|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
44-581 |
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: 554.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 44 RAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQ 123
Cdd:COG0143 2 KFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRG---HDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 124 LFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF---- 193
Cdd:COG0143 79 LFEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEgtcpkcGAEDAYGDQCencg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 ----------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQaITPEpFHHVVLQWLDEELPDLSVSRRsshLH 263
Cdd:COG0143 159 atleptelinPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQPE-VRNEVLSWLKEGLQDLSISRD---FD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 264 WGIPVPGDDSQTIYVWLDALVNYLT-VIGYPN-----AEFKSWWPATS----HIIGKDILKFHAIYWPAFLLGAGMSPPQ 333
Cdd:COG0143 234 WGIPVPGDPGKVFYVWFDALIGYISaTKGYADdrglpEDFEKYWPAPDtelvHFIGKDIIRFHAIIWPAMLMAAGLPLPK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 334 RICVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC--- 410
Cdd:COG0143 314 KVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTlsm 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 411 TAKRINpsetypafcttcfpsepGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRH 490
Cdd:COG0143 394 IHKYFD-----------------GKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDET 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 491 APWKLNWESpvDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSASERSLGELYFLPRfyghpcpfEGRRLG 570
Cdd:COG0143 457 APWKLAKDE--DPERLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLP--------AGHKIG 526
|
570
....*....|.
gi 24308436 571 PETgLLFPRLD 581
Cdd:COG0143 527 KPE-PLFPRIE 536
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
46-581 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 521.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:PRK11893 4 YITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDV---FFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 126 QEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVTQqpgpsGDSFPVslESGHPVSW 205
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIE-----DGYRCP--PTGAPVEW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 206 TKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRrsSHLHWGIPVPGDDSQTIYVWLDALVN 285
Cdd:PRK11893 154 VEEESYFFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISR--TNFDWGIPVPGDPKHVIYVWFDALTN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 286 YLTVIGYPNAE------FKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPR 359
Cdd:PRK11893 232 YLTALGYPDDEellaelFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 360 TCLNRYTVDGFRYFLLRQgVP-NWDCDYYDEKVVKLLNSELADALGGLLNRcTAKRINPSetypafCTTCFPSEPGLVgp 438
Cdd:PRK11893 312 DLVDEYGVDAVRYFLLRE-IPfGQDGDFSREAFINRINADLANDLGNLAQR-TLSMIAKN------FDGKVPEPGALT-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 439 svraqAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWEspvDAPWLGTVLHVALECLR 518
Cdd:PRK11893 382 -----EADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKT---DPERLATVLYTLLEVLR 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308436 519 VFGTLLQPVTPSLADKLLSRLGVSASE-RSLGELYFLPRFYGHPcpfegrrLGPETGlLFPRLD 581
Cdd:PRK11893 454 GIAVLLQPVMPELAAKILDQLGVEEDEnRDFAALSWGRLAPGTT-------LPKPEP-IFPRLE 509
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
44-386 |
2.34e-170 |
|
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: 486.27 E-value: 2.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 44 RAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQ 123
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRG---YDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 124 LFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEakvtqqpgpsgdsfpvslesghpv 203
Cdd:cd00814 78 LFKWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPE------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 204 sWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRRSSHlhWGIPVPGDDSQTIYVWLDAL 283
Cdd:cd00814 134 -WREEEHYFFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITRDLFD--WGIPVPLDPGKVIYVWFDAL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 284 VNYLTVIGYPNAE------FKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVD 357
Cdd:cd00814 211 IGYISATGYYNEEwgnswwWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVD 290
|
330 340
....*....|....*....|....*....
gi 24308436 358 PRTCLNRYTVDGFRYFLLRQGVPNWDCDY 386
Cdd:cd00814 291 PDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
45-410 |
1.75e-147 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 430.56 E-value: 1.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 45 AYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQL 124
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDV---LFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHRED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 125 FQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF----- 193
Cdd:pfam09334 78 FKKFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEgtcphcGSEDARGDQCencgr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 ---------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWL-RGNPQAitPEPFHHVVLQWLDEELPDLSVSRRsshLH 263
Cdd:pfam09334 158 hleptelinPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIeENNPEW--PENVKNMVLEWLKEGLKDRAISRD---LD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 264 WGIPVPGDDSQTIYVWLDALVNYLTVIGYP---NAEFKSWWPATS-----HIIGKDILKFHAIYWPAFLLGAGMSPPQRI 335
Cdd:pfam09334 233 WGIPVPGAEGKVFYVWLDAPIGYISATKELsgnEEKWKEWWPNDPdtelvHFIGKDIIYFHTIFWPAMLLGAGYRLPTTV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24308436 336 CVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC 410
Cdd:pfam09334 313 FAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
46-543 |
1.20e-146 |
|
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: 434.11 E-value: 1.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:TIGR00398 2 LITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEV---LFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 126 QEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF------ 193
Cdd:TIGR00398 79 KWLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEgtcpkcGSEDARGDHCevcgrh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 --------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITP-EPFHHVVLQWLDEELPDLSVSRRSSHlhW 264
Cdd:TIGR00398 159 leptelinPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPaSNVKNKAQNWLKGGLKDLAITRDLVY--W 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 265 GIPVPGDDSQTIYVWLDALVNYLTVIGYPNA---EFKSWWPATS-----HIIGKDILKFHAIYWPAFLLGAGMSPPQRIC 336
Cdd:TIGR00398 237 GIPVPNDPNKVVYVWFDALIGYISSLGILSGdteDWKKWWNNDEdaeliHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 337 VHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC---TAK 413
Cdd:TIGR00398 317 SHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTlgfIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 414 RINpsetypafcttcfpsepGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPW 493
Cdd:TIGR00398 397 YFN-----------------GVLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPW 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24308436 494 KLNWESPVDApwlgTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSA 543
Cdd:TIGR00398 460 ELFKQSPRLK----ELLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFEL 505
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
44-581 |
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: 554.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 44 RAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQ 123
Cdd:COG0143 2 KFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRG---HDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 124 LFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF---- 193
Cdd:COG0143 79 LFEKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEgtcpkcGAEDAYGDQCencg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 ----------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQaITPEpFHHVVLQWLDEELPDLSVSRRsshLH 263
Cdd:COG0143 159 atleptelinPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQPE-VRNEVLSWLKEGLQDLSISRD---FD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 264 WGIPVPGDDSQTIYVWLDALVNYLT-VIGYPN-----AEFKSWWPATS----HIIGKDILKFHAIYWPAFLLGAGMSPPQ 333
Cdd:COG0143 234 WGIPVPGDPGKVFYVWFDALIGYISaTKGYADdrglpEDFEKYWPAPDtelvHFIGKDIIRFHAIIWPAMLMAAGLPLPK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 334 RICVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC--- 410
Cdd:COG0143 314 KVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTlsm 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 411 TAKRINpsetypafcttcfpsepGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRH 490
Cdd:COG0143 394 IHKYFD-----------------GKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDET 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 491 APWKLNWESpvDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSASERSLGELYFLPRfyghpcpfEGRRLG 570
Cdd:COG0143 457 APWKLAKDE--DPERLATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLP--------AGHKIG 526
|
570
....*....|.
gi 24308436 571 PETgLLFPRLD 581
Cdd:COG0143 527 KPE-PLFPRIE 536
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
46-581 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 521.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:PRK11893 4 YITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDV---FFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 126 QEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVTQqpgpsGDSFPVslESGHPVSW 205
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIE-----DGYRCP--PTGAPVEW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 206 TKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRrsSHLHWGIPVPGDDSQTIYVWLDALVN 285
Cdd:PRK11893 154 VEEESYFFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISR--TNFDWGIPVPGDPKHVIYVWFDALTN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 286 YLTVIGYPNAE------FKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPR 359
Cdd:PRK11893 232 YLTALGYPDDEellaelFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 360 TCLNRYTVDGFRYFLLRQgVP-NWDCDYYDEKVVKLLNSELADALGGLLNRcTAKRINPSetypafCTTCFPSEPGLVgp 438
Cdd:PRK11893 312 DLVDEYGVDAVRYFLLRE-IPfGQDGDFSREAFINRINADLANDLGNLAQR-TLSMIAKN------FDGKVPEPGALT-- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 439 svraqAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWEspvDAPWLGTVLHVALECLR 518
Cdd:PRK11893 382 -----EADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKT---DPERLATVLYTLLEVLR 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308436 519 VFGTLLQPVTPSLADKLLSRLGVSASE-RSLGELYFLPRFYGHPcpfegrrLGPETGlLFPRLD 581
Cdd:PRK11893 454 GIAVLLQPVMPELAAKILDQLGVEEDEnRDFAALSWGRLAPGTT-------LPKPEP-IFPRLE 509
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
46-581 |
4.59e-177 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 515.89 E-value: 4.59e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:PRK12267 7 YITTPIYYPNGKPHIGHAYTTIAADALARYKRLQG---YDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 126 QEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAK-VTQQPGPsgdsfpvslESGHPVS 204
Cdd:PRK12267 84 KKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQlVDGGKCP---------DCGREVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 205 WTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEE-LPDLSVSRRSshLHWGIPVPGDDSQTIYVWLDAL 283
Cdd:PRK12267 155 LVKEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPgLEDLSISRTS--FDWGIPVPFDPKHVVYVWIDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 284 VNYLTVIGYPN---AEFKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRT 360
Cdd:PRK12267 233 LNYITALGYGSdddELFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 361 CLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRCTAKrinpSETYpafcttcfpsEPGLVGPSV 440
Cdd:PRK12267 313 LVDRYGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAM----INKY----------FDGEIPAPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 441 RAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNwESPVDAPWLGTVLHVALECLRVF 520
Cdd:PRK12267 379 NVTEFDEELIALAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLA-KDEGKKERLATVMYHLAESLRKV 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308436 521 GTLLQPVTPSLADKLLSRLGVSASERSLGELYF---LPrfyghpcpfEGRRLGPETGlLFPRLD 581
Cdd:PRK12267 458 AVLLSPFMPETSKKIFEQLGLEEELTSWESLLEwggLP---------AGTKVAKGEP-LFPRID 511
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
44-386 |
2.34e-170 |
|
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: 486.27 E-value: 2.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 44 RAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQ 123
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRG---YDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 124 LFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEakvtqqpgpsgdsfpvslesghpv 203
Cdd:cd00814 78 LFKWLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPE------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 204 sWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRRSSHlhWGIPVPGDDSQTIYVWLDAL 283
Cdd:cd00814 134 -WREEEHYFFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITRDLFD--WGIPVPLDPGKVIYVWFDAL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 284 VNYLTVIGYPNAE------FKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVD 357
Cdd:cd00814 211 IGYISATGYYNEEwgnswwWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVD 290
|
330 340
....*....|....*....|....*....
gi 24308436 358 PRTCLNRYTVDGFRYFLLRQGVPNWDCDY 386
Cdd:cd00814 291 PDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
45-410 |
1.75e-147 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 430.56 E-value: 1.75e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 45 AYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQL 124
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDV---LFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHRED 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 125 FQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF----- 193
Cdd:pfam09334 78 FKKFNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEgtcphcGSEDARGDQCencgr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 ---------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWL-RGNPQAitPEPFHHVVLQWLDEELPDLSVSRRsshLH 263
Cdd:pfam09334 158 hleptelinPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIeENNPEW--PENVKNMVLEWLKEGLKDRAISRD---LD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 264 WGIPVPGDDSQTIYVWLDALVNYLTVIGYP---NAEFKSWWPATS-----HIIGKDILKFHAIYWPAFLLGAGMSPPQRI 335
Cdd:pfam09334 233 WGIPVPGAEGKVFYVWLDAPIGYISATKELsgnEEKWKEWWPNDPdtelvHFIGKDIIYFHTIFWPAMLLGAGYRLPTTV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24308436 336 CVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC 410
Cdd:pfam09334 313 FAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
46-543 |
1.20e-146 |
|
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: 434.11 E-value: 1.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTaatRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:TIGR00398 2 LITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEV---LFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 126 QEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF------ 193
Cdd:TIGR00398 79 KWLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEgtcpkcGSEDARGDHCevcgrh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 --------PVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITP-EPFHHVVLQWLDEELPDLSVSRRSSHlhW 264
Cdd:TIGR00398 159 leptelinPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPaSNVKNKAQNWLKGGLKDLAITRDLVY--W 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 265 GIPVPGDDSQTIYVWLDALVNYLTVIGYPNA---EFKSWWPATS-----HIIGKDILKFHAIYWPAFLLGAGMSPPQRIC 336
Cdd:TIGR00398 237 GIPVPNDPNKVVYVWFDALIGYISSLGILSGdteDWKKWWNNDEdaeliHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 337 VHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRC---TAK 413
Cdd:TIGR00398 317 SHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTlgfIKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 414 RINpsetypafcttcfpsepGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPW 493
Cdd:TIGR00398 397 YFN-----------------GVLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPW 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 24308436 494 KLNWESPVDApwlgTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSA 543
Cdd:TIGR00398 460 ELFKQSPRLK----ELLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFEL 505
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
47-545 |
8.52e-105 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 328.98 E-value: 8.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 47 FTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTAatrFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLFQ 126
Cdd:PLN02224 73 LTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVI---FITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 127 EAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVTQQpgpsgDSFPVSlesGHPVSWT 206
Cdd:PLN02224 150 DLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLEN-----NCCPVH---QMPCVAR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 207 KEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRrsSHLHWGIPVPGDDSQTIYVWLDALVNY 286
Cdd:PLN02224 222 KEDNYFFALSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSGLRDFSISR--ALVDWGIPVPDDDKQTIYVWFDALLGY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 287 LTVIGYPNAE------FKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRT 360
Cdd:PLN02224 300 ISALTEDNKQqnletaVSFGWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 361 CLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRctakrinpseTYPAFCTTCfpsEPGLVGPSV 440
Cdd:PLN02224 380 LVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNR----------TLGLLKKNC---ESTLVEDST 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 441 RAqAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWESPVDAPWLGTVLHVALECLRVF 520
Cdd:PLN02224 447 VA-AEGVPLKDTVEKLVEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKQGGVSAEEAAKDLVIILEVMRVI 525
|
490 500
....*....|....*....|....*
gi 24308436 521 GTLLQPVTPSLADKLLSRLGVSASE 545
Cdd:PLN02224 526 AVALSPIAPCLSLRIYSQLGYSEDQ 550
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
53-584 |
8.70e-86 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 280.50 E-value: 8.70e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 53 YVNAAPHIGHLYSALLADALCRHRRLRGPSTAatrFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLFQEAGISC 132
Cdd:PRK00133 12 YANGPIHLGHLVEYIQADIWVRYQRMRGHEVL---FVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFGISF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 133 TDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVT------QQPGPSGDSF------------- 193
Cdd:PRK00133 89 DNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKgtcpkcGAEDQYGDNCevcgatyspteli 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 194 -PVSLESGH-PVswTKE-ENYIFRLSQFRKPLQRWLrGNPQAITPEpfhhV---VLQWLDEELPDLSVSRrssHLHW-GI 266
Cdd:PRK00133 169 nPKSAISGAtPV--LKEsEHFFFKLPRFEEFLKEWI-TRSGELQPN----VankMKEWLEEGLQDWDISR---DAPYfGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 267 PVPGDDSQTIYVWLDAlvnyltVIGY-----------PNAEFKSWWPATS-----HIIGKDILKFHAIYWPAFLLGAGMS 330
Cdd:PRK00133 239 EIPGAPGKVFYVWLDA------PIGYisstknlcdkrGGLDWDEYWKKDSdtelyHFIGKDIIYFHTLFWPAMLEGAGYR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 331 PPQRICVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNW-DCDY----YDEKVvkllNSELADALGG 405
Cdd:PRK00133 313 LPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIdDLDFnwedFQQRV----NSELVGKVVN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 406 LLNRC---TAKRinpsetypafcttcFPSEpglvgpsVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQ 482
Cdd:PRK00133 389 FASRTagfINKR--------------FDGK-------LPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 483 TNGFVQRHAPWKLNWESPVDApwlGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSAserslgelyflPRFYGHPC 562
Cdd:PRK00133 448 ANKYVDDNEPWKLAKQDGERL---QAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEE-----------LTWDDAQQ 513
|
570 580
....*....|....*....|..
gi 24308436 563 PFEGRRLGPeTGLLFPRLDQSR 584
Cdd:PRK00133 514 PLAGHPINK-FKILFTRIEDKQ 534
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
46-376 |
1.03e-62 |
|
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: 209.20 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTAatrFSTGTDEHGLKIQQAAATAGL-------------APTE 112
Cdd:cd00668 3 YVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVP---FLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 113 LCDRVSEQFQQLFQEAGIS--CTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGwycasdecflpeakvtqqpgpsg 190
Cdd:cd00668 80 FVEEMSGEHKEDFRRLGISydWSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV----------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 191 dsfpvslesghpvswTKEENYIFRLSQFRKPLQRWLRGNPqaITPEPFHHVVLQWLdEELPDLSVSRRsshLHWGIPVPG 270
Cdd:cd00668 137 ---------------RITEQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWL-ESLLDWAISRQ---RYWGTPLPE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 271 DdsqTIYVWLDALVNYLTVIGYP--NAEFKSWWPATSHIIGKDILKFHAIYWPAFLLGA-GMSPPQRICVHSHWTV-CGQ 346
Cdd:cd00668 196 D---VFDVWFDSGIGPLGSLGYPeeKEWFKDSYPADWHLIGKDILRGWANFWITMLVALfGEIPPKNLLVHGFVLDeGGQ 272
|
330 340 350
....*....|....*....|....*....|
gi 24308436 347 KMSKSLGNVVDPRTCLNRYTVDGFRYFLLR 376
Cdd:cd00668 273 KMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
395-539 |
1.31e-33 |
|
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: 124.52 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 395 LNSELADALGGLLNRCTAkrinpsetypaFCTTCFPsepGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALE 474
Cdd:cd07957 1 INSELANNLGNLVNRTLN-----------MASKYFG---GVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALE 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24308436 475 AVSSCVRQTNGFVQRHAPWKLNWESpvDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRL 539
Cdd:cd07957 67 EIMELARAANKYIDETAPWKLAKEE--DPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
48-550 |
1.88e-32 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 132.98 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 48 TTPIFYVNAAPHIGHLYSALL-ADALCRHRRLRGPSTAatrFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLFQ 126
Cdd:PLN02610 22 TSALPYVNNVPHLGNIIGCVLsADVFARYCRLRGYNAI---YICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 127 EAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFL----------------------------- 177
Cdd:PLN02610 99 WFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLadrlvegtcptegcnydsargdqcekcgk 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 178 ---------PEAKVTQqpgpsgdSFPVSLESGH-----PVSWTKEENYIFRLSQfrkpLQRWLRGNPQAITpepfhhvvl 243
Cdd:PLN02610 179 llnptelidPKCKVCK-------NTPRIRDTDHlflelPLLKDKLVEYINETSV----AGGWSQNAIQTTN--------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 244 QWLDEELPDLSVSRrssHLHWGIPVP--GDDSQTIYVWLDALVNYLTVIGYPNAEFKSWWPATSHI-----IGKDILKFH 316
Cdd:PLN02610 239 AWLRDGLKPRCITR---DLKWGVPVPleKYKDKVFYVWFDAPIGYVSITACYTPEWEKWWKNPENVelyqfMGKDNVPFH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 317 AIYWPAFLLGAG-----MsppQRICVHSHWTVCGQKMSKS-----LGNVVDPRtclnRYTVDGFRYFLLRQGVPNWDCDY 386
Cdd:PLN02610 316 TVMFPSTLLGTGenwtmM---KTISVTEYLNYEGGKFSKSkgvgvFGNDAKDT----NIPVEVWRYYLLTNRPEVSDTLF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 387 YDEKVVKLLNSELADALGGLLNRC---TAKRINpsetypAFCTTCFPSEPGlvgpsvraqAEDYALVSAVATLPKQVADH 463
Cdd:PLN02610 389 TWADLQAKLNSELLNNLGNFINRVlsfIAKPPG------AGYGSVIPDAPG---------AESHPLTKKLAEKVGKLVEQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 464 Y----DNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWEspvDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRL 539
Cdd:PLN02610 454 YveamEKVKLKQGLKTAMSISSEGNAYLQESQFWKLYKE---DKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQL 530
|
570
....*....|.
gi 24308436 540 GVSASERSLGE 550
Cdd:PLN02610 531 NLPPESLSLSD 541
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
46-378 |
6.41e-24 |
|
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: 102.71 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 46 YFTTPIF-YVNAAPHIGHLYSALLADALCRHRRLRGPSTAatrFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQL 124
Cdd:cd00812 2 FYILVMFpYPSGALHVGHVRTYTIGDIIARYKRMQGYNVL---FPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 125 FQEAGIScTDF---IRTTEARHRVAVQHFWGVLKSRGLLYKGvyegwycasdecflpeakvtqqpgpsgdsfpvslesGH 201
Cdd:cd00812 79 LKRMGFS-YDWrreFTTCDPEYYKFTQWLFLKLYEKGLAYKK------------------------------------EA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 202 PVSWTKEEN-YIFRLSQ--FRKPLQRWLrgNPQAITPEPFHHVVLQWLDeelpdlsVSRRSshlHWGIPVPGDDsqTIYV 278
Cdd:cd00812 122 PVNWCKLLDqWFLKYSEteWKEKLLKDL--EKLDGWPEEVRAMQENWIG-------CSRQR---YWGTPIPWTD--TMES 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 279 WLDALVNYL--TVIGYPNA-----------EFKSWWPATSHIIGKDILKFH---AIYWPAFLLGAGMS---PPQRICVHS 339
Cdd:cd00812 188 LSDSTWYYAryTDAHNLEQpyegdlefdreEFEYWYPVDIYIGGKEHAPNHllySRFNHKALFDEGLVtdePPKGLIVQG 267
|
330 340 350
....*....|....*....|....*....|....*....
gi 24308436 340 HWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQG 378
Cdd:cd00812 268 MVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAA 306
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
53-380 |
8.57e-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: 78.81 E-value: 8.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 53 YVNAAPHIGHLYSALLADALCRHRRLRGpSTAATRFstGTDEHGLKI-----QQAAATAGLAPTEL--------C----D 115
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQG-YYVPRRP--GWDCHGLPIelkveKELGISGKKDIEKMgiaefnakCrefaL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 116 RVSEQFQQLFQEAGIsCTDF---IRTTEARHRVAVqhfWGVLKS---RGLLYKG---VYegW---YCASDECFLPEAKVT 183
Cdd:cd00818 88 RYVDEQEEQFQRLGV-WVDWenpYKTMDPEYMESV---WWVFKQlheKGLLYRGykvVP--WpliYRATPQWFIRVTKIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 184 QQpgpsgdsfpvSLESGHPVSWTKEENYifrlSQFRKplqrwlrgnpqaitpepfhhvvlqWLdEELPDLSVSR-RSshl 262
Cdd:cd00818 162 DR----------LLEANDKVNWIPEWVK----NRFGN------------------------WL-ENRRDWCISRqRY--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 263 hWGIPVP--------------GDDsqTIYVWLDALVNYLTVIGYP--NAEFKSWWPATSHIIGKDILK--FHAIywpaFL 324
Cdd:cd00818 200 -WGTPIPvwycedcgevlvrrVPD--VLDVWFDSGSMPYAQLHYPfeNEDFEELFPADFILEGSDQTRgwFYSL----LL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24308436 325 LGAGM--SPPQRICVhSHWTVC---GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVP 380
Cdd:cd00818 273 LSTALfgKAPYKNVI-VHGFVLdedGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
49-375 |
1.10e-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: 79.21 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 49 TPIFYVNAAPHIGHLYSALLADALCRHRRLRGpstAATRFSTGTDEHGLKIQ-----QAAATAGLAP-------TELC-- 114
Cdd:cd00817 7 TPPPNVTGSLHMGHALNNTIQDIIARYKRMKG---YNVLWPPGTDHAGIATQvvvekKLGIEGKTRHdlgreefLEKCwe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 115 ------DRVSEQFQQLfqeaGISC--TDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVtqqp 186
Cdd:cd00817 84 wkeesgGKIREQLKRL----GASVdwSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAISDIEV---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 187 gpsgdsfpvSLESGHPVS-WTKEENYIfRLSQFRKP-LQRWLRGNPQaITPEPFHHVVLQWLdEELPDLSVSRRsshLHW 264
Cdd:cd00817 156 ---------CSRSGDVIEpLLKPQWFV-KVKDLAKKaLEAVKEGDIK-FVPERMEKRYENWL-ENIRDWCISRQ---LWW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 265 GIPVP---GDDSQTIYV---------------------------------WLDALVNYLTVIGYPNA--EFKSWWPATSH 306
Cdd:cd00817 221 GHRIPawyCKDGGHWVVareedeaidkaapeacvpcggeelkqdedvldtWFSSSLWPFSTLGWPEEtkDLKKFYPTSLL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24308436 307 IIGKDILKFhaiyWPAFLLGAGMS-----PPQRICVHShwTVC---GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLL 375
Cdd:cd00817 301 VTGHDIIFF----WVARMIMRGLKltgklPFKEVYLHG--LVRdedGRKMSKSLGNVIDPLDVIDGYGADALRFTLA 371
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
345-476 |
2.03e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 63.67 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 345 GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLL--RQGVpnwdcDY-YDEKVV--------KLLN-SELADALGGllnrcTA 412
Cdd:PRK13208 531 GKKMSKSKGNVVTPEELLEKYGADAVRYWAAsaRLGS-----DTpFDEKQVkigrrlltKLWNaSRFVLHFSA-----DP 600
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24308436 413 KRINPSETYPAfcttcfpsepglvgpsvraqaeDYALVSAVATLPKQVADHYDNFRIYKALEAV 476
Cdd:PRK13208 601 EPDKAEVLEPL----------------------DRWILAKLAKVVEKATEALENYDFAKALEEI 642
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
227-374 |
1.39e-09 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 61.23 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 227 RGNPQaITPEPFHHVVLQWLdEELPDLSVSRRsshLHWGIPVP---GDDSQTIYV------------------------- 278
Cdd:TIGR00422 375 EGEIK-FVPKRMEKRYLNWL-RNIKDWCISRQ---LIWGHRIPvwyCKECGEVYVakeeplpddktntgpsveleqdtdv 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 279 ---WLDALVNYLTVIGYP--NAEFKSWWPATSHIIGKDILKFhaiyWPAFLLGAGMS-----PPQRICVHShwTVC---G 345
Cdd:TIGR00422 450 ldtWFSSSLWPFSTLGWPdeTKDLKKFYPTDLLVTGYDIIFF----WVARMIFRSLAltgqvPFKEVYIHG--LVRdeqG 523
|
170 180
....*....|....*....|....*....
gi 24308436 346 QKMSKSLGNVVDPRTCLNRYTVDGFRYFL 374
Cdd:TIGR00422 524 RKMSKSLGNVIDPLDVIEKYGADALRFTL 552
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
272-375 |
1.50e-08 |
|
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: 57.42 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 272 DSQTIYVWLDALVNYLTVIGYPNA---EFKSWWPATSHIIGKDILKFhaiyWPAFLLGAGM----SPPQRIcVHSHWTVC 344
Cdd:pfam00133 483 DEDVLDTWFSSGSWPFSTLGWPFVnteEFKKFFPADMLLEGSDQTRG----WFYRMIMLSTaltgSVPFKN-VLVHGLVR 557
|
90 100 110
....*....|....*....|....*....|....
gi 24308436 345 ---GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLL 375
Cdd:pfam00133 558 deqGRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
272-369 |
6.39e-08 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 55.68 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 272 DSQTIYVWLDALVNYLTVIGYPN--AEFKSWWPATSHIIGKDILKFhaiyWPAFLLGAGMS-----PPQRICVH-----S 339
Cdd:PLN02381 576 DPDVLDTWFSSGLFPLSVLGWPDdtDDLKAFYPTSVLETGHDILFF----WVARMVMMGMQlggdvPFRKVYLHpmirdA 651
|
90 100 110
....*....|....*....|....*....|
gi 24308436 340 HwtvcGQKMSKSLGNVVDPRTCLNRYTVDG 369
Cdd:PLN02381 652 H----GRKMSKSLGNVIDPLEVINGISLEG 677
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
345-476 |
1.92e-07 |
|
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: 54.29 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 345 GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVV-------KLLN-SELAdalggLLNRCTAkrin 416
Cdd:COG0525 520 GRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIKFDEERVEgyrnfanKLWNaSRFV-----LMNLEGF---- 590
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 417 psetypafcttcfpsEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAV 476
Cdd:COG0525 591 ---------------DPGLDPDPEELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQAL 635
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
48-125 |
2.55e-07 |
|
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: 50.17 E-value: 2.55e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24308436 48 TTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPStaaTRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLF 125
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYK---VRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDV 76
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
345-476 |
2.68e-07 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 53.57 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 345 GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVvkllnseladalggllnrctakrinpsETYPAF 424
Cdd:PRK05729 518 GRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFDEERV---------------------------EGYRNF 570
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24308436 425 CT-----------TCFPSEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAV 476
Cdd:PRK05729 571 ANklwnasrfvlmNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARAL 633
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
345-480 |
2.60e-06 |
|
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: 50.46 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 345 GQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQgvpnwdcDYYDEKVV--KLLNsELADALGGLLNrcTAK-------RI 415
Cdd:COG0060 601 GRKMSKSLGNVVDPQEVIDKYGADILRLWVASS-------DYWGDLRFsdEILK-EVRDVYRRLRN--TYRfllanldDF 670
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24308436 416 NPSETYPAFCttcfpSEPglvgpsvraqAED-YALvSAVATLPKQVADHYDNFRIYKALEAVSS-CV 480
Cdd:COG0060 671 DPAEDAVPYE-----DLP----------ELDrWIL-SRLNELIKEVTEAYDNYDFHRAYRALHNfCV 721
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
233-374 |
2.96e-06 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 50.32 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 233 ITPEPFHHVVLQWLdEELPDLSVSRRsshLHWG--IPV---PGDDSQTIYV----------------------------- 278
Cdd:PLN02943 432 IIPERFEKIYNHWL-SNIKDWCISRQ---LWWGhrIPVwyiVGKDCEEDYIvarsaeealekarekygkdveiyqdpdvl 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 279 --WLDALVNYLTVIGYPNA---EFKSWWPATSHIIGKDILKFhaiyWPAFLLGAGMSPPQRI---CVHSHWTV---CGQK 347
Cdd:PLN02943 508 dtWFSSALWPFSTLGWPDVsaeDFKKFYPTTVLETGHDILFF----WVARMVMMGIEFTGTVpfsYVYLHGLIrdsQGRK 583
|
170 180
....*....|....*....|....*..
gi 24308436 348 MSKSLGNVVDPRTCLNRYTVDGFRYFL 374
Cdd:PLN02943 584 MSKTLGNVIDPLDTIKEFGTDALRFTL 610
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
337-376 |
3.59e-06 |
|
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: 49.72 E-value: 3.59e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 24308436 337 VHSHW-TVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLR 376
Cdd:COG0215 254 MHNGFlTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLS 294
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
53-182 |
6.56e-06 |
|
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: 48.95 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 53 YVNAAPHIGHLYSALLADALCRHRRLRGPStaaTRFSTGTDEHGLKIQQA-----AATAGL--------APTELC----- 114
Cdd:pfam00133 33 NATGSLHIGHALAKTLKDIVIRYKRMKGYY---VLWVPGWDHHGLPTEQVvekklGIKEKKtrhkygreEFREKCrewkm 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24308436 115 ---DRVSEQFQQLfqeaGIScTDFIR--------TTEARHRVAVQhfwgvLKSRGLLYKGVYEGWYCASDECFLPEAKV 182
Cdd:pfam00133 110 eyaDEIRKQFRRL----GRS-IDWDReyftmdpeLEAAVWEVFVR-----LHDKGLIYRGKKLVNWSPALNTALSNLEV 178
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
327-375 |
7.95e-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: 47.19 E-value: 7.95e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 24308436 327 AGMSPPQRICVHS-HWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLL 375
Cdd:cd00672 153 ATGKPFARYWLHTgHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALL 202
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
296-375 |
1.10e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 45.24 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 296 EFKSWWPATSHIIGKDI----LKFH-----AI----YWPafllgagmsppQRICVHSHWTVCGQKMSKSLGNVVDPRTCL 362
Cdd:PRK12300 524 EFLYWYPVDWRHSGKDLipnhLTFFifnhvAIfpeeKWP-----------RGIVVNGFVLLEGKKMSKSKGNVIPLRKAI 592
|
90
....*....|...
gi 24308436 363 NRYTVDGFRYFLL 375
Cdd:PRK12300 593 EEYGADVVRLYLT 605
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
331-375 |
1.30e-04 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 44.28 E-value: 1.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 24308436 331 PPQRICVHS-HWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLL 375
Cdd:pfam01406 236 QLANYWLHNgHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLL 281
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
235-374 |
2.25e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 44.21 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 235 PEPFHHVVLQWLdEELPDLSVSRRsshLHWGIPVPG---------------------------DDSQTIYVWLDALVNYL 287
Cdd:PRK14900 399 PEQWTNTYMAWM-RNIHDWCISRQ---LWWGHQIPAwycpdghvtvaretpeacstcgkaelrQDEDVLDTWFSSGLWPF 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 288 TVIGYP--NAEFKSWWPATSHIIGKDILKFhaiyWPAFLLGAGM----SPPQRIcVHSHWTV---CGQKMSKSLGNVVDP 358
Cdd:PRK14900 475 STMGWPeqTDTLRTFYPTSVMETGHDIIFF----WVARMMMMGLhfmgEVPFRT-VYLHPMVrdeKGQKMSKTKGNVIDP 549
|
170
....*....|....*.
gi 24308436 359 RTCLNRYTVDGFRYFL 374
Cdd:PRK14900 550 LVITEQYGADALRFTL 565
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
347-375 |
3.59e-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: 43.50 E-value: 3.59e-04
10 20
....*....|....*....|....*....
gi 24308436 347 KMSKSLGNVVDPRTCLNRYTVDGFRYFLL 375
Cdd:COG0495 589 KMSKSKGNVVDPDEIIEKYGADTLRLFEM 617
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
345-360 |
4.13e-04 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 43.61 E-value: 4.13e-04
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
287-358 |
5.46e-04 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 43.07 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24308436 287 LTVIGYPNA--EFKSWWPATSHIIGKDILKFhaiyWPA-----FLLGAGMSPPQRICVH-----SHwtvcGQKMSKSLGN 354
Cdd:PTZ00419 521 FSTLGWPDQtdDLQRFFPTSLLETGSDILFF----WVArmvmmSLHLTDKLPFKTVFLHamvrdSQ----GEKMSKSKGN 592
|
....
gi 24308436 355 VVDP 358
Cdd:PTZ00419 593 VIDP 596
|
|
| |
