKIReqlkrlGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLI-----------YRDNRLVNW-----CPKLRTAIS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 157 dNCEVCGATYSPtelIEPKSvvsgatpvmrdSEHFFFDLPSFSEMLQAWTRSGALQ---EQVANKMQEWFESgLQQWDIS 233
Cdd:cd00817 152 -DIEVCSRSGDV---IEPLL-----------KPQWFVKVKDLAKKALEAVKEGDIKfvpERMEKRYENWLEN-IRDWCIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 234 RDApYFGFEIPnapgkyfyVWLDAPIGY--------------MGSFKNLCDK---RGDTVSFDE------------YWKK 284
Cdd:cd00817 216 RQL-WWGHRIP--------AWYCKDGGHwvvareedeaidkaAPEACVPCGGeelKQDEDVLDTwfssslwpfstlGWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 285 DsTAELYHFI-------GKDIVYfhslFWPA--MLEGSNF--RKP-TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHF 351
Cdd:cd00817 287 E-TKDLKKFYptsllvtGHDIIF----FWVArmIMRGLKLtgKLPfKEVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGY 361
|
410 420
....*....|....*....|..
gi 556489810 352 DADSLRyYYTAKLSSRIDDIDL 373
Cdd:cd00817 362 GADALR-FTLASAATQGRDINL 382
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
15-80 |
9.84e-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: 68.57 E-value: 9.84e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGISpEQMIAEMSQE 80
Cdd:COG0060 55 PYANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIELKVeKELGIK-KKDIEKVGIA 120
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
15-152 |
8.38e-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: 62.04 E-value: 8.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGISPEQMIAEMSQEHQTDFAGFDISYd 93
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVeKKLGIKEKKTRHKYGREEFREKCREWKME- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556489810 94 nYHSTHSDENRELSELI-----YTRLKEnGFIKN--RTISQLYDpeKGMFLPDRFVKGTCPKCKSP 152
Cdd:pfam00133 111 -YADEIRKQFRRLGRSIdwdreYFTMDP-ELEAAvwEVFVRLHD--KGLIYRGKKLVNWSPALNTA 172
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
15-120 |
1.12e-09 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 61.75 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNF-ICADDaHGTPIMLKAQ-QLGISP----------------EQMIAE 76
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcreltDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 556489810 77 MSQEHQTdfAGFDISYDNYHSTHSDENRELSELIYTRLKENGFI 120
Cdd:PRK13208 126 FRELWRR--LGLSVDWSLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
15-65 |
1.81e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 60.94 E-value: 1.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQ 65
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
15-120 |
1.62e-08 |
|
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: 58.15 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGISPE-----------QMIAEMSQEH- 81
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESg 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 556489810 82 -----QTDFAGFDISYDNYHSTHSDENRELSELIYTRLKENGFI 120
Cdd:TIGR00422 122 gtiknQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLI 165
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
292-377 |
4.71e-06 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 48.90 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 292 HFIGKDIVYFHSLFWPAMLEGSNFRKPTNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY-YTAKLSSRID 369
Cdd:pfam01406 211 HGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFlLSVHYRSPLD 290
|
....*...
gi 556489810 370 DIDLNLED 377
Cdd:pfam01406 291 FSEELLEQ 298
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
320-360 |
4.81e-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: 47.96 E-value: 4.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556489810 320 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 360
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
295-445 |
7.94e-06 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 49.10 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 295 GKDIVYFHSLF-------------WPAMLEgsnfrkptnlfVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYT 361
Cdd:PRK12300 537 GKDLIPNHLTFfifnhvaifpeekWPRGIV-----------VNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 362 --AKLSSridDIDLNlEDFVQRVnADIVNKVVNLASRNAGFIAKRFDGVLSAELADpELYKTFTDAAaavgEAWESREFG 439
Cdd:PRK12300 606 ssAELLQ---DADWR-EKEVESV-RRQLERFYELAKELIEIGGEEELRFIDKWLLS-RLNRIIKETT----EAMESFQTR 675
|
....*.
gi 556489810 440 KAIREI 445
Cdd:PRK12300 676 DAVQEA 681
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
320-360 |
2.45e-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: 2.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 556489810 320 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 360
Cdd:COG0215 251 RYWMHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
15-96 |
3.14e-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: 44.39 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFI-CADDAHGTpIMLKAQQLGISPEQMIAEMSQEHQTDFA-GFDISY 92
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIaLIDDAGGL-IGDPANKKGENAKAFVERWIERIKEDVEyMFLQAA 84
|
....
gi 556489810 93 DNYH 96
Cdd:cd00802 85 DFLL 88
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
19-46 |
4.97e-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: 46.58 E-value: 4.97e-05
10 20
....*....|....*....|....*....
gi 556489810 19 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 46
Cdd:COG0525 48 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 75
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
19-46 |
5.68e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 46.64 E-value: 5.68e-05
10 20
....*....|....*....|....*....
gi 556489810 19 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 46
Cdd:PRK05729 49 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 76
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-46 |
1.06e-04 |
|
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: 1.06e-04
10 20 30
....*....|....*....|....*....|...
gi 556489810 14 LPYANGSIHLGHMLEHIQADVWVRYQRMRGHEV 46
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
15-142 |
6.46e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 43.27 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 15 PYANGS-IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGISPE----QMIAEMSQEHQTdfAGFD 89
Cdd:PLN02563 119 PYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKittlKNIARFRSQLKS--LGFS 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 556489810 90 ISYDNYHSTHSDENRELSELIYTRLKENGFIKNRTISQLYDPEKGMFLPDRFV 142
Cdd:PLN02563 197 YDWDREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV 249
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
295-445 |
8.23e-04 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.78 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 295 GKDIVYFhslfWPA--MLEGSNFRK--P-TNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRI 368
Cdd:PRK05729 480 GFDIIFF----WVArmIMMGLHFTGqvPfKDVYIHGLVrDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAA-LASPG 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 369 DDIDLNLEdfvqRVNA--DIVNKVVNlASRnagFIAKRFDGVLSAELADPELYKT--------FTDAAAAVGEAWESREF 438
Cdd:PRK05729 555 RDIRFDEE----RVEGyrNFANKLWN-ASR---FVLMNLEGADVGELPDPEELSLadrwilsrLNRTVAEVTEALDKYRF 626
|
....*..
gi 556489810 439 GKAIREI 445
Cdd:PRK05729 627 DEAARAL 633
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
21-152 |
1.09e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.16 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 21 IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPImlkaqqLGIS--------------------PEQMIAEM--- 77
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPI------LGIAeriargdpetielykslygiPEEELEKFkdp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 78 -------SQEHQTDF--AGFDIsyD---NYHSThsDEnrELSELI---YTRLKENGFIknrtisqlydpekgmflpdrfV 142
Cdd:PRK12300 75 eyiveyfSEEAKEDMkrIGYSI--DwrrEFTTT--DP--EYSKFIewqFRKLKEKGLI---------------------V 127
|
170
....*....|....*
gi 556489810 143 KGT-----CPKCKSP 152
Cdd:PRK12300 128 KGShpvryCPNDNNP 142
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
15-77 |
2.86e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 40.86 E-value: 2.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556489810 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGISPEQMIAEM 77
Cdd:PLN02882 47 PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIdKKLGIKRRDDVLKM 110
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
301-497 |
6.46e-03 |
|
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: 39.68 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 301 FHSLFWPA-MLEGSN-FRkptNLFVHGYVtV--NGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAklSSRIDDIDLNlE 376
Cdd:COG0060 571 FYSSLLTStALFGRApYK---NVLTHGFV-LdeDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS--SDYWGDLRFS-D 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 377 DFVQRVnADIVNKVVN----LASRNAGFIAKRfDGVLSAELadPE-----LYKTfTDAAAAVGEAWESREFGKAIREIMA 447
Cdd:COG0060 644 EILKEV-RDVYRRLRNtyrfLLANLDDFDPAE-DAVPYEDL--PEldrwiLSRL-NELIKEVTEAYDNYDFHRAYRALHN 718
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 556489810 448 LA--DVANRYVDeqapwvVAKQ----EGRD--ADLQAICTMgLNMFRVLMTWLKPVLP 497
Cdd:COG0060 719 FCveDLSNWYLD------ISKDrlytEAADslDRRAAQTTL-YEVLETLVRLLAPILP 769
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
581-674 |
8.67e-03 |
|
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.
Pssm-ID: 239196 [Multi-domain] Cd Length: 103 Bit Score: 36.33 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556489810 581 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGirsaypDPQVLIGrQTVMVAN----------LAPRKMRFGISEG 649
Cdd:cd02796 1 VVVGKVLEVEPHPNADKLNVCKVDIGENKpLQIVCG------APNVRAG-DKVVVALpgavlpgglkIKKRKLRGVESEG 73
|
90 100 110
....*....|....*....|....*....|
gi 556489810 650 MVMAA---GPGGKD--IFLLSPDegAKPGQ 674
Cdd:cd02796 74 MLCSAkelGLGEDSdgIIELPED--APVGT 101
|
|
| |
