|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
34-560 |
3.39e-178 |
|
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: 513.89 E-value: 3.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 34 RPHLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIF 113
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 114 DALDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSE-----------------------GQT 170
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDryvegtcpkcgaedaygdqcencGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 171 AEHTDFegnKIRVSLESGHQVHWVSEENYMFRLSSLRPALLNWLQTEPVHPAPFLKLVHHWLEEELPDLSVSRqrsRLSW 250
Cdd:COG0143 161 LEPTEL---INPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEVRNEVLSWLKEGLQDLSISR---DFDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 251 GIPVPSDSSHVIYVWLDALVNYLTAA-GYPNPQLAP------W-GPST---HLLGKDILRFHAIYWPAFLIAAGLPPPQK 319
Cdd:COG0143 235 GIPVPGDPGKVFYVWFDALIGYISATkGYADDRGLPedfekyWpAPDTelvHFIGKDIIRFHAIIWPAMLMAAGLPLPKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 320 LLVHSHWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHR--TARMllNSELADALGGLLNRCTA 397
Cdd:COG0143 315 VFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEdfVARV--NSDLANDLGNLASRTLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 398 painpmqhfpkFQYENF------PVASRDQVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKL 471
Cdd:COG0143 393 -----------MIHKYFdgkvpePGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 472 QRGVEKEAAlrDSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVPHKMRTLKKNTFLAATrgeicyfqAQTLGPDKgL 551
Cdd:COG0143 462 AKDEDPERL--ATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLPA--------GHKIGKPE-P 530
|
....*....
gi 162287115 552 LFPRLEKSE 560
Cdd:COG0143 531 LFPRIEDEQ 539
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
39-560 |
9.30e-177 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 513.96 E-value: 9.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDALDI 118
Cdd:PRK12267 9 TTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 119 SYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEGQTAehtdfEGNKirvSLESGHQVHWVSEEN 198
Cdd:PRK12267 89 SYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLV-----DGGK---CPDCGREVELVKEES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 199 YMFRLSSLRPALLNWLQTEP--VHPApFLK--LVHHWLEEELPDLSVSrqRSRLSWGIPVPSDSSHVIYVWLDALVNYLT 274
Cdd:PRK12267 161 YFFRMSKYQDRLLEYYEENPdfIQPE-SRKneMINNFIKPGLEDLSIS--RTSFDWGIPVPFDPKHVVYVWIDALLNYIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 275 AAGYPNPQLAP----WGPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSDCIRRY 350
Cdd:PRK12267 238 ALGYGSDDDELfkkfWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 351 TTDGLRYYLLRH---GAperDCDFT-----HRtarmlLNSELADALGGLLNRCTApainpMQHfpkfQYENFPVASRDQV 422
Cdd:PRK12267 318 GLDALRYYLLREvpfGS---DGDFSpealvER-----INSDLANDLGNLLNRTVA-----MIN----KYFDGEIPAPGNV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 423 HD----LLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKLQRGVEKEAALrDSVIYLTLEALRLYAT 498
Cdd:PRK12267 381 TEfdeeLIALAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKDEGKKERL-ATVMYHLAESLRKVAV 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162287115 499 LLHPAVPGLATVVLDRLGVPHKMRT----LKKNTFLAATR---GEIcyfqaqtlgpdkglLFPRLEKSE 560
Cdd:PRK12267 460 LLSPFMPETSKKIFEQLGLEEELTSweslLEWGGLPAGTKvakGEP--------------LFPRIDVEE 514
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
35-371 |
1.55e-164 |
|
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: 470.48 E-value: 1.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 35 PHLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFD 114
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 115 ALDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEgqtaehtdfegnkirvslesghqvhWV 194
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPE-------------------------WR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 195 SEENYMFRLSSLRPALLNWLQTEP--VHPAPFLKLVHHWLEEELPDLSVSRQRSrlSWGIPVPSDSSHVIYVWLDALVNY 272
Cdd:cd00814 136 EEEHYFFRLSKFQDRLLEWLEKNPdfIWPENARNEVLSWLKEGLKDLSITRDLF--DWGIPVPLDPGKVIYVWFDALIGY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 273 LTAAGYPNPQ-------LAPWGPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSD 345
Cdd:cd00814 214 ISATGYYNEEwgnswwwKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDD 293
|
330 340
....*....|....*....|....*.
gi 162287115 346 CIRRYTTDGLRYYLLRHGAPERDCDF 371
Cdd:cd00814 294 LLERYGADALRYYLLRERPEGKDSDF 319
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
37-557 |
5.47e-141 |
|
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: 418.32 E-value: 5.47e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 37 LYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDAL 116
Cdd:TIGR00398 2 LITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 117 DISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFL-------------SEGQTAEHTDFEGN---- 179
Cdd:TIGR00398 82 NISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLpdryvegtcpkcgSEDARGDHCEVCGRhlep 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 180 ---KIRVSLESGHQVHWVSEENYMFRLSSLRPALLNWLQTEPVHPAP---FLKLVHHWLEEELPDLSVSRQRSRlsWGIP 253
Cdd:TIGR00398 162 telINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPasnVKNKAQNWLKGGLKDLAITRDLVY--WGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 254 VPSDSSHVIYVWLDALVNYLTAAGYPN---PQLAPWGPST------HLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHS 324
Cdd:TIGR00398 240 VPNDPNKVVYVWFDALIGYISSLGILSgdtEDWKKWWNNDedaeliHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 325 HWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLLNRCTApainpMQ 404
Cdd:TIGR00398 320 YLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLG-----FI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 405 HfpkfQYENFPVASRD----QVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKLqrgvEKEAA 480
Cdd:TIGR00398 395 K----KYFNGVLPSEDitdeEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWEL----FKQSP 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162287115 481 LRDSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVphkmrTLKKNTFLAATRGEicyfqaQTLGPDKglLFPRLE 557
Cdd:TIGR00398 467 RLKELLAVCSMLIRVLSILLYPIMPKLSEKILKFLNF-----ELEWDFKLKLLEGH------KLNKAEP--LFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
36-395 |
5.20e-140 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 410.53 E-value: 5.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 36 HLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDA 115
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 116 LDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFL-------------SEGQTAEHTDFEGNKI- 181
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLpdryvegtcphcgSEDARGDQCENCGRHLe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 182 ------RVSLESGHQVHWVSEENYMFRLSSLRPALLNWL-QTEPVHPAPFLKLVHHWLEEELPDLSVSRqrsRLSWGIPV 254
Cdd:pfam09334 161 ptelinPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIeENNPEWPENVKNMVLEWLKEGLKDRAISR---DLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 255 PSDSSHVIYVWLDALVNYLTAAGYPNPQLAPW---------GPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSH 325
Cdd:pfam09334 238 PGAEGKVFYVWLDAPIGYISATKELSGNEEKWkewwpndpdTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGY 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 326 WTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLLNRC 395
Cdd:pfam09334 318 LTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
34-560 |
3.39e-178 |
|
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: 513.89 E-value: 3.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 34 RPHLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIF 113
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 114 DALDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSE-----------------------GQT 170
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDryvegtcpkcgaedaygdqcencGAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 171 AEHTDFegnKIRVSLESGHQVHWVSEENYMFRLSSLRPALLNWLQTEPVHPAPFLKLVHHWLEEELPDLSVSRqrsRLSW 250
Cdd:COG0143 161 LEPTEL---INPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPDIQPEVRNEVLSWLKEGLQDLSISR---DFDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 251 GIPVPSDSSHVIYVWLDALVNYLTAA-GYPNPQLAP------W-GPST---HLLGKDILRFHAIYWPAFLIAAGLPPPQK 319
Cdd:COG0143 235 GIPVPGDPGKVFYVWFDALIGYISATkGYADDRGLPedfekyWpAPDTelvHFIGKDIIRFHAIIWPAMLMAAGLPLPKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 320 LLVHSHWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHR--TARMllNSELADALGGLLNRCTA 397
Cdd:COG0143 315 VFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEdfVARV--NSDLANDLGNLASRTLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 398 painpmqhfpkFQYENF------PVASRDQVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKL 471
Cdd:COG0143 393 -----------MIHKYFdgkvpePGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 472 QRGVEKEAAlrDSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVPHKMRTLKKNTFLAATrgeicyfqAQTLGPDKgL 551
Cdd:COG0143 462 AKDEDPERL--ATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGWPLPA--------GHKIGKPE-P 530
|
....*....
gi 162287115 552 LFPRLEKSE 560
Cdd:COG0143 531 LFPRIEDEQ 539
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
39-560 |
9.30e-177 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 513.96 E-value: 9.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDALDI 118
Cdd:PRK12267 9 TTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFKELWKKLDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 119 SYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEGQTAehtdfEGNKirvSLESGHQVHWVSEEN 198
Cdd:PRK12267 89 SYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLV-----DGGK---CPDCGREVELVKEES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 199 YMFRLSSLRPALLNWLQTEP--VHPApFLK--LVHHWLEEELPDLSVSrqRSRLSWGIPVPSDSSHVIYVWLDALVNYLT 274
Cdd:PRK12267 161 YFFRMSKYQDRLLEYYEENPdfIQPE-SRKneMINNFIKPGLEDLSIS--RTSFDWGIPVPFDPKHVVYVWIDALLNYIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 275 AAGYPNPQLAP----WGPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSDCIRRY 350
Cdd:PRK12267 238 ALGYGSDDDELfkkfWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 351 TTDGLRYYLLRH---GAperDCDFT-----HRtarmlLNSELADALGGLLNRCTApainpMQHfpkfQYENFPVASRDQV 422
Cdd:PRK12267 318 GLDALRYYLLREvpfGS---DGDFSpealvER-----INSDLANDLGNLLNRTVA-----MIN----KYFDGEIPAPGNV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 423 HD----LLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKLQRGVEKEAALrDSVIYLTLEALRLYAT 498
Cdd:PRK12267 381 TEfdeeLIALAEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKDEGKKERL-ATVMYHLAESLRKVAV 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162287115 499 LLHPAVPGLATVVLDRLGVPHKMRT----LKKNTFLAATR---GEIcyfqaqtlgpdkglLFPRLEKSE 560
Cdd:PRK12267 460 LLSPFMPETSKKIFEQLGLEEELTSweslLEWGGLPAGTKvakGEP--------------LFPRIDVEE 514
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
39-557 |
1.34e-166 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 482.84 E-value: 1.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDALDI 118
Cdd:PRK11893 6 TTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 119 SYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEGQTAEhtdfegnKIRVSLESGHQVHWVSEEN 198
Cdd:PRK11893 86 SYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIE-------DGYRCPPTGAPVEWVEEES 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 199 YMFRLSSLRPALLNWLQTEP--VHPAPFLKLVHHWLEEELPDLSVSrqRSRLSWGIPVPSDSSHVIYVWLDALVNYLTAA 276
Cdd:PRK11893 159 YFFRLSKYQDKLLELYEANPdfIQPASRRNEVISFVKSGLKDLSIS--RTNFDWGIPVPGDPKHVIYVWFDALTNYLTAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 277 GYP------NPQLAPWGPST-HLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSDCIRR 349
Cdd:PRK11893 237 GYPddeellAELFNKYWPADvHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 350 YTTDGLRYYLLRHgAPE-RDCDFTHRTARMLLNSELADALGGLLNRCTAPAINPMQHFPKfqyenFPVASRDQVHDLLGA 428
Cdd:PRK11893 317 YGVDAVRYFLLRE-IPFgQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVP-----EPGALTEADEALLEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 429 LQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKLqrgVEKEAALRDSVIYLTLEALRLYATLLHPAVPGLA 508
Cdd:PRK11893 391 AAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSL---AKTDPERLATVLYTLLEVLRGIAVLLQPVMPELA 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 162287115 509 TVVLDRLGVP-HKMRTLKKNTFLAATRGeicyfqaQTLGPDKGlLFPRLE 557
Cdd:PRK11893 468 AKILDQLGVEeDENRDFAALSWGRLAPG-------TTLPKPEP-IFPRLE 509
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
35-371 |
1.55e-164 |
|
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: 470.48 E-value: 1.55e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 35 PHLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFD 114
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 115 ALDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEgqtaehtdfegnkirvslesghqvhWV 194
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPE-------------------------WR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 195 SEENYMFRLSSLRPALLNWLQTEP--VHPAPFLKLVHHWLEEELPDLSVSRQRSrlSWGIPVPSDSSHVIYVWLDALVNY 272
Cdd:cd00814 136 EEEHYFFRLSKFQDRLLEWLEKNPdfIWPENARNEVLSWLKEGLKDLSITRDLF--DWGIPVPLDPGKVIYVWFDALIGY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 273 LTAAGYPNPQ-------LAPWGPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSD 345
Cdd:cd00814 214 ISATGYYNEEwgnswwwKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDD 293
|
330 340
....*....|....*....|....*.
gi 162287115 346 CIRRYTTDGLRYYLLRHGAPERDCDF 371
Cdd:cd00814 294 LLERYGADALRYYLLRERPEGKDSDF 319
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
37-557 |
5.47e-141 |
|
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: 418.32 E-value: 5.47e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 37 LYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDAL 116
Cdd:TIGR00398 2 LITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 117 DISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFL-------------SEGQTAEHTDFEGN---- 179
Cdd:TIGR00398 82 NISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLpdryvegtcpkcgSEDARGDHCEVCGRhlep 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 180 ---KIRVSLESGHQVHWVSEENYMFRLSSLRPALLNWLQTEPVHPAP---FLKLVHHWLEEELPDLSVSRQRSRlsWGIP 253
Cdd:TIGR00398 162 telINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPasnVKNKAQNWLKGGLKDLAITRDLVY--WGIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 254 VPSDSSHVIYVWLDALVNYLTAAGYPN---PQLAPWGPST------HLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHS 324
Cdd:TIGR00398 240 VPNDPNKVVYVWFDALIGYISSLGILSgdtEDWKKWWNNDedaeliHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 325 HWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLLNRCTApainpMQ 404
Cdd:TIGR00398 320 YLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLG-----FI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 405 HfpkfQYENFPVASRD----QVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAFFQSQAPWKLqrgvEKEAA 480
Cdd:TIGR00398 395 K----KYFNGVLPSEDitdeEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWEL----FKQSP 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162287115 481 LRDSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVphkmrTLKKNTFLAATRGEicyfqaQTLGPDKglLFPRLE 557
Cdd:TIGR00398 467 RLKELLAVCSMLIRVLSILLYPIMPKLSEKILKFLNF-----ELEWDFKLKLLEGH------KLNKAEP--LFSKIE 530
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
36-395 |
5.20e-140 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 410.53 E-value: 5.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 36 HLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDA 115
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 116 LDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFL-------------SEGQTAEHTDFEGNKI- 181
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLpdryvegtcphcgSEDARGDQCENCGRHLe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 182 ------RVSLESGHQVHWVSEENYMFRLSSLRPALLNWL-QTEPVHPAPFLKLVHHWLEEELPDLSVSRqrsRLSWGIPV 254
Cdd:pfam09334 161 ptelinPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIeENNPEWPENVKNMVLEWLKEGLKDRAISR---DLDWGIPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 255 PSDSSHVIYVWLDALVNYLTAAGYPNPQLAPW---------GPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSH 325
Cdd:pfam09334 238 PGAEGKVFYVWLDAPIGYISATKELSGNEEKWkewwpndpdTELVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGY 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 326 WTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLLNRC 395
Cdd:pfam09334 318 LTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
39-516 |
3.36e-91 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 292.39 E-value: 3.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDALDI 118
Cdd:PLN02224 74 TTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKDLDI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 119 SYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEGQTaehtdFEGNKIRVslesgHQVHWVS--E 196
Cdd:PLN02224 154 AYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKEL-----LENNCCPV-----HQMPCVArkE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 197 ENYMFRLSSLRPALLNWLQTEP--VHPAPFLKLVHHWLEEELPDLSVSrqRSRLSWGIPVPSDSSHVIYVWLDALVNYLT 274
Cdd:PLN02224 224 DNYFFALSKYQKPLEDILAQNPrfVQPSYRLNEVQSWIKSGLRDFSIS--RALVDWGIPVPDDDKQTIYVWFDALLGYIS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 275 AAGYPNPQLA-------PWGPSTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSDCI 347
Cdd:PLN02224 302 ALTEDNKQQNletavsfGWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 348 RRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLLNRCTApainpmqhFPKFQYENFPVAsrdqvhDLLG 427
Cdd:PLN02224 382 QKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLG--------LLKKNCESTLVE------DSTV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 428 ALQELPVE--VDQWIKK-------FQVHKALECIDACVRRSNAFFQSQAPWKL--QRGVEKEAALRDSVIylTLEALRLY 496
Cdd:PLN02224 448 AAEGVPLKdtVEKLVEKaqtnyenLSLSSACEAVLEIGNAGNTYMDQRAPWFLfkQGGVSAEEAAKDLVI--ILEVMRVI 525
|
490 500
....*....|....*....|
gi 162287115 497 ATLLHPAVPGLATVVLDRLG 516
Cdd:PLN02224 526 AVALSPIAPCLSLRIYSQLG 545
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
33-518 |
5.08e-72 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 243.14 E-value: 5.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 33 SRPHLYTTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTI 112
Cdd:PRK00133 1 MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 113 FDALDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFL-------------SEGQ---------- 169
Cdd:PRK00133 81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLpdrfvkgtcpkcgAEDQygdncevcga 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 170 TAEHTDFE-------GNK--IRVSlesghqvhwvseENYMFRLSSLRPALLNWLQTEPVHPAPFLKLVHHWLEEELPDLS 240
Cdd:PRK00133 161 TYSPTELInpksaisGATpvLKES------------EHFFFKLPRFEEFLKEWITRSGELQPNVANKMKEWLEEGLQDWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 241 VSRQrsrLSW-GIPVPSDSSHVIYVWLDALVNY------LTAAGYPNPQLAPWGPST-----HLLGKDILRFHAIYWPAF 308
Cdd:PRK00133 229 ISRD---APYfGFEIPGAPGKVFYVWLDAPIGYisstknLCDKRGGLDWDEYWKKDSdtelyHFIGKDIIYFHTLFWPAM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 309 LIAAGLPPPQKLLVHSHWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHgAPER--DCDFTHR--TARmlLNSEL 384
Cdd:PRK00133 306 LEGAGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAK-LPETidDLDFNWEdfQQR--VNSEL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 385 ADALGGLLNRCTapainpmqhfpKFQYENFP--VASRDQVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRSNAF 462
Cdd:PRK00133 383 VGKVVNFASRTA-----------GFINKRFDgkLPDALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKY 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 162287115 463 FQSQAPWKLQRGVEKEAAlrdSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVP 518
Cdd:PRK00133 452 VDDNEPWKLAKQDGERLQ---AVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLE 504
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
39-371 |
5.43e-61 |
|
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: 204.19 E-value: 5.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGL-------------DPQTFCSTV 105
Cdd:cd00668 5 TTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGGrkkktiwieefreDPKEFVEEM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 106 SLQFRTIFDALDISY--TDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGwyctsdeaflsegqtaehtdfegnkirv 183
Cdd:cd00668 85 SGEHKEDFRRLGISYdwSDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV---------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 184 slesghqvhwVSEENYMFRLSSLRPALLNWLQTEPVHPAPFLKLVHHWLeEELPDLSVSRQRsrlSWGIPVPSDsshVIY 263
Cdd:cd00668 137 ----------RITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAWL-ESLLDWAISRQR---YWGTPLPED---VFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 264 VWLDALVNYLTAAGYP--NPQLAPWGPST-HLLGKDILRFHAIYWPAFLIAAGLP-PPQKLLVHSHWTSE-GTKMSKSLK 338
Cdd:cd00668 200 VWFDSGIGPLGSLGYPeeKEWFKDSYPADwHLIGKDILRGWANFWITMLVALFGEiPPKNLLVHGFVLDEgGQKMSKSKG 279
|
330 340 350
....*....|....*....|....*....|...
gi 162287115 339 NVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDF 371
Cdd:cd00668 280 NVIDPSDVVEKYGADALRYYLTSLAPYGDDIRL 312
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
37-518 |
6.33e-36 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 143.38 E-value: 6.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 37 LYTTPIFYVNAAPHLGHVYSALL-ADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTFCSTVSLQFRTIFDA 115
Cdd:PLN02610 20 LITSALPYVNNVPHLGNIIGCVLsADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 116 LDISYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSE-------------------------GQT 170
Cdd:PLN02610 100 FDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCDTCQKFLADrlvegtcptegcnydsargdqcekcGKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 171 AEHTDFEGNKIRVSLESGHqvhwVSEENYMF-RLSSLRPALLNWLQTEPVH---PAPFLKLVHHWLEEELPDLSVSRQrs 246
Cdd:PLN02610 180 LNPTELIDPKCKVCKNTPR----IRDTDHLFlELPLLKDKLVEYINETSVAggwSQNAIQTTNAWLRDGLKPRCITRD-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 247 rLSWGIPVPSD--SSHVIYVWLDALVNYLT-AAGYpNPQLAPWGPST------HLLGKDILRFHAIYWPAFLIAAGLPPP 317
Cdd:PLN02610 254 -LKWGVPVPLEkyKDKVFYVWFDAPIGYVSiTACY-TPEWEKWWKNPenvelyQFMGKDNVPFHTVMFPSTLLGTGENWT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 318 --QKLLVHSHWTSEGTKMSKSLKNVV---DPSDciRRYTTDGLRYYLLRHGAPERDCDFTHRTARMLLNSELADALGGLL 392
Cdd:PLN02610 332 mmKTISVTEYLNYEGGKFSKSKGVGVfgnDAKD--TNIPVEVWRYYLLTNRPEVSDTLFTWADLQAKLNSELLNNLGNFI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 393 NRCTAPAINPMQHFpkfqYEN-FPVASRDQVHDLLGAL-QELPVEVDQWIK---KFQVHKALECIDACVRRSNAFFQSQA 467
Cdd:PLN02610 410 NRVLSFIAKPPGAG----YGSvIPDAPGAESHPLTKKLaEKVGKLVEQYVEameKVKLKQGLKTAMSISSEGNAYLQESQ 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 162287115 468 PWKLqrgVEKEAALRDSVIYLTLEALRLYATLLHPAVPGLATVVLDRLGVP 518
Cdd:PLN02610 486 FWKL---YKEDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLP 533
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
380-515 |
7.74e-25 |
|
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: 99.87 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 380 LNSELADALGGLLNRCTAPAINPMQHFPKFqyenfPVASRDQVHDLLGALQELPVEVDQWIKKFQVHKALECIDACVRRS 459
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPE-----FGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 162287115 460 NAFFQSQAPWKLQRGVEKEAAlrDSVIYLTLEALRLYATLLHPAVPGLATVVLDRL 515
Cdd:cd07957 76 NKYIDETAPWKLAKEEDPERL--ATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
40-371 |
7.48e-20 |
|
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: 91.54 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 40 TPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHG----MKVQQAASALG-----LDPQTF---C----- 102
Cdd:cd00817 7 TPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGiatqVVVEKKLGIEGktrhdLGREEFlekCwewke 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 103 ---STVSLQFRTIFDALDisYTDFVRTTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSegqtaehtdfegn 179
Cdd:cd00817 87 esgGKIREQLKRLGASVD--WSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRTAIS------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 180 KIRVSLESGHQVHWVSEENYMFRLSSLRPALL--------NWlqtepvHPAPFLKLVHHWLEEeLPDLSVSRQRSrlsWG 251
Cdd:cd00817 152 DIEVCSRSGDVIEPLLKPQWFVKVKDLAKKALeavkegdiKF------VPERMEKRYENWLEN-IRDWCISRQLW---WG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 252 IPVP----SDSSHVIYV--------------------------------WLDALVNYLTAAGYPN--PQLAPWGPsTHLL 293
Cdd:cd00817 222 HRIPawycKDGGHWVVAreedeaidkaapeacvpcggeelkqdedvldtWFSSSLWPFSTLGWPEetKDLKKFYP-TSLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 294 --GKDILRFhaiyWPAFLIAAGLP-----PPQKLLVHShWT--SEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGA 364
Cdd:cd00817 301 vtGHDIIFF----WVARMIMRGLKltgklPFKEVYLHG-LVrdEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAAT 375
|
....*..
gi 162287115 365 PERDCDF 371
Cdd:cd00817 376 QGRDINL 382
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
44-360 |
8.10e-18 |
|
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: 84.98 E-value: 8.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 44 YVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAAS-ALGLDPQTFCSTVS-LQFRTI-----FDAL 116
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEkELGISGKKDIEKMGiAEFNAKcrefaLRYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 117 DISYTDFVR------------TTEPRHIEAVSRFWMTLEEQGYIYKGTY-----------EGWYctsdeaflsegqtaeh 173
Cdd:cd00818 91 DEQEEQFQRlgvwvdwenpykTMDPEYMESVWWVFKQLHEKGLLYRGYKvvpwpliyratPQWF---------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 174 tdfegnkIRVS------LESGHQVHWVSEenymfrlsSLRPALLNWLqtepvhpapflklvhhwleEELPDLSVSRQRsr 247
Cdd:cd00818 155 -------IRVTkikdrlLEANDKVNWIPE--------WVKNRFGNWL-------------------ENRRDWCISRQR-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 248 lSWGIPVP---SDS---------SHVIYVWLDALVNYLTAAGYPnPQLAPWGPSthllgkdilrfhaiyWPAFLIAAGL- 314
Cdd:cd00818 199 -YWGTPIPvwyCEDcgevlvrrvPDVLDVWFDSGSMPYAQLHYP-FENEDFEEL---------------FPADFILEGSd 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162287115 315 -------------------PPPQKLLVHSHWTSE-GTKMSKSLKNVVDPSDCIRRYTTDGLRYYLL 360
Cdd:cd00818 262 qtrgwfysllllstalfgkAPYKNVIVHGFVLDEdGRKMSKSLGNYVDPQEVVDKYGADALRLWVA 327
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
221-371 |
3.99e-11 |
|
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: 65.85 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 221 PAPFLKLVHHWLEEeLPDLSVSRQrsrLSWGIPVPS---DSSHVIYV----------------------------WLDAL 269
Cdd:TIGR00422 382 PKRMEKRYLNWLRN-IKDWCISRQ---LIWGHRIPVwycKECGEVYVakeeplpddktntgpsveleqdtdvldtWFSSS 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 270 VNYLTAAGYP--NPQLAPWGPsTHLL--GKDILRFhaiyWPAFLIAAGLP-----PPQKLLVHSHWTSE-GTKMSKSLKN 339
Cdd:TIGR00422 458 LWPFSTLGWPdeTKDLKKFYP-TDLLvtGYDIIFF----WVARMIFRSLAltgqvPFKEVYIHGLVRDEqGRKMSKSLGN 532
|
170 180 190
....*....|....*....|....*....|..
gi 162287115 340 VVDPSDCIRRYTTDGLRYYLLRHGAPERDCDF 371
Cdd:TIGR00422 533 VIDPLDVIEKYGADALRFTLASLVTPGDDINF 564
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
202-360 |
8.14e-11 |
|
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: 64.74 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 202 RLSSLRPALLNWLQTEPVHPAPFLKLVHHWLEEeLPDLSVSRQRSrlsWGIPVP--------------SDSSHVIY---- 263
Cdd:pfam00133 383 RMDELADQALEAVEKVQFVPKSGEKRYFNWLAN-IQDWCISRQRW---WGHPIPawvskdteevvcrgELFELVAGrfee 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 264 ------------------------------VWLDALVNYLTAAGYPN---PQLAPWGPSTHLL-GKDILRFhaiyWPAFL 309
Cdd:pfam00133 459 egsikwlhreakdklgygkgtleqdedvldTWFSSGSWPFSTLGWPFvntEEFKKFFPADMLLeGSDQTRG----WFYRM 534
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 162287115 310 IAAGL-----PPPQKLLVHSHWT-SEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLL 360
Cdd:pfam00133 535 IMLSTaltgsVPFKNVLVHGLVRdEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
220-368 |
9.07e-08 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 55.11 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 220 HPAPFLKLVHHWLEEeLPDLSVSRQrsrLSWG--IPVPSDSSHVIYV------------W------LD-----ALVNYLT 274
Cdd:PRK05729 383 VPERWEKTYFHWMEN-IQDWCISRQ---LWWGhrIPAWYDEDGEVYVgreepearekalLtqdedvLDtwfssALWPFST 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 275 AaGYPN--PQLAPWGPsTHLL--GKDILRFhaiyWPAFLIAAGL-----PPPQKLLVH-----SHwtseGTKMSKSLKNV 340
Cdd:PRK05729 459 L-GWPEktEDLKRFYP-TSVLvtGFDIIFF----WVARMIMMGLhftgqVPFKDVYIHglvrdEQ----GRKMSKSKGNV 528
|
170 180
....*....|....*....|....*...
gi 162287115 341 VDPSDCIRRYTTDGLRYYLLRHGAPERD 368
Cdd:PRK05729 529 IDPLDLIDKYGADALRFTLAALASPGRD 556
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
221-505 |
1.11e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 54.95 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 221 PAPFLKLVHHWLEEeLPDLSVSRQrsrLSWG--IPV------PSDSSHV---------------------IYVWLDALVN 271
Cdd:PLN02943 434 PERFEKIYNHWLSN-IKDWCISRQ---LWWGhrIPVwyivgkDCEEDYIvarsaeealekarekygkdveIYQDPDVLDT 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 272 YLTAAGYPNPQLApWG-----------PSTHL-LGKDILRFhaiyWPAFLIAAGLPPPQKL---LVHSHW---TSEGTKM 333
Cdd:PLN02943 510 WFSSALWPFSTLG-WPdvsaedfkkfyPTTVLeTGHDILFF----WVARMVMMGIEFTGTVpfsYVYLHGlirDSQGRKM 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 334 SKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPErdcDFTHRTARMLLNSELAdalggllnrctapaiNPMQHFPKFQYEN 413
Cdd:PLN02943 585 SKTLGNVIDPLDTIKEFGTDALRFTLALGTAGQ---DLNLSTERLTSNKAFT---------------NKLWNAGKFVLQN 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 414 FPVAS--------RDQVHDLLGALQELPVEvDQWIkkfqVHKALECIDACVRRSNAFFQSQ-------------APWKLQ 472
Cdd:PLN02943 647 LPSQSdtsawehiLACKFDKEESLLSLPLP-ECWV----VSKLHELIDSVTTSYDKYFFGDvgreiydffwsdfADWYIE 721
|
330 340 350
....*....|....*....|....*....|....*...
gi 162287115 473 RGVEKEAALRDSVIYLTLEALRLYA-----TLLHPAVP 505
Cdd:PLN02943 722 ASKTRLYHSGDNSALSRAQAVLLYVfenilKLLHPFMP 759
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
329-372 |
2.34e-07 |
|
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: 53.90 E-value: 2.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 162287115 329 EGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFT 372
Cdd:COG0495 586 GIEKMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPPERDLEWS 629
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
229-360 |
4.23e-07 |
|
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: 53.16 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 229 HHWLEEeLPDLSVSRQRSrlsWGIPVP----SDSSHVIY------------------VW--LDALVNYLtAAGYPNPQLA 284
Cdd:COG0060 449 GNMLEN-RPDWCISRQRY---WGVPIPiwvcEDCGELHRteevigsvaelleeegadAWfeLDLHRPFL-DETLKCPKCG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 285 -----------PW---GpSTH---LLGKDILRfhaiyWPA-------------F----LIAAGL---PPPQKLLVHSHwT 327
Cdd:COG0060 524 gtmrrvpdvldVWfdsG-SMHfavLENREELH-----FPAdfylegsdqtrgwFysslLTSTALfgrAPYKNVLTHGF-V 596
|
170 180 190
....*....|....*....|....*....|....*
gi 162287115 328 --SEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLL 360
Cdd:COG0060 597 ldEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVA 631
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
328-368 |
5.40e-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: 52.75 E-value: 5.40e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 162287115 328 SEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERD 368
Cdd:COG0525 518 EQGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRD 558
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
330-505 |
5.02e-06 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 49.42 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 330 GTKMSKSLKNVVDPSDCIRRYTTDGLRYYLL--RHGA----PERDCDFTHRTARMLLN-SELADALGGLLNRCTAPAINP 402
Cdd:PRK13208 531 GKKMSKSKGNVVTPEELLEKYGADAVRYWAAsaRLGSdtpfDEKQVKIGRRLLTKLWNaSRFVLHFSADPEPDKAEVLEP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 403 MqhfpkfqyenfpvasrdqvhD--LLGALQELPVEVDQWIKKFQVHKALECIDacvrrsnAFFqsqapWKL--------- 471
Cdd:PRK13208 611 L--------------------DrwILAKLAKVVEKATEALENYDFAKALEEIE-------SFF-----WHVfcddylelv 658
|
170 180 190
....*....|....*....|....*....|....*...
gi 162287115 472 -QR--GvEKEAALRDSVIYlTL-EALRLYATLLHPAVP 505
Cdd:PRK13208 659 kSRayG-EDEEEEQKSARY-TLyTVLDTLLRLLAPFLP 694
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
44-184 |
8.87e-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: 48.56 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 44 YVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASA-LGLD-PQT-----------FCSTVSLQF- 109
Cdd:pfam00133 33 NATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKkLGIKeKKTrhkygreefreKCREWKMEYa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 110 ---RTIFDALDISYtDFVR---TTEPRHIEAVSRFWMTLEEQGYIYKGTYEGWYCTSDEAFLSEGQTaEHTDFEGNKIRV 183
Cdd:pfam00133 113 deiRKQFRRLGRSI-DWDReyfTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEV-EYKDVKGPSIHV 190
|
.
gi 162287115 184 S 184
Cdd:pfam00133 191 A 191
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
289-360 |
1.57e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 48.18 E-value: 1.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162287115 289 STHLLGKdilrfhaiywPAF--LIAAGLpppqkLLvhshwTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLL 360
Cdd:PLN02882 589 STALFDK----------PAFknLICNGL-----VL-----AEDGKKMSKSLKNYPDPNEVIDKYGADALRLYLI 642
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
230-368 |
3.86e-05 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 46.91 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 230 HWLEEeLPDLSVSRQrsrLSWGIPVPS---DSSHVIY------------------------VWLDALVNYLTAAGYP--N 280
Cdd:PRK14900 408 AWMRN-IHDWCISRQ---LWWGHQIPAwycPDGHVTVaretpeacstcgkaelrqdedvldTWFSSGLWPFSTMGWPeqT 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 281 PQLAPWGPSTHL-LGKDILRFhaiyWPAFLIAAGLP-----PPQKLLVHSHWTSE-GTKMSKSLKNVVDPSDCIRRYTTD 353
Cdd:PRK14900 484 DTLRTFYPTSVMeTGHDIIFF----WVARMMMMGLHfmgevPFRTVYLHPMVRDEkGQKMSKTKGNVIDPLVITEQYGAD 559
|
170
....*....|....*
gi 162287115 354 GLRYYLLRHGAPERD 368
Cdd:PRK14900 560 ALRFTLAALTAQGRD 574
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
311-362 |
4.99e-05 |
|
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: 44.49 E-value: 4.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 162287115 311 AAGLPPPQKLLVHS-HWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRH 362
Cdd:cd00672 152 AATGKPFARYWLHTgHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSS 204
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
285-361 |
6.21e-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: 45.48 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 285 PWGP------------STHLLGK--DI------LRF-H----------------AIYWpafliaaglpppqkllVHSHW- 326
Cdd:COG0215 196 PWGRgrpgwhiecsamSTKYLGEtfDIhgggidLIFpHheneiaqseaatgkpfARYW----------------MHNGFl 259
|
90 100 110
....*....|....*....|....*....|....*
gi 162287115 327 TSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLR 361
Cdd:COG0215 260 TVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLS 294
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
45-360 |
8.60e-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: 44.67 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 45 VNAAPHLGHVYSALLADVQHRYSAMCGIESKLS---TGTDEhgmKVQQAASALGLDPQTFCSTVSLQFRTIFDALDISYT 121
Cdd:pfam01406 19 VYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVqnfTDIDD---KIIKRARQEGESFRQLAARFIEAYTKDMDALNVLPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 122 DFV-RTTEprHIEAVSRFWMTLEEQGYIYKGTYEGWYcTSDEAFLSEGQTAEHtdfegNKIRVSLESGHQVHWVSEENYM 200
Cdd:pfam01406 96 DLEpRVTE--HIDEIIEFIERLIKKGYAYVSDNGDVY-FDVSSFPDYGKLSGQ-----NLEQLEAGARGEVSEGKRDPLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 201 FRLsslrpallnWLQT---EPVHPAPflklvhhWleeelpdlsvsrQRSRLSWGIPVPSDSSHVIYVWLDalvnyltaag 277
Cdd:pfam01406 168 FAL---------WKASkegEPSWDSP-------W------------GKGRPGWHIECSAMARKYLGDQID---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 278 ypnpqlapwgpsTHLLGKDILRFHAIYWPAFLIAAGLPPPQKLLVHS-HWTSEGTKMSKSLKNVVDPSDCIRRYTTDGLR 356
Cdd:pfam01406 210 ------------IHGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHNgHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILR 277
|
....
gi 162287115 357 YYLL 360
Cdd:pfam01406 278 YFLL 281
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
39-101 |
2.93e-04 |
|
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: 41.31 E-value: 2.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162287115 39 TTPIFYVNAAPHLGHVYSALLADVQHRYSAMCGIESKLSTGTDEHGMKVQQAASALGLDPQTF 101
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAF 64
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
261-355 |
3.60e-04 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 43.73 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 261 VIYVWLDALVNYLTAAGYPN--PQLAPWGPSTHL-LGKDILRFhaiyWPAFLIAAGLP-----PPQKLLVHSHW-TSEGT 331
Cdd:PLN02381 579 VLDTWFSSGLFPLSVLGWPDdtDDLKAFYPTSVLeTGHDILFF----WVARMVMMGMQlggdvPFRKVYLHPMIrDAHGR 654
|
90 100
....*....|....*....|....
gi 162287115 332 KMSKSLKNVVDPSDCIRRYTTDGL 355
Cdd:PLN02381 655 KMSKSLGNVIDPLEVINGISLEGL 678
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
327-377 |
9.78e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 42.16 E-value: 9.78e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 162287115 327 TSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYYLLRHGAPERDCDFTHRTAR 377
Cdd:PRK12300 572 LLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVE 622
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
300-360 |
3.58e-03 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 40.34 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162287115 300 FHAIYwPAFLIAAGLPPPQ----KLLVHSHW-----------------TSEGTKMSKSLKNVVDPSDCIRRYTTDGLRYY 358
Cdd:PTZ00427 668 FHKIF-PADFIAEGLDQTRgwfyTLLVISTLlfdkapfknlicnglvlASDGKKMSKRLKNYPDPLYILDKYGADSLRLY 746
|
..
gi 162287115 359 LL 360
Cdd:PTZ00427 747 LI 748
|
|
| |
