|
Name |
Accession |
Description |
Interval |
E-value |
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
15-550 |
0e+00 |
|
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model appears to recognize the methionyl-tRNA synthetase of every species, including eukaryotic cytosolic and mitochondrial forms. The UPGMA difference tree calculated after search and alignment according to this model shows an unusual deep split between two families of MetG. One family contains forms from the Archaea, yeast cytosol, spirochetes, and E. coli, among others. The other family includes forms from yeast mitochondrion, Synechocystis sp., Bacillus subtilis, the Mycoplasmas, Aquifex aeolicus, and Helicobacter pylori. The E. coli enzyme is homodimeric, although monomeric forms can be prepared that are fully active. Activity of this enzyme in bacteria includes aminoacylation of fMet-tRNA with Met; subsequent formylation of the Met to fMet is catalyzed by a separate enzyme. Note that the protein from Aquifex aeolicus is split into an alpha (large) and beta (small) subunit; this model does not include the C-terminal region corresponding to the beta chain. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273058 [Multi-domain] Cd Length: 530 Bit Score: 600.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 15 SHVTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDK 94
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLT-PKELVDKYHEEFKDDWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 95 IYGINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVI-KDPKNDGKYLNTE--------- 164
Cdd:TIGR00398 80 WLNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEgTCPKCGSEDARGDhcevcgrhl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 165 ------------SKNEVVYQSETNYFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKElETGGTLPDLSISRPSARlkW 232
Cdd:TIGR00398 160 eptelinprckiCGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQN-WLKGGLKDLAITRDLVY--W 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 233 GIPTPNDPSQKVYVWFDALCNYLSSIGgipsILSNATEVVSRHYSDKSnvkgqllipypkevQRNTIHVIGKDIAKFHTV 312
Cdd:TIGR00398 237 GIPVPNDPNKVVYVWFDALIGYISSLG----ILSGDTEDWKKWWNNDE--------------DAELIHFIGKDIVRFHTI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 313 YWPSFLLAAGLPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYETR-EL 391
Cdd:TIGR00398 299 YWPAMLMGLGLPLPTQVFSHGYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVnAD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 392 LVSKWGNLINRCCGSKFNIERAVMKFSDKANfqfqeifqnepivsERIENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWS 471
Cdd:TIGR00398 379 LANKLGNLLNRTLGFIKKYFNGVLPSEDITD--------------EEDKKLLKLINEALEQIDEAIESFEFRKALREIMK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 472 IINDANTLVQNSKPWERELDQ--QDNIIFLAMETSRILSILCQSIIPSLSQSFLDRIDVSKE-----KRTINYARLGSDK 544
Cdd:TIGR00398 445 LADRGNKYIDENKPWELFKQSprLKELLAVCSMLIRVLSILLYPIMPKLSEKILKFLNFELEwdfklKLLEGHKLNKAEP 524
|
....*.
gi 6321610 545 TYGKQS 550
Cdd:TIGR00398 525 LFSKIE 530
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
17-569 |
5.64e-153 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 448.56 E-value: 5.64e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKIY 96
Cdd:PRK11893 5 ITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGIS-PQELADRNSAAFKRLWEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVIkdpknDGKYLNTESKNEVVYQSETN 176
Cdd:PRK11893 84 NISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELI-----EDGYRCPPTGAPVEWVEEES 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 177 YFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETGgtLPDLSISRPSarLKWGIPTPNDPSQKVYVWFDALCNYLS 256
Cdd:PRK11893 159 YFFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSG--LKDLSISRTN--FDWGIPVPGDPKHVIYVWFDALTNYLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 257 SIGgipsilsnatevvsrhYSDKSNVKGQLLIPY-PkevqrNTIHVIGKDIAKFHTVYWPSFLLAAGLPLPRQIVVHGHW 335
Cdd:PRK11893 235 ALG----------------YPDDEELLAELFNKYwP-----ADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 336 LCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYETR-ELLVSKWGNLINRccgskfnieraV 414
Cdd:PRK11893 294 TLDGEKMSKSLGNVIDPFDLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRInADLANDLGNLAQR-----------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 415 MKFSDKanfQFQEIFQNEPIVSERIENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWSIINDANTLVQNSKPWERELDQQD 494
Cdd:PRK11893 363 LSMIAK---NFDGKVPEPGALTEADEALLEAAAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPE 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6321610 495 ---NIIFLAMETSRILSILCQSIIPSLSQSFLDRIDVSKEkRTINYARLGSDKTygkqsnKKGREVPLKKIPF-RLQEE 569
Cdd:PRK11893 440 rlaTVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEED-ENRDFAALSWGRL------APGTTLPKPEPIFpRLEEE 511
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
16-380 |
3.61e-151 |
|
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: 436.96 E-value: 3.61e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 16 HVTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKI 95
Cdd:cd00814 3 LITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVT-PQELCDKYHEIFKDLFKW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 96 YGINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPEskvikdpkndgkylntesknevvYQSET 175
Cdd:cd00814 82 LNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLPE-----------------------WREEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 176 NYFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETGgtLPDLSISRPSArlKWGIPTPNDPSQKVYVWFDALCNYL 255
Cdd:cd00814 139 HYFFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEG--LKDLSITRDLF--DWGIPVPLDPGKVIYVWFDALIGYI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 256 SSIGGipsilsnatevvsrhYSDKSNvkgqlLIPYPKEVQRNTIHVIGKDIAKFHTVYWPSFLLAAGLPLPRQIVVHGHW 335
Cdd:cd00814 215 SATGY---------------YNEEWG-----NSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYL 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 6321610 336 LCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDF 380
Cdd:cd00814 275 TVEGKKMSKSRGNVVDPDDLLERYGADALRYYLLRERPEGKDSDF 319
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
17-539 |
6.56e-143 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 427.68 E-value: 6.56e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKIY 96
Cdd:PRK12267 8 ITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKT-PQEYVDEISAGFKELWKKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVIkdpkNDGKYlnTESKNEVVYQSETN 176
Cdd:PRK12267 87 DISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLV----DGGKC--PDCGREVELVKEES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 177 YFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETGGtLPDLSISRpsARLKWGIPTPNDPSQKVYVWFDALCNYLS 256
Cdd:PRK12267 161 YFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPG-LEDLSISR--TSFDWGIPVPFDPKHVVYVWIDALLNYIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 257 SIGgipsilsnatevvsrhYSDKSNVKGQLLIPypkevqrNTIHVIGKDIAKFHTVYWPSFLLAAGLPLPRQIVVHGHWL 336
Cdd:PRK12267 238 ALG----------------YGSDDDELFKKFWP-------ADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 337 CNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEaklyetrELLVSK--------WGNLINRCCGskf 408
Cdd:PRK12267 295 MKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLREVPFGSDGDFSP-------EALVERinsdlandLGNLLNRTVA--- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 409 nieravM--KFSDkanFQFQEIFQNEPIVSErIENLAK-LLNKSQEVFDEkiaiFQYPQLLRHVWSIINDANTLVQNSKP 485
Cdd:PRK12267 365 ------MinKYFD---GEIPAPGNVTEFDEE-LIALAEeTLKNYEELMEE----LQFSRALEEVWKLISRANKYIDETAP 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321610 486 W-----ERELDQQDNIIFLAMETSRILSILCQSIIPSLSQSFLDRIDVSKEKRTINYAR 539
Cdd:PRK12267 431 WvlakdEGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLGLEEELTSWESLL 489
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
17-540 |
5.56e-142 |
|
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: 421.83 E-value: 5.56e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKIY 96
Cdd:COG0143 5 VTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGIT-PQELVDRIHAEFKELFEKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVI-KDPK------------NDGKYLN- 162
Cdd:COG0143 84 GISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRYVEgTCPKcgaedaygdqceNCGATLEp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 163 --------TESKNEVVYQSETNYFFRLSLFNKKIVDHIRKNPDfIFPaSKRDQILKELETGgtLPDLSISRpsaRLKWGI 234
Cdd:COG0143 164 telinprsAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQP-EVRNEVLSWLKEG--LQDLSISR---DFDWGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 235 PTPNDPSQKVYVWFDALCNYLSSIGGipsilsnatevvsrhYSDKSNvKGQLLIPYPKEVQRNTIHVIGKDIAKFHTVYW 314
Cdd:COG0143 237 PVPGDPGKVFYVWFDALIGYISATKG---------------YADDRG-LPEDFEKYWPAPDTELVHFIGKDIIRFHAIIW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 315 PSFLLAAGLPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYEtR---El 391
Cdd:COG0143 301 PAMLMAAGLPLPKKVFAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVA-RvnsD- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 392 LVSKWGNLINRCcgskfnieravMKFSDKanfQFQEIFQNEPIVSERIENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWS 471
Cdd:COG0143 379 LANDLGNLASRT-----------LSMIHK---YFDGKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321610 472 IINDANTLVQNSKPWE--RELDQQ--DNIIFLAMETSRILSILCQSIIPSLSQSFLDRIDVSKEKRTINYARL 540
Cdd:COG0143 445 LARAANKYIDETAPWKlaKDEDPErlATVLYTLLEALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGW 517
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
17-403 |
2.80e-107 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 327.32 E-value: 2.80e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKIY 96
Cdd:pfam09334 3 VTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGIT-PEELVDRYHEIHREDFKKF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVI--------KDPKND-----GKYLN- 162
Cdd:pfam09334 82 NISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEgtcphcgsEDARGDqcencGRHLEp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 163 --------TESKNEVVYQSETNYFFRLSLFNKKIVDHIRKNpDFIFPASKRDQILKELETGgtLPDLSISRpsaRLKWGI 234
Cdd:pfam09334 162 telinpkcVICGTTPEVKETEHYFFDLSKFQDKLREWIEEN-NPEWPENVKNMVLEWLKEG--LKDRAISR---DLDWGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 235 PTPNDPSQKVYVWFDALCNYLSSIGGipsiLSNATEVVSRHYSDKSNVKgqllipypkevqrnTIHVIGKDIAKFHTVYW 314
Cdd:pfam09334 236 PVPGAEGKVFYVWLDAPIGYISATKE----LSGNEEKWKEWWPNDPDTE--------------LVHFIGKDIIYFHTIFW 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 315 PSFLLAAGLPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYET-RELLV 393
Cdd:pfam09334 298 PAMLLGAGYRLPTTVFAHGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERvNSELA 377
|
410
....*....|
gi 6321610 394 SKWGNLINRC 403
Cdd:pfam09334 378 DDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
17-532 |
1.39e-77 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 256.95 E-value: 1.39e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDQPKKfVDKLYPEFVQLDKIY 96
Cdd:PLN02224 73 LTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEH-CDIISQSYRTLWKDL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVIKDpkndgkylNTESKNEV--VYQSE 174
Cdd:PLN02224 152 DIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELLEN--------NCCPVHQMpcVARKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 175 TNYFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETGgtLPDLSISRpsARLKWGIPTPNDPSQKVYVWFDALCNY 254
Cdd:PLN02224 224 DNYFFALSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSG--LRDFSISR--ALVDWGIPVPDDDKQTIYVWFDALLGY 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 255 LSSIggipsilsnaTEvvsrhYSDKSNVKGQLLIPYPKevqrnTIHVIGKDIAKFHTVYWPSFLLAAGLPLPRQIVVHGH 334
Cdd:PLN02224 300 ISAL----------TE-----DNKQQNLETAVSFGWPA-----SLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGF 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 335 WLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYE-TRELLVSKWGNLINRCCG-SKFNIER 412
Cdd:PLN02224 360 LTKDGMKMGKSLGNTLEPFELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKiVNAHLANTIGNLLNRTLGlLKKNCES 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 413 AVMKFSDKANfqfqeifQNEPIVseriENLAKLLNKSQEVFDEkiaiFQYPQLLRHVWSIINDANTLVQNSKPW------ 486
Cdd:PLN02224 440 TLVEDSTVAA-------EGVPLK----DTVEKLVEKAQTNYEN----LSLSSACEAVLEIGNAGNTYMDQRAPWflfkqg 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6321610 487 --ERELDQQDNIIFLamETSRILSILCQSIIPSLSQSFLDRIDVSKEK 532
Cdd:PLN02224 505 gvSAEEAAKDLVIIL--EVMRVIAVALSPIAPCLSLRIYSQLGYSEDQ 550
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
17-380 |
4.66e-49 |
|
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: 172.60 E-value: 4.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNG------------FDQPKKFVDK 84
Cdd:cd00668 4 VTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGgrkkktiwieefREDPKEFVEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 85 LYPEFVQLDKIYGINY--TRFIRTTDPDHIENV-MKLWELcLKNGYIYMGEHkgwysisdetfypeskvikdpkndgkyl 161
Cdd:cd00668 84 MSGEHKEDFRRLGISYdwSDEYITTEPEYSKAVeLIFSRL-YEKGLIYRGTH---------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 162 nteskneVVYQSEtNYFFRLSLFNKKIVDHIRKNPdfIFPASKRDQILKELETGGtlpDLSISRPsarLKWGIPTPNDps 241
Cdd:cd00668 135 -------PVRITE-QWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLL---DWAISRQ---RYWGTPLPED-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 242 qKVYVWFDALCNYLSSIGgipsilsNATEVVSRHYSdksnvkgqllipYPKEVqrntiHVIGKDIAKFHTVYWPSFLLAA 321
Cdd:cd00668 197 -VFDVWFDSGIGPLGSLG-------YPEEKEWFKDS------------YPADW-----HLIGKDILRGWANFWITMLVAL 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321610 322 GLPLP-RQIVVHGHWLCN-GMKMSKSLGNVVDPIDMARYYGADIVRWFLLenSKLEEDGDF 380
Cdd:cd00668 252 FGEIPpKNLLVHGFVLDEgGQKMSKSKGNVIDPSDVVEKYGADALRYYLT--SLAPYGDDI 310
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
17-520 |
1.05e-45 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 171.10 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFVQLDKIY 96
Cdd:PRK00133 6 VTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGIT-PEELIARYHAEHKRDFAGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 97 GINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVI--------KDPKND-----GKYLN- 162
Cdd:PRK00133 85 GISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIEQLYDPEKGMFLPDRFVKgtcpkcgaEDQYGDncevcGATYSp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 163 TESKNEV--------VYQSETNYFFRLSLFNKKIVDHIRKNPDFifPASKRDQILKELETGgtLPDLSISRPsarLKW-G 233
Cdd:PRK00133 165 TELINPKsaisgatpVLKESEHFFFKLPRFEEFLKEWITRSGEL--QPNVANKMKEWLEEG--LQDWDISRD---APYfG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 234 IPTPNDPSQKVYVWFDALCNYLSSiggipsilsnatevvSRHYSDKSNvkGQLLIPY-PKEVQRNTIHVIGKDIAKFHTV 312
Cdd:PRK00133 238 FEIPGAPGKVFYVWLDAPIGYISS---------------TKNLCDKRG--GLDWDEYwKKDSDTELYHFIGKDIIYFHTL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 313 YWPSFLLAAGLPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEED------GDFQEakly 386
Cdd:PRK00133 301 FWPAMLEGAGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDdldfnwEDFQQ---- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 387 etR---ElLVSKWGNLINRCcgskfnieravMKFSDKAnfqfqeiFQNEPIVSERIENLAKLLNKSQEVFDEKIAIFQYP 463
Cdd:PRK00133 377 --RvnsE-LVGKVVNFASRT-----------AGFINKR-------FDGKLPDALADPELLEEFEAAAEKIAEAYEAREFR 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321610 464 QLLRHVWSIINDANTLVQNSKPWerELDQQD-----NIIFLAMETSRILSILCQSIIPSLSQ 520
Cdd:PRK00133 436 KALREIMALADFANKYVDDNEPW--KLAKQDgerlqAVCSVGLNLFRALAIYLKPVLPELAE 495
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
17-531 |
1.31e-27 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 117.96 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLS-DVYHRWQLFKGNLSFFTTGTDEHGlkiqCASESNGFDQ---PKKFVDKLYPEFVQL 92
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGCVLSaDVFARYCRLRGYNAIYICGTDEYG----TATETKALEEnctPKEICDKYHAIHKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 93 DKIYGINYTRFIRTTDPDHIENV----MKLWElclkNGYIYMGEHKGWYSISDETFYPESKVI----------KDPKND- 157
Cdd:PLN02610 97 YDWFDISFDKFGRTSTPQQTEICqaifKKLME----NNWLSENTMQQLYCDTCQKFLADRLVEgtcptegcnyDSARGDq 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 158 ----GKYLN-TE--------SKNEVVYQSETNYFFRLSLFNKKIVDHIRK---------NPDFIFPASKRDqilkeletg 215
Cdd:PLN02610 173 cekcGKLLNpTElidpkckvCKNTPRIRDTDHLFLELPLLKDKLVEYINEtsvaggwsqNAIQTTNAWLRD--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 216 gTLPDLSISRPsarLKWGIPTPNDP-SQKV-YVWFDALCNYLSsiggipsILSNATEVVSRHYSDKSNVKgqllipypke 293
Cdd:PLN02610 244 -GLKPRCITRD---LKWGVPVPLEKyKDKVfYVWFDAPIGYVS-------ITACYTPEWEKWWKNPENVE---------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 294 vqrnTIHVIGKDIAKFHTVYWPSFLLAAGLP--LPRQIVVHGHWLCNGMKMSKS-----LGNVVD----PIDMARYYgad 362
Cdd:PLN02610 303 ----LYQFMGKDNVPFHTVMFPSTLLGTGENwtMMKTISVTEYLNYEGGKFSKSkgvgvFGNDAKdtniPVEVWRYY--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 363 ivrwfLLENSKLEEDGDFQ----EAKLyeTRELLvSKWGNLINRCcgskfnieraVMKFSDKANFQFQEIFQNEPIVSER 438
Cdd:PLN02610 376 -----LLTNRPEVSDTLFTwadlQAKL--NSELL-NNLGNFINRV----------LSFIAKPPGAGYGSVIPDAPGAESH 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 439 --IENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWSIINDANTLVQNSKPWERELDQQDNIIFLaMETS----RILSILCQ 512
Cdd:PLN02610 438 plTKKLAEKVGKLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYLQESQFWKLYKEDKPSCAIV-VKTSvglvYLLACLLE 516
|
570
....*....|....*....
gi 6321610 513 SIIPSLSQSFLDRIDVSKE 531
Cdd:PLN02610 517 PFMPSFSKEVLKQLNLPPE 535
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
23-377 |
3.36e-21 |
|
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: 94.99 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 23 YPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDQPKKFVDKLYP-EFVQLDKIYGINYT 101
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKELGISGKKDIEKMGIaEFNAKCREFALRYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 102 R-----FIR------------TTDPDHIENVMKLWELCLKNGYIYMGehkgwysisdetfypeSKVIKDPkndgkylnte 164
Cdd:cd00818 91 DeqeeqFQRlgvwvdwenpykTMDPEYMESVWWVFKQLHEKGLLYRG----------------YKVVPWP---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 165 skneVVYQSETNYFFRLSLFNKKIVDHIrKNPDFIfPASKRDQILKELETggtLPDLSISRPSArlkWGIPTP----NDP 240
Cdd:cd00818 145 ----LIYRATPQWFIRVTKIKDRLLEAN-DKVNWI-PEWVKNRFGNWLEN---RRDWCISRQRY---WGTPIPvwycEDC 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 241 SQKVY--------VWFDalcnylssiggipsilSNATEVVSRHYsdksnvkgqlliPYPKEVQRNT--IHVI--GKDIAK 308
Cdd:cd00818 213 GEVLVrrvpdvldVWFD----------------SGSMPYAQLHY------------PFENEDFEELfpADFIleGSDQTR 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321610 309 --FHTvywpSFLLAAGL---PLPRQIVVHGHWLC-NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEED 377
Cdd:cd00818 265 gwFYS----LLLLSTALfgkAPYKNVIVHGFVLDeDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
17-380 |
1.16e-20 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 93.08 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVDKLYPEFV-QLDKI 95
Cdd:cd00812 4 ILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRD-PEDWTEYNIKKMKeQLKRM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 96 -YGINYTRFIRTTDPDHIENV----MKLWElclkNGYIYMGEHK-GWYSISDETFYpeskvikdpkndgKYLNTEsknev 169
Cdd:cd00812 83 gFSYDWRREFTTCDPEYYKFTqwlfLKLYE----KGLAYKKEAPvNWCKLLDQWFL-------------KYSETE----- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 170 vyqsetnyffrlslFNKKIVDHIRKnPDFIFPASKRDQILKeletggtlpdLSISRpsaRLKWGIPTPndpsqkvyvWFD 249
Cdd:cd00812 141 --------------WKEKLLKDLEK-LDGWPEEVRAMQENW----------IGCSR---QRYWGTPIP---------WTD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 250 AlcnylssiggIPSiLSNATEVVSRhYSDKSNVKGqlliPYPKEVQRNT----------IHVIGKDIAKFHTVY---WPS 316
Cdd:cd00812 184 T----------MES-LSDSTWYYAR-YTDAHNLEQ----PYEGDLEFDReefeywypvdIYIGGKEHAPNHLLYsrfNHK 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321610 317 FLLAAGLPL---PRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDF 380
Cdd:cd00812 248 ALFDEGLVTdepPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDADFDW 314
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
29-377 |
5.40e-17 |
|
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: 83.06 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 29 HLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHG----------LKIQCASESNgfDQPKKFVDKLYpEFV-------- 90
Cdd:cd00817 17 HMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGiatqvvvekkLGIEGKTRHD--LGREEFLEKCW-EWKeesggkir 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 91 -QLDKI-YGINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKgwysisdetfypeskVIKDPKndgkyLNTE-SKN 167
Cdd:cd00817 94 eQLKRLgASVDWSREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRL---------------VNWCPK-----LRTAiSDI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 168 EVVYQSET--------NYFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETggtLPDLSISRpsaRLKWGIPTPnd 239
Cdd:cd00817 154 EVCSRSGDviepllkpQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLEN---IRDWCISR---QLWWGHRIP-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 240 psqkvyVWFDALCNYLSsIGGIPSILSNATEVVSRHYSDKSNVKG---------------QLLIPYPKEVQR------NT 298
Cdd:cd00817 226 ------AWYCKDGGHWV-VAREEDEAIDKAAPEACVPCGGEELKQdedvldtwfssslwpFSTLGWPEETKDlkkfypTS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 299 IHVIGKDIAKFhtvyWPSFLLAAGLPL----P-RQIVVHGhWLC--NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLEN 371
Cdd:cd00817 299 LLVTGHDIIFF----WVARMIMRGLKLtgklPfKEVYLHG-LVRdeDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASA 373
|
....*.
gi 6321610 372 SKLEED 377
Cdd:cd00817 374 ATQGRD 379
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
325-402 |
8.66e-14 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 74.52 E-value: 8.66e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6321610 325 LPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYETRELLvSKWGNLINR 402
Cdd:PRK12300 561 WPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAELLQDADWREKEVESVRRQL-ERFYELAKE 637
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
392-526 |
1.03e-12 |
|
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: 65.20 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 392 LVSKWGNLINRccgskfnieraVMKFSDKAnfqFQEIFQNEPIVSERIENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWS 471
Cdd:cd07957 5 LANNLGNLVNR-----------TLNMASKY---FGGVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIME 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321610 472 IINDANTLVQNSKPWE--RELDQQ--DNIIFLAMETSRILSILCQSIIPSLSQSFLDRI 526
Cdd:cd07957 71 LARAANKYIDETAPWKlaKEEDPErlATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
327-369 |
1.45e-12 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 70.49 E-value: 1.45e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 6321610 327 RQIVVHGHWL-CNGMKMSKSLGNVVDPIDMARYYGADIVRWFLL 369
Cdd:COG0060 588 KNVLTHGFVLdEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVA 631
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
341-383 |
2.72e-10 |
|
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: 63.15 E-value: 2.72e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6321610 341 KMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEA 383
Cdd:COG0495 589 KMSKSKGNVVDPDEIIEKYGADTLRLFEMFAGPPERDLEWSDS 631
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
338-385 |
9.85e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 61.66 E-value: 9.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 6321610 338 NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKL 385
Cdd:PRK05729 517 QGRKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFDEERV 564
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
303-455 |
1.93e-09 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 60.59 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 303 GKDIAK---FHTVYwPSFLLAAGLPLpRQIVVHGHWLC-NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLeNSKLEEDG 378
Cdd:PRK13208 493 GHDIIRtwlFYTIL-RAYLLTGKLPW-KNIMISGMVLDpDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDT 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 379 DFQEAKLYETRELLVSKWgnlinrccgskfNIERAVMKFSDKANFQFQEIFqnEP----IVSErienLAKLLNKSQEVFD 454
Cdd:PRK13208 570 PFDEKQVKIGRRLLTKLW------------NASRFVLHFSADPEPDKAEVL--EPldrwILAK----LAKVVEKATEALE 631
|
.
gi 6321610 455 E 455
Cdd:PRK13208 632 N 632
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
301-521 |
3.04e-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: 60.07 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 301 VIGKDIAKFhtvyWPSFLLAAGLPLPRQ-----IVVHGhwLC---NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENS 372
Cdd:TIGR00422 483 VTGYDIIFF----WVARMIFRSLALTGQvpfkeVYIHG--LVrdeQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLV 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 373 KLEEDGDFQEAKLYETRELLVSKWGnlinrccGSKFnierAVMKFSDKANFQFQEIFQNepiVSER-IenLAKLLNKSQE 451
Cdd:TIGR00422 557 TPGDDINFDWKRVESARNFLNKLWN-------ASRF----VLMNLSDDLELSGGEEKLS---LADRwI--LSKLNRTIKE 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321610 452 VfDEKIAIFQYPQLLRHVWSII-ND-ANTLVQNSKP--WERELDQQDNIIF-LAMETSRILSILCqSIIPSLSQS 521
Cdd:TIGR00422 621 V-RKALDKYRFAEAAKALYEFIwNDfCDWYIELVKYrlYNGNEAEKKAARDtLYYVLDKALRLLH-PFMPFITEE 693
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
338-369 |
3.99e-09 |
|
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: 59.68 E-value: 3.99e-09
10 20 30
....*....|....*....|....*....|..
gi 6321610 338 NGMKMSKSLGNVVDPIDMARYYGADIVRWFLL 369
Cdd:COG0525 519 QGRKMSKSKGNVIDPLDLIDKYGADALRFTLA 550
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
327-369 |
2.28e-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: 57.03 E-value: 2.28e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 6321610 327 RQIVVHGHWL-CNGMKMSKSLGNVVDPIDMARYYGADIVRWFLL 369
Cdd:pfam00133 548 KNVLVHGLVRdEQGRKMSKSLGNVIDPLDVIDKYGADALRLWLA 591
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
17-83 |
1.09e-06 |
|
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: 48.24 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6321610 17 VTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDqPKKFVD 83
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGEN-AKAFVE 66
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
334-369 |
7.44e-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: 48.56 E-value: 7.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 6321610 334 HWLCNGM------KMSKSLGNVVDPIDMARYYGADIVRWFLL 369
Cdd:COG0215 252 YWMHNGFltvngeKMSKSLGNFFTVRDLLKKYDPEVLRFFLL 293
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
334-389 |
1.84e-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: 46.98 E-value: 1.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321610 334 HWLCNGM------KMSKSLGNVVDPIDMARYYGADIVRWFLLE---NSKLeedgDFQEAKLYETR 389
Cdd:pfam01406 240 YWLHNGHvmidgeKMSKSLGNFFTIRDVLKRYDPEILRYFLLSvhyRSPL----DFSEELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
331-369 |
2.74e-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: 45.65 E-value: 2.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 6321610 331 VH-GHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLL 369
Cdd:cd00672 163 LHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALL 202
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
327-366 |
1.32e-04 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 45.15 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6321610 327 RQIVVHGHWLC-NGMKMSKSLGNVVDP---IDMAR------YYGADIVR-W 366
Cdd:PLN02843 596 KSVLTHGFVLDeKGFKMSKSLGNVVDPrlvIEGGKnqkqepAYGADVLRlW 646
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
339-368 |
2.95e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 43.78 E-value: 2.95e-04
10 20 30
....*....|....*....|....*....|
gi 6321610 339 GMKMSKSLGNVVDPIDMARYYGADIVRWFL 368
Cdd:PLN02943 581 GRKMSKTLGNVIDPLDTIKEFGTDALRFTL 610
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
23-154 |
4.29e-04 |
|
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: 43.17 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 23 YPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDQPKKFVDKL-YPEFVQLDKIYGINYT 101
Cdd:pfam00133 33 NATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVVEKKLGIKEKKTRHKYgREEFREKCREWKMEYA 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321610 102 RFIR-----------------TTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDET----FYPESKVIKDP 154
Cdd:pfam00133 113 DEIRkqfrrlgrsidwdreyfTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTalsnLEVEYKDVKGP 186
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
23-67 |
5.57e-04 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 42.84 E-value: 5.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 6321610 23 YPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQ 67
Cdd:PLN02843 42 YANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGLPIE 86
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
339-368 |
8.82e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 42.29 E-value: 8.82e-04
10 20 30
....*....|....*....|....*....|
gi 6321610 339 GMKMSKSLGNVVDPIDMARYYGADIVRWFL 368
Cdd:PRK14900 536 GQKMSKTKGNVIDPLVITEQYGADALRFTL 565
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
334-372 |
1.90e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 41.25 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 6321610 334 HWLCNGM-------KMSKSLGNVVDPIDMARYYGADIVRWFLLeNS 372
Cdd:PLN02882 600 NLICNGLvlaedgkKMSKSLKNYPDPNEVIDKYGADALRLYLI-NS 644
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
338-354 |
1.97e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 41.14 E-value: 1.97e-03
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
23-143 |
2.84e-03 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 40.83 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 23 YPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKI-QCASESNGFDqpKKFVDKLYP-EFVQLDKIYGINY 100
Cdd:COG0060 56 YANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGLPIeLKVEKELGIK--KKDIEKVGIaEFREKCREYALKY 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6321610 101 TR-----FIR------------TTDPDHIENVMklWEL--CLKNGYIYmgehKG----WYSISDET 143
Cdd:COG0060 134 VDeqredFKRlgvwgdwdnpylTMDPEYEESIW--WALkkLYEKGLLY----KGlkpvPWCPRCGT 193
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
341-365 |
3.94e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 40.19 E-value: 3.94e-03
10 20
....*....|....*....|....*
gi 6321610 341 KMSKSLGNVVDPIDMARYYGADIVR 365
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLR 747
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
299-380 |
3.99e-03 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 40.05 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321610 299 IHVIGKDIAK----F----HTVYWPSFllaaglPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLE 370
Cdd:PLN02959 674 LRVSGKDLIQnhltFaiynHTAIWAEE------HWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALAD 747
|
90
....*....|
gi 6321610 371 NSKLEEDGDF 380
Cdd:PLN02959 748 AGDGVDDANF 757
|
|
| lysK |
PRK00750 |
lysyl-tRNA synthetase; Reviewed |
338-373 |
7.14e-03 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234829 [Multi-domain] Cd Length: 510 Bit Score: 39.02 E-value: 7.14e-03
10 20 30
....*....|....*....|....*....|....*.
gi 6321610 338 NGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSK 373
Cdd:PRK00750 277 KGEKISKSKGNVITIEDWLEYAPPESLRLFMFARPK 312
|
|
| |
