|
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: 1314.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 85
Cdd:PRK00133 2 RKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 86 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:PRK00133 82 AGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKGTCPKCGAEDQYGDNCEVCGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 166 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAW-TRSGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEIP 244
Cdd:PRK00133 162 YSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWiTRSGELQPNVANKMKEWLEEGLQDWDISRDAPYFGFEIP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 245 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDsVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 324
Cdd:PRK00133 242 GAPGKVFYVWLDAPIGYISSTKNLCDKRGG-LDWDEYWKKDSDTELYHFIGKDIIYFHTLFWPAMLEGAGYRLPTNVFAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 325 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 404
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLDFNWEDFQQRVNSELVGKVVNFASRTAGFINKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 405 FDGVLASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdlQAICSMGINL 484
Cdd:PRK00133 401 FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQDGERL--QAVCSVGLNL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 485 FRVLMTYLKPVLPKLTERAEAFLN-TELTWDGIQQPLLGHKVNPFKALYNRIDMRQVEALVEASKE--EVKAAAAPVTGP 561
Cdd:PRK00133 479 FRALAIYLKPVLPELAERAEAFLNlEELTWDDAQQPLAGHPINKFKILFTRIEDKQIEALIEASKEaaAAKAAAAAAAAP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 562 LADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYpDPQALIGRHTIMVANLAPRK 641
Cdd:PRK00133 559 LAEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIKSAY-DPEELVGKLVVMVANLAPRK 637
|
650 660 670
....*....|....*....|....*....|....*.
gi 1352185596 642 MRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK 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: 872.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 85
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 86 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGAT 165
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEGTCPKCGAEDAYGDQCENCGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 166 YSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRS-GALQEQVANKMQEWFESGLQQWDISRDAPYfGFEIP 244
Cdd:COG0143 161 LEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEEnPDIQPEVRNEVLSWLKEGLQDLSISRDFDW-GIPVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 245 NAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWkKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH 324
Cdd:COG0143 240 GDPGKVFYVWFDALIGYISATKGYADDRGLPEDFEKYW-PAPDTELVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 325 GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINKR 404
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLRE-VPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 405 FDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDAdLQAICSM 480
Cdd:COG0143 398 FDGKVpepgELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDEDPER-LATVLYT 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352185596 481 GINLFRVLMTYLKPVLPKLTERAEAFLN---TELTWDGIQQPLL-GHKVNPFKALYNRIDMRQVEALV 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: 791.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 8 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 87
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 88 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 167
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSEDARGDHCEVCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 168 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTR----SGALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 243
Cdd:TIGR00398 161 PTELINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRknpeSGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 244 PNAPGKYFYVWLDAPIGYMGSfknLCDKRGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 323
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISS---LGILSGDTEDWKKWWNNDEDAELIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 324 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDLNLEDFVQRVNADIVNKVVNLASRNAGFINK 403
Cdd:TIGR00398 318 HGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKER-PLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 404 RFDGVLASELA----DPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQAICS 479
Cdd:TIGR00398 397 YFNGVLPSEDItdeeDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLKELLAVCS 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352185596 480 MginLFRVLMTYLKPVLPKLTERAEAFLNTELTWDGIQQPLLGHKVNPFKALYNRID 536
Cdd:TIGR00398 477 M---LIRVLSILLYPIMPKLSEKILKFLNFELEWDFKLKLLEGHKLNKAEPLFSKIE 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: 625.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 8 ILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFAG 87
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 88 FNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPKCKSPDQYGDNCEVCGATYS 167
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTCPHCGSEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 168 PTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGA--LQEQVANKMQEWFESGLQQWDISRDAPYfGFEIPN 245
Cdd:pfam09334 161 PTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEENNpeWPENVKNMVLEWLKEGLKDRAISRDLDW-GIPVPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 246 APGKYFYVWLDAPIGYMGSFKNLCdkrGDSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVHG 325
Cdd:pfam09334 240 AEGKVFYVWLDAPIGYISATKELS---GNEEKWKEWWPNDPDTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352185596 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 |
4.58e-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: 430.03 E-value: 4.58e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDFA 86
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 87 GFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPdrfvkgtcpkckspdqygdncevcgaty 166
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP---------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 167 spteliepksvvsgatpVMRDSEHFFFDLPSFSEMLQAWTRS---GALQEQVANKMQEWFESGLQQWDISRDAPYFGFEI 243
Cdd:cd00814 133 -----------------EWREEEHYFFRLSKFQDRLLEWLEKnpdFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 244 PNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSvsfdeYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFV 323
Cdd:cd00814 196 PLDPGKVIYVWFDALIGYISATGYYNEEWGNS-----WWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1352185596 324 HGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKlSSRIDDID 372
Cdd:cd00814 271 HGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRE-RPEGKDSD 318
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
6-677 |
1.24e-129 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 397.25 E-value: 1.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 85
Cdd:PRK12267 4 KTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 86 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI-KNR-------------TISQLYDPEKgmflpdrfvkgtCPKCKS 151
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIyKGEyegwycvscetffTESQLVDGGK------------CPDCGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 152 PdqygdncevcgatyspTELIEPKSvvsgatpvmrdsehFFFDLPSFSEMLQAWTRSGA---LQEQVANKMQEWF-ESGL 227
Cdd:PRK12267 152 E----------------VELVKEES--------------YFFRMSKYQDRLLEYYEENPdfiQPESRKNEMINNFiKPGL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 228 QQWDISRDAPYFGFEIPNAPGKYFYVWLDA------PIGYMGSfknlcdkrgDSVSFDEYWKKDstaelYHFIGKDIVYF 301
Cdd:PRK12267 202 EDLSISRTSFDWGIPVPFDPKHVVYVWIDAllnyitALGYGSD---------DDELFKKFWPAD-----VHLVGKDILRF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 302 HSLFWPAMLEGSNFRKPSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYytakLSSRI---DDIDLNLEDF 378
Cdd:PRK12267 268 HAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYY----LLREVpfgSDGDFSPEAL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 379 VQRVNADIVNKVVNLASRNAGFINKRFDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR 454
Cdd:PRK12267 344 VERINSDLANDLGNLLNRTVAMINKYFDGEIpapgNVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANK 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 455 YVDEQAPWVVAKQEGRDADLQAICSMGINLFRVLMTYLKPVLPKLTER---------AEAFLNTELTWDGIQqplLGHKV 525
Cdd:PRK12267 424 YIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKifeqlgleeELTSWESLLEWGGLP---AGTKV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 526 NPFKALYNRIDmrqVEALVEASKEEVKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDL 605
Cdd:PRK12267 501 AKGEPLFPRID---VEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEITIDDFDKVELRVAEVLEAEKVEKSDKLLKLQVDL 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1352185596 606 GGEK-RNVFSGIRSAYPdPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKdIFLLSPDAGAKPGHQVK 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 |
6.07e-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: 378.30 E-value: 6.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGI-------------TPEQM 73
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 74 IGEMSQEHQTDFAGFNISYD--NYHSTHSEENRQLSELIYSRLKENGFIKNRTISQlydpekgmflpdrfvkgtcpkcks 151
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 152 pdqygdncevcgatyspteliepksvvsgatpvmRDSEHFFFDLPSFSEMLQAWTRSGA-LQEQVANKMQEWFESGLQqW 230
Cdd:cd00668 137 ----------------------------------RITEQWFFDMPKFKEKLLKALRRGKiVPEHVKNRMEAWLESLLD-W 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 231 DISRDApYFGFEIPNapgKYFYVWLDAPIGYMGSFKNLCDKRgdsvsfdeyWKKDSTAELYHFIGKDIVYFHSLFWPAML 310
Cdd:cd00668 182 AISRQR-YWGTPLPE---DVFDVWFDSGIGPLGSLGYPEEKE---------WFKDSYPADWHLIGKDILRGWANFWITML 248
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1352185596 311 EGSNFR-KPSNLFVHGYVTVN-GAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLsSRIDDIDL 373
Cdd:cd00668 249 VALFGEiPPKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLA-PYGDDIRL 312
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
6-536 |
2.32e-102 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 321.83 E-value: 2.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 6 KKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTDF 85
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 86 AGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkckspdqygdnCEVCGAT 165
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWY-----------------------------CVRCEEF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 166 YSPTELIEPKSV--VSGATPVMRDSEHFFFDLPSFSEMLQAW--TRSGALQ-EQVANKMQEWFESGLQQWDISR---DAp 237
Cdd:PRK11893 132 YTESELIEDGYRcpPTGAPVEWVEEESYFFRLSKYQDKLLELyeANPDFIQpASRRNEVISFVKSGLKDLSISRtnfDW- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 238 yfGFEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDStaelyHFIGKDIVYFHSLFWPAMLEGSNFRK 317
Cdd:PRK11893 211 --GIPVPGDPKHVIYVWFDALTNYLTALGYPDDEELLAELFNKYWPADV-----HLIGKDILRFHAVYWPAFLMAAGLPL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 318 PSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRyYYTAKLSSRIDDIDLNLEDFVQRVNADIVNKVVNLASRN 397
Cdd:PRK11893 284 PKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDAVR-YFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 398 AGFINKRFDGVL----ASELADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANRYVDEQAPWVVAKQEgrDAD 473
Cdd:PRK11893 363 LSMIAKNFDGKVpepgALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTD--PER 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352185596 474 LQAICSMGINLFRVLMTYLKPVLPKLTERAEAFLNTE---------LTWDGIQQpllGHKVNPFKALYNRID 536
Cdd:PRK11893 441 LATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEedenrdfaaLSWGRLAP---GTTLPKPEPIFPRLE 509
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
6-677 |
5.28e-94 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 308.25 E-value: 5.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 6 KKILVTCALPYANGSIHLGHMLEHI-QADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 84
Cdd:PLN02610 17 RNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 85 FAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFVKGTCPK--CKSPDQYGDNCEVC 162
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADRLVEGTCPTegCNYDSARGDQCEKC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 163 GATYSPTELIEPKSVVSGATPVMRDSEHFFFDLPSFSEMLQAWTRSGALQEQ-VANKMQ---EWFESGLQQWDISRD--- 235
Cdd:PLN02610 177 GKLLNPTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYINETSVAGGwSQNAIQttnAWLRDGLKPRCITRDlkw 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 236 ---APYFGFEipnapGKYFYVWLDAPIGYMGSFKNLcdkrgdSVSFDEYWKKDSTAELYHFIGKDIVYFHSLFWPAMLEG 312
Cdd:PLN02610 257 gvpVPLEKYK-----DKVFYVWFDAPIGYVSITACY------TPEWEKWWKNPENVELYQFMGKDNVPFHTVMFPSTLLG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 313 S--NFRKPSNLFVHGYVTVNGAKMSKSRG----------TFIKASTWlnhfdadslRYYYtakLSSR--IDDIDLNLEDF 378
Cdd:PLN02610 326 TgeNWTMMKTISVTEYLNYEGGKFSKSKGvgvfgndakdTNIPVEVW---------RYYL---LTNRpeVSDTLFTWADL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 379 VQRVNADIVNKVVNLASRNAGFI----NKRFDGVL--ASELADPQLYKTFtdaAEVIG-------EAWESREFGKAVREI 445
Cdd:PLN02610 394 QAKLNSELLNNLGNFINRVLSFIakppGAGYGSVIpdAPGAESHPLTKKL---AEKVGklveqyvEAMEKVKLKQGLKTA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 446 MALADLANRYVDEQAPWVVAKQegrDADLQAI---CSMGinLFRVLMTYLKPVLPKLTERAEAFLNTELTW--------- 513
Cdd:PLN02610 471 MSISSEGNAYLQESQFWKLYKE---DKPSCAIvvkTSVG--LVYLLACLLEPFMPSFSKEVLKQLNLPPESlslsdekge 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 514 -DGIQQP--LL--GHKVNPFKALYNRIDMRQVEALVE----------------------------------ASKEEVKAA 554
Cdd:PLN02610 546 vARAKRPweLVpaGHKIGTPEPLFKELKDEEVEAYREkfagsqadraaraeaaeakklakqlkkkalsdggKKKQGKKAG 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 555 AAPVTGPLADDPIqetitfdDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQALIGRHTIM 633
Cdd:PLN02610 626 GGGKSKAAAEREI-------DVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGApRTVVSGLVKYIP-LEEMQNRKVCV 697
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1352185596 634 VANLAPRKMRFGISEGMVMAAGPG-GKDIFLLSPDAGAKPGHQVK 677
Cdd:PLN02610 698 LCNLKPAAMRGIKSQAMVLAASNSdHTKVELVEPPESAAVGERVT 742
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
541-677 |
6.48e-62 |
|
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: 202.66 E-value: 6.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 541 EALVEASKEE-VKAAAAPVTGPLADDPIQETITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSA 619
Cdd:TIGR00399 1 DKKIEELKLKgAKKKEKKDEGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAGY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352185596 620 YPdPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQVK 677
Cdd:TIGR00399 81 YT-PEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFLLSPDQEAIAGERIK 137
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
5-572 |
3.93e-55 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 198.78 E-value: 3.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 5 AKKILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQMIGEMSQEHQTD 84
Cdd:PLN02224 68 ADTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 85 FAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtCPKCkspDQYGDNcevcga 164
Cdd:PLN02224 148 WKDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLY----------------CVNC---EEYKDE------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 165 tyspTELIEPKSVVSGATP-VMRDSEHFFFDLPSFSEMLQAWTRSGALQEQVA---NKMQEWFESGLQQWDISRDAPYFG 240
Cdd:PLN02224 203 ----KELLENNCCPVHQMPcVARKEDNYFFALSKYQKPLEDILAQNPRFVQPSyrlNEVQSWIKSGLRDFSISRALVDWG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 241 FEIPNAPGKYFYVWLDAPIGYMGSFKNLCDKRGDSVSFDEYWKKDstaelYHFIGKDIVYFHSLFWPAMLEGSNFRKPSN 320
Cdd:PLN02224 279 IPVPDDDKQTIYVWFDALLGYISALTEDNKQQNLETAVSFGWPAS-----LHLIGKDILRFHAVYWPAMLMSAGLELPKM 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 321 LFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAKLSSRiDDIDLNLEDFVQRVNADIVNKVVNLASRNAGF 400
Cdd:PLN02224 354 VFGHGFLTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFG-NDGDYSEDRFIKIVNAHLANTIGNLLNRTLGL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 401 INKRFDGVLASELADPQLYKTFTDAAEVIGEA----WESREFGKAVREIMALADLANRYVDEQAPWVVAKQEGRDADLQA 476
Cdd:PLN02224 433 LKKNCESTLVEDSTVAAEGVPLKDTVEKLVEKaqtnYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 477 I-CSMGINLFRVLMTYLKPVLPKLTERAEAFLN-----------TELTWDGIQQPLLGHKVNPfkaLYNRIDMRQvealv 544
Cdd:PLN02224 513 KdLVIILEVMRVIAVALSPIAPCLSLRIYSQLGysedqfnsitwSDTKWGGLKGGQVMEQASP---VFARIELNP----- 584
|
570 580
....*....|....*....|....*...
gi 1352185596 545 EASKEEVKAAAAPVTGPLADDPIQETIT 572
Cdd:PLN02224 585 EKEEDEKKPKVGKKTGKAKVKVVEQTPT 612
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
571-677 |
1.16e-49 |
|
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: 168.45 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 571 ITFDDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPdPQALIGRHTIMVANLAPRKMRFGISEGM 650
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYP-PEELVGKKVVVVANLKPRKLRGVESQGM 79
|
90 100
....*....|....*....|....*..
gi 1352185596 651 VMAAGPGGKdIFLLSPDAGAKPGHQVK 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 |
1.40e-39 |
|
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: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 375 LEDFVQRVNADIVNKVVNLASRNAGFINKRFDGVLAselADPQLYKTFTDAAEVIGEAWESREFGKAVREIMALADLANR 454
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTE---EDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANK 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1352185596 455 YVDEQAPWVVAKQEGRDAdLQAICSMGINLFRVLMTYLKPVLPKLTERAEAFL 507
Cdd:cd07957 78 YIDETAPWKLAKEEDPER-LATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
548-673 |
6.52e-30 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 126.12 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 548 KEEVKAAAAPVTgpLADDPIQETITFDDFAKVD----LRVALIENAEFVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPD- 622
Cdd:COG0073 9 KEYVDLDLSPEE--LAEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYAGd 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1352185596 623 --PQALIGRHTIMVANLAPRKMRFGISEGMVMAA---GPGGKDIFLLSPDAGAKPG 673
Cdd:COG0073 87 kvPEALVGAQVPGVVNLKPRKIRGVESEGMLCSAeelGLGEDHDGILELPEDAPPG 142
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
581-675 |
1.26e-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: 112.72 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 581 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQALIGRHTIMVANLAPRKMRFGISEGMVMAAGP-GG 658
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEpRQIVSGAVNVYP-PEELVGRLVVVVANLKPAKLRGVESEGMILSAEElDG 79
|
90
....*....|....*..
gi 1352185596 659 KDIFLLSPDAGAKPGHQ 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 |
4.34e-27 |
|
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: 105.29 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 581 LRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQALIGRHTIMVANLAPRKMRFGISEGMVMAA---GP 656
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKpRQIVSGAANVYP-PEELVGKKVVVAVNLKPKKLRGVESEGMLLSAeelGL 79
|
90 100
....*....|....*....|
gi 1352185596 657 GGKDIFLLSPDAGAKPGHQV 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 |
1.69e-21 |
|
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: 89.61 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 571 ITFDDFAKVDLRVALIENAE-FVEGSDKLLRLTLDLGGEKRNVFSGIRSAYPDPQALIGRHTIMVANLAPRKMRFGISEG 649
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEdFPEARKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*..
gi 1352185596 650 MVMAAGPGGKDIFLLSPDAGAKPGHQV 676
Cdd:cd02798 81 LVLGADDEGGEVVLLVPDREVPNGAKV 107
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-359 |
3.82e-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: 91.93 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 7 KILVTCALPYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLGITPEQM----IGEMSQehQ 82
Cdd:cd00812 1 KFYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWteynIKKMKE--Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 83 TDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYdpekgmflpdrfvkgtcpkCKSPDQYGDNcevc 162
Cdd:cd00812 79 LKRMGFSYDWRREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNW-------------------CKLLDQWFLK---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 163 gatYSPTELIEpksvvsgatpvmrdsehfffDLPSFSEMLQAWTrsgalqEQVANKMQEWFesglqqwDISRDApYFGFE 242
Cdd:cd00812 136 ---YSETEWKE--------------------KLLKDLEKLDGWP------EEVRAMQENWI-------GCSRQR-YWGTP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 243 IPnapgkYFYV---WLDAPIgYMGSF---KNLCDKRGDSVSFD----EYWkkdSTAELYHFiGKDIVYFH---SLFWPAM 309
Cdd:cd00812 179 IP-----WTDTmesLSDSTW-YYARYtdaHNLEQPYEGDLEFDreefEYW---YPVDIYIG-GKEHAPNHllySRFNHKA 248
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1352185596 310 L--EGSNFRK-PSNLFVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 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 |
4.78e-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: 82.66 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 574 DDFAKVDLRVALIENAEFVEGSDKLLRLTLDLGGEK-RNVFSGIRSAYPdPQALIGRHTIMVANLAPRKMRfGI-SEGMV 651
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEpRTIVSGLVKFVP-LEQMQNRLVVVLCNLKPRKMR-GVkSQGMV 78
|
90 100
....*....|....*....|....*.
gi 1352185596 652 MAAGPGGKDIF-LLSPDAGAKPGHQV 676
Cdd:cd02799 79 LCASNADHEKVeLLEPPEGAKPGERV 104
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
569-676 |
1.12e-16 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 76.02 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 569 ETITFDDFAKVDLRVALIENAEFVEGSDKL-LRLTLDLGGEkrnvfSGIR--SA----YPDPQALIGRHTIMVANLAPRK 641
Cdd:PRK10089 2 ETITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEE-----IGVKqsSAqitpHYTPEELIGKQVVAVVNFPPKQ 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1352185596 642 MRFGISEGMVMAAGPGGKDIFLLSPDAGAKPGHQV 676
Cdd:PRK10089 77 IAGFMSEVLVLGFEDEDGEVVLLTPDRPVPNGVKL 111
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
15-359 |
1.68e-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: 78.43 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMS--------------- 78
Cdd:cd00818 10 PYANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVeKELGISGKKDIEKMGiaefnakcrefalry 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 79 ---QEHQTDFAGFNISYDNYHSTHSEEnrqlseliysrlkengFIKN--RTISQLYdpEKGMflpdrfvkgtcpkckspd 153
Cdd:cd00818 90 vdeQEEQFQRLGVWVDWENPYKTMDPE----------------YMESvwWVFKQLH--EKGL------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 154 qygdncevcgatyspteliepksVVSGATPVM-----RDSEHFFFDLPSF-SEMLQAWTRSGALQEQVANKMQEWFEsGL 227
Cdd:cd00818 134 -----------------------LYRGYKVVPwpliyRATPQWFIRVTKIkDRLLEANDKVNWIPEWVKNRFGNWLE-NR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 228 QQWDISRDApYFGFEIP----NAPGKY--------FYVWLDApiGYMGSFKNlcDKRGDSVSFDEYWKKDSTAElyhfiG 295
Cdd:cd00818 190 RDWCISRQR-YWGTPIPvwycEDCGEVlvrrvpdvLDVWFDS--GSMPYAQL--HYPFENEDFEELFPADFILE-----G 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 296 KDIV--YFHSLfwpaMLEGS-NFRKPS--NLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYY 359
Cdd:cd00818 260 SDQTrgWFYSL----LLLSTaLFGKAPykNVIVHGFVlDEDGRKMSKSLGNYVDPQEVVDKYGADALRLW 325
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
15-373 |
2.64e-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: 78.06 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEHQ 82
Cdd:cd00817 10 PNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGIATQVVVEkKLGIEGKtrhdlgreeflEKCWEWKEESG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 83 TDFA------GFNISYDNYHSTHSEENRQLSELIYSRLKENGFIknrtisqlydpEKGMFLPDRfvkgtCPKCKSPDQyg 156
Cdd:cd00817 90 GKIReqlkrlGASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLI-----------YRDNRLVNW-----CPKLRTAIS-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 157 dNCEVCGATYSPtelIEPKSvvsgatpvmrdSEHFFFDLPSFSEMLQAWTRSGALQ---EQVANKMQEWFESgLQQWDIS 233
Cdd:cd00817 152 -DIEVCSRSGDV---IEPLL-----------KPQWFVKVKDLAKKALEAVKEGDIKfvpERMEKRYENWLEN-IRDWCIS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 234 RDApYFGFEIPnapgkyfyVWLDAPIGY--------------MGSFKNLCDK---RGDSVSFDE------------YWKK 284
Cdd:cd00817 216 RQL-WWGHRIP--------AWYCKDGGHwvvareedeaidkaAPEACVPCGGeelKQDEDVLDTwfssslwpfstlGWPE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 285 DsTAELYHFI-------GKDIVYfhslFWPA--MLEGSNF--RKP-SNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHF 351
Cdd:cd00817 287 E-TKDLKKFYptsllvtGHDIIF----FWVArmIMRGLKLtgKLPfKEVYLHGLVrDEDGRKMSKSLGNVIDPLDVIDGY 361
|
410 420
....*....|....*....|..
gi 1352185596 352 DADSLRyYYTAKLSSRIDDIDL 373
Cdd:cd00817 362 GADALR-FTLASAATQGRDINL 382
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
15-80 |
1.12e-11 |
|
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: 1.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITpEQMIGEMSQE 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 |
1.75e-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: 63.97 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEMSQEHQTDFAGFNISYd 93
Cdd:pfam00133 32 PNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVeKKLGIKEKKTRHKYGREEFREKCREWKME- 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352185596 94 nYHSTHSEENRQLSELI-----YSRLKEnGFIKN--RTISQLYDpeKGMFLPDRFVKGTCPKCKSP 152
Cdd:pfam00133 111 -YADEIRKQFRRLGRSIdwdreYFTMDP-ELEAAvwEVFVRLHD--KGLIYRGKKLVNWSPALNTA 172
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
15-120 |
1.90e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 64.06 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNF-ICADDaHGTPIMLKAQ-QLGITP----------------EQMIGE 76
Cdd:PRK13208 47 PTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFpQGWDD-NGLPTERKVEkYYGIRKddisreefielcreltDEDEKK 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1352185596 77 MSQEHQTdfAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI 120
Cdd:PRK13208 126 FRELWRR--LGLSVDWSLEYQTISPEYRRISQKSFLDLYKKGLI 167
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
15-120 |
9.50e-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: 62.00 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQ-QLGITPE-----------QMIGEMSQEH- 81
Cdd:TIGR00422 42 PNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGIATQVKVEkKLGAEGKtkhdlgreefrEKIWEWKEESg 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1352185596 82 -----QTDFAGFNISYDNYHSTHSEENRQLSELIYSRLKENGFI 120
Cdd:TIGR00422 122 gtiknQIKRLGASLDWSRERFTMDEGLSKAVKEAFVRLYEKGLI 165
|
|
| 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 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQ 65
Cdd:PLN02843 41 PYANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIELKVLQ 91
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
320-360 |
5.42e-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: 5.42e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1352185596 320 NLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 360
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLAL 201
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
292-377 |
1.27e-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: 47.75 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 292 HFIGKDIVYFHSLFWPAMLEGSNFRKPSNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYY-YTAKLSSRID 369
Cdd:pfam01406 211 HGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFlLSVHYRSPLD 290
|
....*...
gi 1352185596 370 DIDLNLED 377
Cdd:pfam01406 291 FSEELLEQ 298
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
295-399 |
1.47e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 48.33 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 295 GKDIVYFHSLF-------------WPAMLEgsnfrkpsnlfVHGYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYT 361
Cdd:PRK12300 537 GKDLIPNHLTFfifnhvaifpeekWPRGIV-----------VNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT 605
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1352185596 362 --AKLSSridDIDLNlEDFVQRVnADIVNKVVNLASRNAG 399
Cdd:PRK12300 606 ssAELLQ---DADWR-EKEVESV-RRQLERFYELAKELIE 640
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
317-360 |
2.31e-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: 2.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1352185596 317 KPSNLFVH-GYVTVNGAKMSKSRGTFIKASTWLNHFDADSLRYYY 360
Cdd:COG0215 248 PFARYWMHnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFL 292
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
19-46 |
4.37e-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: 4.37e-05
10 20
....*....|....*....|....*....
gi 1352185596 19 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 46
Cdd:COG0525 48 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 75
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
19-46 |
5.26e-05 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 46.64 E-value: 5.26e-05
10 20
....*....|....*....|....*....
gi 1352185596 19 GSIHLGHMLEH-IQaDVWVRYQRMRGHEV 46
Cdd:PRK05729 49 GSLHMGHALNNtLQ-DILIRYKRMQGYNT 76
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
15-100 |
8.41e-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: 43.24 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFI-CADDAHGTPIMLKAQQLGITP---EQMIGEMSQ--EHQTDFAGF 88
Cdd:cd00802 6 ITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIaLIDDAGGLIGDPANKKGENAKafvERWIERIKEdvEYMFLQAAD 85
|
90
....*....|..
gi 1352185596 89 NISYDNYHSTHS 100
Cdd:cd00802 86 FLLLYETECDIH 97
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
14-46 |
9.95e-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: 45.81 E-value: 9.95e-05
10 20 30
....*....|....*....|....*....|...
gi 1352185596 14 LPYANGSIHLGHMLEHIQADVWVRYQRMRGHEV 46
Cdd:COG0495 41 FPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
15-142 |
3.13e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 44.04 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 15 PYANGS-IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQLG----ITPEQMIGEMSQEHQTdfAGFN 89
Cdd:PLN02563 119 PYPSGAgLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGthpkITTLKNIARFRSQLKS--LGFS 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1352185596 90 ISYDNYHSTHSEENRQLSELIYSRLKENGFIKNRTISQLYDPEKGMFLPDRFV 142
Cdd:PLN02563 197 YDWDREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEV 249
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
301-457 |
9.81e-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: 42.37 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 301 FHSLFWPA-MLEGSN-FRkpsNLFVHGYVtV--NGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAklSSRIDDIdlnle 376
Cdd:COG0060 571 FYSSLLTStALFGRApYK---NVLTHGFV-LdeDGRKMSKSLGNVVDPQEVIDKYGADILRLWVAS--SDYWGDL----- 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 377 dfvqRVNADIVNkvvnlasRNAGFINK-----RFdgvLASELA--DPQ----------------LYKTFTDAAEVIgEAW 433
Cdd:COG0060 640 ----RFSDEILK-------EVRDVYRRlrntyRF---LLANLDdfDPAedavpyedlpeldrwiLSRLNELIKEVT-EAY 704
|
170 180
....*....|....*....|....*.
gi 1352185596 434 ESREFGKAVREIMALA--DLANRYVD 457
Cdd:COG0060 705 DNYDFHRAYRALHNFCveDLSNWYLD 730
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
295-501 |
1.24e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 42.01 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 295 GKDIVYFhslfWPA--MLEGSNFRK--P-SNLFVHGYV-TVNGAKMSKSRGTFIKASTWLNHFDADSLRYYYTAkLSSRI 368
Cdd:PRK05729 480 GFDIIFF----WVArmIMMGLHFTGqvPfKDVYIHGLVrDEQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAA-LASPG 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 369 DDIDLNLEdfvqRVNadivnkvvnlASRNagFINK-----RF----DGVLASELADPQLYKTFTD----------AAEVI 429
Cdd:PRK05729 555 RDIRFDEE----RVE----------GYRN--FANKlwnasRFvlmnLEGADVGELPDPEELSLADrwilsrlnrtVAEVT 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352185596 430 gEAWESREFGKAVREIMALA--DLANRYVdEqapwvVAKQEGRDADLQAICSMginLFRVLMTYLK---PVLPKLTE 501
Cdd:PRK05729 619 -EALDKYRFDEAARALYEFIwnEFCDWYL-E-----LAKPVLQEAAKRATRAT---LAYVLEQILRllhPFMPFITE 685
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
15-77 |
1.62e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 42.02 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352185596 15 PYANGSIHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKA-QQLGITPEQMIGEM 77
Cdd:PLN02882 47 PFATGLPHYGHILAGTIKDIVTRYQSMTGHHVTRRFGWDCHGLPVEYEIdKKLGIKRRDDVLKM 110
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
21-152 |
5.69e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 39.85 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 21 IHLGHMLEHIQADVWVRYQRMRGHEVNFICADDAHGTPIMLKAQQL---------------GItPEQMIGEM-------- 77
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFPMAFHVTGTPILGIAERIargdpetielykslyGI-PEEELEKFkdpeyive 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352185596 78 --SQEHQTDF--AGFNIsyD---NYHSThSEENRQLSELIYSRLKENGFIknrtisqlydpekgmflpdrfVKGT----- 145
Cdd:PRK12300 80 yfSEEAKEDMkrIGYSI--DwrrEFTTT-DPEYSKFIEWQFRKLKEKGLI---------------------VKGShpvry 135
|
....*..
gi 1352185596 146 CPKCKSP 152
Cdd:PRK12300 136 CPNDNNP 142
|
|
| |
