|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
5-514 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 894.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 5 TPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMG 84
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 85 QLLNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYqeDETELRADGVRYGPQGTPVEWVEEAS 164
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFY--TESELIEDGYRCPPTGAPVEWVEEES 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 165 YFFRLSDYQDRLLKLYEEQPDFIGPAERRNEVISFVKSGLKDLSVSRTTFDWGIPVPDDPDHVMYVWVDALTNYVTATGY 244
Cdd:PRK11893 159 YFFRLSKYQDKLLELYEANPDFIQPASRRNEVISFVKSGLKDLSISRTNFDWGIPVPGDPKHVIYVWFDALTNYLTALGY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 245 LTDE---TGPRAKFWPADLHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGFLLNKGEKMSKSLGNVVDPVNLVEHFG 321
Cdd:PRK11893 239 PDDEellAELFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPFDLVDEYG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 322 LDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRSLSMIVKNCEGAVPVCGDLSEADAAILATADALVETV 401
Cdd:PRK11893 319 VDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPEPGALTEADEALLEAAAALLERV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 402 RAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKKTDPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLDLVAVPE 481
Cdd:PRK11893 399 RAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPERLATVLYTLLEVLRGIAVLLQPVMPELAAKILDQLGVEE 478
|
490 500 510
....*....|....*....|....*....|....
gi 1129126296 482 EK-RSFAFLgQAGRLVAGTPLSAPTPVFPRYQPP 514
Cdd:PRK11893 479 DEnRDFAAL-SWGRLAPGTTLPKPEPIFPRLEEE 511
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
2-517 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 787.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 2 TTKTPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFR 81
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 82 KMGQLLNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYqeDETELrADGVRYGPQGTPVEWVE 161
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFF--TESQL-VDGGKCPDCGREVELVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 162 EASYFFRLSDYQDRLLKLYEEQPDFIGPAERRNEVI-SFVKSGLKDLSVSRTTFDWGIPVPDDPDHVMYVWVDALTNYVT 240
Cdd:PRK12267 158 EESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMInNFIKPGLEDLSISRTSFDWGIPVPFDPKHVVYVWIDALLNYIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 241 ATGYLTDETGPRAKFWPADLHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGFLLNKGEKMSKSLGNVVDPVNLVEHF 320
Cdd:PRK12267 238 ALGYGSDDDELFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPEELVDRY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 321 GLDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRSLSMIVKNCEGAVPVCGDLSEADAAILATADALVET 400
Cdd:PRK12267 318 GLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPAPGNVTEFDEELIALAEETLKN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 401 VRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKK--TDPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLDLVA 478
Cdd:PRK12267 398 YEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKdeGKKERLATVMYHLAESLRKVAVLLSPFMPETSKKIFEQLG 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 1129126296 479 VPEEKRSFAFLGQAGRLVAGTPLSAPTPVFPRYQPPAEA 517
Cdd:PRK12267 478 LEEELTSWESLLEWGGLPAGTKVAKGEPLFPRIDVEEEI 516
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
6-517 |
0e+00 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 782.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 6 PYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQ 85
Cdd:COG0143 2 KFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 86 LLNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYQED----------ETELRAD-----GVRY 150
Cdd:COG0143 82 KLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDRyvegtcpkcgAEDAYGDqcencGATL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 151 GP----------QGTPVEWVEEASYFFRLSDYQDRLLKLYEEQPDfIGPaERRNEVISFVKSGLKDLSVSRTtFDWGIPV 220
Cdd:COG0143 162 EPtelinprsaiSGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQP-EVRNEVLSWLKEGLQDLSISRD-FDWGIPV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 221 PDDPDHVMYVWVDALTNYVTAT-GYLTDETGPRA--KFWPAD----LHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAH 293
Cdd:COG0143 239 PGDPGKVFYVWFDALIGYISATkGYADDRGLPEDfeKYWPAPdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKVFAH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 294 GFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRSLSMIVKNC 373
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIHKYF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 374 EGAVPVCGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKKT-DPARMATVLYVTA 452
Cdd:COG0143 399 DGKVPEPGELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDeDPERLATVLYTLL 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129126296 453 EVVRQIALLLQPFMPGSSAKLLDLVAVPEEKRSFAFLGQagRLVAGTPLSAPTPVFPRYQPPAEA 517
Cdd:COG0143 479 EALRILAILLKPFLPETAEKILEQLGLEGDELTWEDAGW--PLPAGHKIGKPEPLFPRIEDEQIE 541
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
7-510 |
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: 542.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 7 YYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQL 86
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 87 LNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAY----YQEDETELRADGVRYGPQ--------- 153
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFlpdrYVEGTCPKCGSEDARGDHcevcgrhle 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 154 ------------GTPVEWVEEASYFFRLSDYQDRLLKLYEEQPDFIGPAERRNEVI-SFVKSGLKDLSVSRTTFDWGIPV 220
Cdd:TIGR00398 161 ptelinprckicGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAqNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 221 PDDPDHVMYVWVDALTNYVTATGYLTDETGPRAKFWPAD-----LHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGF 295
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISSLGILSGDTEDWKKWWNNDedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 296 LLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRSLSMIVKNCEG 375
Cdd:TIGR00398 321 LTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKYFNG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 376 AVPVCGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKKTDPaRMATVLYVTAEVV 455
Cdd:TIGR00398 401 VLPSEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSP-RLKELLAVCSMLI 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1129126296 456 RQIALLLQPFMPGSSAKLLDLVAVPEEKrsfaflGQAGRLVAGTPLSAPTPVFPR 510
Cdd:TIGR00398 480 RVLSILLYPIMPKLSEKILKFLNFELEW------DFKLKLLEGHKLNKAEPLFSK 528
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
6-341 |
0e+00 |
|
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: 511.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 6 PYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQ 85
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 86 LLNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYqedetelradgvrygpqgtpVEWVEEASY 165
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFL--------------------PEWREEEHY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 166 FFRLSDYQDRLLKLYEEQPDFIGPAERRNEVISFVKSGLKDLSVSRTTFDWGIPVPDDPDHVMYVWVDALTNYVTATGYL 245
Cdd:cd00814 141 FFRLSKFQDRLLEWLEKNPDFIWPENARNEVLSWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDALIGYISATGYY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 246 TDETG---PRAKFWPADLHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGFLLNKGEKMSKSLGNVVDPVNLVEHFGL 322
Cdd:cd00814 221 NEEWGnswWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGA 300
|
330
....*....|....*....
gi 1129126296 323 DQIRYFFLREVSFGQDGSY 341
Cdd:cd00814 301 DALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
7-365 |
2.05e-161 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 463.30 E-value: 2.05e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 7 YYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQL 86
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 87 LNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYQEDETE--------LRADGVRYGPQGTPVE 158
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEgtcphcgsEDARGDQCENCGRHLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 159 ----------------WV-EEASYFFRLSDYQDRLLKLYEEqPDFIGPAERRNEVISFVKSGLKDLSVSRtTFDWGIPVP 221
Cdd:pfam09334 161 ptelinpkcvicgttpEVkETEHYFFDLSKFQDKLREWIEE-NNPEWPENVKNMVLEWLKEGLKDRAISR-DLDWGIPVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 222 DDPDHVMYVWVDALTNYVTATGYLTDETGPRAKFWPAD-----LHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGFL 296
Cdd:pfam09334 239 GAEGKVFYVWLDAPIGYISATKELSGNEEKWKEWWPNDpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHGYL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129126296 297 LNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRS 365
Cdd:pfam09334 319 TYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
7-512 |
5.44e-136 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 406.79 E-value: 5.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 7 YYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQL 86
Cdd:PLN02224 71 FVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLWKD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 87 LNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYyqEDETELRADGVRYGPQgTPVEWVEEASYF 166
Cdd:PLN02224 151 LDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEY--KDEKELLENNCCPVHQ-MPCVARKEDNYF 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 167 FRLSDYQDRLLKLYEEQPDFIGPAERRNEVISFVKSGLKDLSVSRTTFDWGIPVPDDPDHVMYVWVDALTNYVTAtgyLT 246
Cdd:PLN02224 228 FALSKYQKPLEDILAQNPRFVQPSYRLNEVQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWFDALLGYISA---LT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 247 DETGPR-----AKF-WPADLHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAHGFLLNKGEKMSKSLGNVVDPVNLVEHF 320
Cdd:PLN02224 305 EDNKQQnletaVSFgWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGFLTKDGMKMGKSLGNTLEPFELVQKF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 321 GLDQIRYFFLREVSFGQDGSYSEEGIATRINADLANGIGNLASRSLSMIVKNCEGAVPVCGDLSEADAAILATADALVET 400
Cdd:PLN02224 385 GPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKNCESTLVEDSTVAAEGVPLKDTVEKLVEK 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 401 VRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKK---TDPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLDLV 477
Cdd:PLN02224 465 AQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKqggVSAEEAAKDLVIILEVMRVIAVALSPIAPCLSLRIYSQL 544
|
490 500 510
....*....|....*....|....*....|....*..
gi 1129126296 478 AVPEEKRSFAFLGQA--GRLVAGTPLSAPTPVFPRYQ 512
Cdd:PLN02224 545 GYSEDQFNSITWSDTkwGGLKGGQVMEQASPVFARIE 581
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
4-510 |
1.63e-114 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 353.30 E-value: 1.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 4 KTPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKM 83
Cdd:PRK00133 1 MRKILVTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 84 GQLLNASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSgwysvrdEAYYQEDETELrADgvR-------------- 149
Cdd:PRK00133 81 FAGFGISFDNYGSTHSEENRELAQEIYLKLKENGYIYEKTIE-------QLYDPEKGMFL-PD--Rfvkgtcpkcgaedq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 150 YGPQ---------------------GTPVEWVEEASYFFRLSDYQDRLLKLYEEQPDfiGPAERRNEVISFVKSGLKDLS 208
Cdd:PRK00133 151 YGDNcevcgatysptelinpksaisGATPVLKESEHFFFKLPRFEEFLKEWITRSGE--LQPNVANKMKEWLEEGLQDWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 209 VSRTTfDW-GIPVPDDPDHVMYVWVDALTNYVTATGYLTDETGPR--AKFWPAD-----LHMIGKDIIRFHTVYWPAFLM 280
Cdd:PRK00133 229 ISRDA-PYfGFEIPGAPGKVFYVWLDAPIGYISSTKNLCDKRGGLdwDEYWKKDsdtelYHFIGKDIIYFHTLFWPAMLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 281 SAGLPLPKRVFAHGFL-LNkGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFG-QDGSYSEEGIATRINADLANGI 358
Cdd:PRK00133 308 GAGYRLPTNVFAHGFLtVE-GAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETiDDLDFNWEDFQQRVNSELVGKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 359 GNLASRSLSMIVKNCEGAVPvcgdLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKK 438
Cdd:PRK00133 387 VNFASRTAGFINKRFDGKLP----DALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAK 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129126296 439 TDPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLDLVAVPEEKrsfafLGQAGRLVAGTPLSAPTPVFPR 510
Cdd:PRK00133 463 QDGERLQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEELT-----WDDAQQPLAGHPINKFKILFTR 529
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
6-338 |
1.43e-79 |
|
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: 251.18 E-value: 1.43e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 6 PYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRE-------------NMTAKEL 72
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKggrkkktiwieefREDPKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 73 ADRNSAEFRKMGQLLNASND--DFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSgwysvrdeayyqedetelradgVRY 150
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHP----------------------VRI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 151 GPQgtpvewveeasYFFRLSDYQDRLLKLYEEQPdfIGPAERRNEVISFVKSgLKDLSVSRTTFdWGIPVPDDpdhVMYV 230
Cdd:cd00668 139 TEQ-----------WFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLES-LLDWAISRQRY-WGTPLPED---VFDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 231 WVDALTNYVTATGYLTDETGPRaKFWPADLHMIGKDIIRFHTVYWPAFLMSAGLPLP-KRVFAHGFLL-NKGEKMSKSLG 308
Cdd:cd00668 201 WFDSGIGPLGSLGYPEEKEWFK-DSYPADWHLIGKDILRGWANFWITMLVALFGEIPpKNLLVHGFVLdEGGQKMSKSKG 279
|
330 340 350
....*....|....*....|....*....|
gi 1129126296 309 NVVDPVNLVEHFGLDQIRYFFLREVSFGQD 338
Cdd:cd00668 280 NVIDPSDVVEKYGADALRYYLTSLAPYGDD 309
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
350-475 |
2.97e-49 |
|
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: 165.74 E-value: 2.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 350 INADLANGIGNLASRSLSMIVKNCEGAVPVCGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFA 429
Cdd:cd07957 1 INSELANNLGNLVNRTLNMASKYFGGVVPEFGGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1129126296 430 GQEPWALKKT-DPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLD 475
Cdd:cd07957 81 ETAPWKLAKEeDPERLATVLYVLLELLRILAILLSPFMPETAEKILD 127
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
9-508 |
5.62e-47 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 174.97 E-value: 5.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 9 ITTAISYPNGRPHIGHAYE-LIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQLL 87
Cdd:PLN02610 21 ITSALPYVNNVPHLGNIIGcVLSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKEVYDWF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 88 NASNDDFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYS------VRDEAYYQEDETE------LRAD-----GVRY 150
Cdd:PLN02610 101 DISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCdtcqkfLADRLVEGTCPTEgcnydsARGDqcekcGKLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 151 GP-----------QGTPVewVEEASY-FFRLSDYQDRLLKLYEEQPdfIGPAERRNEVI---SFVKSGLKDLSVSRTtFD 215
Cdd:PLN02610 181 NPtelidpkckvcKNTPR--IRDTDHlFLELPLLKDKLVEYINETS--VAGGWSQNAIQttnAWLRDGLKPRCITRD-LK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 216 WGIPVPDD--PDHVMYVWVDALTNYVTATGYLTDETgprAKFW--PADLHM---IGKDIIRFHTVYWPAFLMSAGLP--L 286
Cdd:PLN02610 256 WGVPVPLEkyKDKVFYVWFDAPIGYVSITACYTPEW---EKWWknPENVELyqfMGKDNVPFHTVMFPSTLLGTGENwtM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 287 PKRVFAHGFLLNKGEKMSKS-----LGNVVDPVNL-VEHFgldqiRYFFLR---EVSfgqDGSYSEEGIATRINADLANG 357
Cdd:PLN02610 333 MKTISVTEYLNYEGGKFSKSkgvgvFGNDAKDTNIpVEVW-----RYYLLTnrpEVS---DTLFTWADLQAKLNSELLNN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 358 IGNLASRSLSMIVKNC----EGAVPvcgDLSEADAAILATADA-----LVETVRAEMNALAIHKALAAIIALVSEGDRYF 428
Cdd:PLN02610 405 LGNFINRVLSFIAKPPgagyGSVIP---DAPGAESHPLTKKLAekvgkLVEQYVEAMEKVKLKQGLKTAMSISSEGNAYL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 429 AGQEPWALKKTDPARMATVLYVTAEVVRQIALLLQPFMPGSSAKLLDLVAVPEEKRSF----AFLGQAGR----LVAGTP 500
Cdd:PLN02610 482 QESQFWKLYKEDKPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNLPPESLSLsdekGEVARAKRpwelVPAGHK 561
|
....*...
gi 1129126296 501 LSAPTPVF 508
Cdd:PLN02610 562 IGTPEPLF 569
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
6-338 |
7.62e-36 |
|
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: 137.38 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 6 PYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHG--------------QKMQQTAKRENMTAK- 70
Cdd:cd00817 2 VFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGiatqvvvekklgieGKTRHDLGREEFLEKc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 71 -ELADRNSAEFRKMGQLLNASND--DFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEayyqedeTELRADG 147
Cdd:cd00817 82 wEWKEESGGKIREQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLR-------TAISDIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 148 VRYgPQGTPVEWVEEASYFFRLSDYQDRLLKLYEEQPDFIGPAERRNEVISFVKSgLKDLSVSRTTFdWGIPVP------ 221
Cdd:cd00817 155 VCS-RSGDVIEPLLKPQWFVKVKDLAKKALEAVKEGDIKFVPERMEKRYENWLEN-IRDWCISRQLW-WGHRIPawyckd 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 222 -------------------------------DDPDhVMYVWVD-ALTNYVTaTGYLtDETGPRAKFWPADLHMIGKDIIR 269
Cdd:cd00817 232 gghwvvareedeaidkaapeacvpcggeelkQDED-VLDTWFSsSLWPFST-LGWP-EETKDLKKFYPTSLLVTGHDIIF 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129126296 270 FhtvyWPAFLMSAGLPL----P-KRVFAHGFLLNK-GEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQD 338
Cdd:cd00817 309 F----WVARMIMRGLKLtgklPfKEVYLHGLVRDEdGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGRD 379
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
15-338 |
3.11e-33 |
|
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: 128.89 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 15 YPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHG--------QKMQQTAKR--ENMT-------AKELADRNS 77
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGlpielkveKELGISGKKdiEKMGiaefnakCREFALRYV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 78 AE----FRKMGQLLNASNDdfIRTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRdeayyqedeteLRAdgvrygpq 153
Cdd:cd00818 91 DEqeeqFQRLGVWVDWENP--YKTMDPEYMESVWWVFKQLHEKGLLYRGYKVVPWPLI-----------YRA-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 154 gTPvewveeaSYFFRLSDYQDRLLKLYEE---QPDFIgpaerRNEVISFVKsGLKDLSVSRTTFdWGIPVP----DDPDH 226
Cdd:cd00818 150 -TP-------QWFIRVTKIKDRLLEANDKvnwIPEWV-----KNRFGNWLE-NRRDWCISRQRY-WGTPIPvwycEDCGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 227 --------VMYVWVDALTNYVTATGYLTDETGPRAKfWPADLHMIGKDIIR--FHTvywpAFLMSAGL---PLPKRVFAH 293
Cdd:cd00818 215 vlvrrvpdVLDVWFDSGSMPYAQLHYPFENEDFEEL-FPADFILEGSDQTRgwFYS----LLLLSTALfgkAPYKNVIVH 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1129126296 294 GFLLN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQD 338
Cdd:cd00818 290 GFVLDeDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-330 |
9.42e-33 |
|
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: 126.98 E-value: 9.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 7 YYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQL 86
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 87 LNASND--DFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYsgwysvrdeayyqedetelradgvrygpqgtPVEW-VEEA 163
Cdd:cd00812 82 MGFSYDwrREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEA-------------------------------PVNWcKLLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 164 SYFFRLS--DYQDRLLKLYEEQPDFigPAErrnevisfVKSGLKD-LSVSRTTFdWGIPVP-DDpdhVMYVWVDA----- 234
Cdd:cd00812 131 QWFLKYSetEWKEKLLKDLEKLDGW--PEE--------VRAMQENwIGCSRQRY-WGTPIPwTD---TMESLSDStwyya 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 235 --LTNYVTATGYLTDETGPRAKF--W-PADLHMIGKDIIRFHTVY---WPAFLMSAGLPL---PKRVFAHGFLLNKGEKM 303
Cdd:cd00812 197 ryTDAHNLEQPYEGDLEFDREEFeyWyPVDIYIGGKEHAPNHLLYsrfNHKALFDEGLVTdepPKGLIVQGMVLLEGEKM 276
|
330 340
....*....|....*....|....*..
gi 1129126296 304 SKSLGNVVDPVNLVEHFGLDQIRYFFL 330
Cdd:cd00812 277 SKSKGNVVTPDEAIKKYGADAARLYIL 303
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
3-467 |
4.45e-26 |
|
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: 112.46 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 3 TKTPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHG----QKMQQTAKRENMTaKELADRNsa 78
Cdd:TIGR00422 31 NKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGiatqVKVEKKLGAEGKT-KHDLGRE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 79 EFRKMGQLLNASNDDFIR-----------------TTEPRHHEAVTAIWKRMAANGDIYKDSY----------------- 124
Cdd:TIGR00422 108 EFREKIWEWKEESGGTIKnqikrlgasldwsrerfTMDEGLSKAVKEAFVRLYEKGLIYRGEYlvnwdpklntaisdiev 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 125 -------SGWY----------------SVRDE--------AYYQEDE--------------------------------- 140
Cdd:TIGR00422 188 eykevkgKLYYiryplangskdylvvaTTRPEtmfgdtavAVHPEDErykhligkkvilpltgrkipiiadeyvdmefgt 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 141 ------------------------------------------------------TELRADG-----------VRYGPQ-G 154
Cdd:TIGR00422 268 gavkvtpahdfndyewgkrhnlefinildedgllnenagkyqgltrfearkkivEDLKEEGllvkiephthnVGTCWRsG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 155 TPVEWVEEASYFFRLSDYQDRLLK-LYEEQPDFIgPAERRNEVISFVKSgLKDLSVSRTTFdWGIPVPddpdhVMY---- 229
Cdd:TIGR00422 348 TVVEPLLSKQWFVKVEKLADKALEaAEEGEIKFV-PKRMEKRYLNWLRN-IKDWCISRQLI-WGHRIP-----VWYckec 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 230 --VWV---DALTNYVTATGYLT--------------------------DETGPRAKFWPADLHMIGKDIIRFhtvyWPAF 278
Cdd:TIGR00422 420 geVYVakeEPLPDDKTNTGPSVeleqdtdvldtwfssslwpfstlgwpDETKDLKKFYPTDLLVTGYDIIFF----WVAR 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 279 LMSAGLPL----P-KRVFAHGFLLN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLREVSFGQDGSYSEEGIATriNA 352
Cdd:TIGR00422 496 MIFRSLALtgqvPfKEVYIHGLVRDeQGRKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVES--AR 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 353 DLANGIGNlASRSLSMIVKNCEGAVPVCGDLSEADAAILATADALVETVRaemNALAIHKALAAIIALVS-----EGDRY 427
Cdd:TIGR00422 574 NFLNKLWN-ASRFVLMNLSDDLELSGGEEKLSLADRWILSKLNRTIKEVR---KALDKYRFAEAAKALYEfiwndFCDWY 649
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1129126296 428 --FAGQEPWAlkkTDPARMATVLYVTAEVVRQIALLLQPFMP 467
Cdd:TIGR00422 650 ieLVKYRLYN---GNEAEKKAARDTLYYVLDKALRLLHPFMP 688
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
154-467 |
1.21e-20 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 95.64 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 154 GTPVEWVEEASYFFRLSDYQDRLLKLYEEQpDFIgPAERRNEVISFVKsGLK-DLSVSRTTFdWGIPVP----DDPDH-- 226
Cdd:PRK13208 347 DTPLEILVTRQWFIKVLDLKEELLERGKEI-NWY-PEHMRVRLENWIE-GLNwDWCISRQRY-FGTPIPvwycKDCGHpi 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 227 ----------------------------------VMYVWVD-ALTNYVtATGYLTDETGpRAKFWPADLHMIGKDIIR-- 269
Cdd:PRK13208 423 lpdeedlpvdptkdeppgykcpqcgspgfegetdVMDTWATsSITPLI-VTGWERDEDL-FEKVFPMDLRPQGHDIIRtw 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 270 -FHTVYwPAFLMSAGLPLpKRVFAHGFLLN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLrEVSFGQDGSYSEEGIa 347
Cdd:PRK13208 501 lFYTIL-RAYLLTGKLPW-KNIMISGMVLDpDGKKMSKSKGNVVTPEELLEKYGADAVRYWAA-SARLGSDTPFDEKQV- 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 348 tRINADLANGIGNlASRSLSMIVKNCEGAVPVcgDLSEADAAILATADALVETVRAEMNALAIHKALAAI---------- 417
Cdd:PRK13208 577 -KIGRRLLTKLWN-ASRFVLHFSADPEPDKAE--VLEPLDRWILAKLAKVVEKATEALENYDFAKALEEIesffwhvfcd 652
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1129126296 418 --IALVSegDRYFAGQEPwalkktDPARMAtvLYVTAEVVRQIALLLQPFMP 467
Cdd:PRK13208 653 dyLELVK--SRAYGEDEE------EEQKSA--RYTLYTVLDTLLRLLAPFLP 694
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
247-467 |
1.11e-18 |
|
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: 89.73 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 247 DETGPRAKFWPADLHMIGKDIIRFhtvyWPAFLMSAGL----PLP-KRVFAHGFLL-NKGEKMSKSLGNVVDPVNLVEHF 320
Cdd:COG0525 465 EKTEDLKYFYPTSVLVTGFDIIFF----WVARMIMMGLhftgEVPfKDVYIHGLVRdEQGRKMSKSKGNVIDPLDLIDKY 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 321 GLDQIRYFFLREVSFGQDGSYSEEgiatRINA--DLANGIGNlASRSLSMivkNCEGAV----PVCGDLSEADAAILATA 394
Cdd:COG0525 541 GADALRFTLAALASPGRDIKFDEE----RVEGyrNFANKLWN-ASRFVLM---NLEGFDpgldPDPEELSLADRWILSRL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 395 DALVETVRAEMNALAIHKALAAIIALVsegdryfagqepW-------------ALKKTDPARMATVLYVTAEVVRQIALL 461
Cdd:COG0525 613 NKTIAEVTEALEKYRFDEAAQALYDFV------------WnefcdwylelakpRLYGGDEAAKRETRATLVYVLEQILRL 680
|
....*.
gi 1129126296 462 LQPFMP 467
Cdd:COG0525 681 LHPFMP 686
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
247-467 |
1.66e-17 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 85.93 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 247 DETGPRAKFWPADLHMIGKDIIRFhtvyWPAFLMSAGLPL----P-KRVFAHGFLL-NKGEKMSKSLGNVVDPVNLVEHF 320
Cdd:PRK05729 463 EKTEDLKRFYPTSVLVTGFDIIFF----WVARMIMMGLHFtgqvPfKDVYIHGLVRdEQGRKMSKSKGNVIDPLDLIDKY 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 321 GLDQIRYFFLREVSFGQDGSYSEEgiatRINA--DLANGIGNlASRSLSMivkNCEGAV----PVCGDLSEADAAILATA 394
Cdd:PRK05729 539 GADALRFTLAALASPGRDIRFDEE----RVEGyrNFANKLWN-ASRFVLM---NLEGADvgelPDPEELSLADRWILSRL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 395 DALVETVRAEMNALAIHKALAAIialvsegdrY-FAgqepW---------ALKKT-DPARMATVLYVTAEVVRQIALLLQ 463
Cdd:PRK05729 611 NRTVAEVTEALDKYRFDEAARAL---------YeFI----WnefcdwyleLAKPVlQEAAKRATRATLAYVLEQILRLLH 677
|
....
gi 1129126296 464 PFMP 467
Cdd:PRK05729 678 PFMP 681
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
256-467 |
4.13e-17 |
|
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: 84.75 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 256 WPADLHMIGKDIIR--FHTvywpAFLMSAGL----PLpKRVFAHGFLL-NKGEKMSKSLGNVVDPVNLVEHFGLDQIRYF 328
Cdd:COG0060 555 FPADFYLEGSDQTRgwFYS----SLLTSTALfgraPY-KNVLTHGFVLdEDGRKMSKSLGNVVDPQEVIDKYGADILRLW 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 329 FLReVSFGQDGSYSEEGIATRinADLANGIGNLAsRSLSMIVKN---CEGAVPVcGDLSEADAAILATADALVETVRAEM 405
Cdd:COG0060 630 VAS-SDYWGDLRFSDEILKEV--RDVYRRLRNTY-RFLLANLDDfdpAEDAVPY-EDLPELDRWILSRLNELIKEVTEAY 704
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129126296 406 NALAIHKALAAIIALVSEG----------DRYfagqepWALKKTDPARMA--TVLYvtaEVVRQIALLLQPFMP 467
Cdd:COG0060 705 DNYDFHRAYRALHNFCVEDlsnwyldiskDRL------YTEAADSLDRRAaqTTLY---EVLETLVRLLAPILP 769
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
255-467 |
4.84e-15 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 78.50 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 255 FWPADLHMIGKDIIRFhtvyWPAFLMSAGL----PLPKR-VFAHGFLLN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRYF 328
Cdd:PRK14900 489 FYPTSVMETGHDIIFF----WVARMMMMGLhfmgEVPFRtVYLHPMVRDeKGQKMSKTKGNVIDPLVITEQYGADALRFT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 329 FLREVSFGQDGSYSEEGIATRinADLANGIGNlASRSLSMivkNCEGAVPVCGDLSE-----ADAAILATADALVETVRA 403
Cdd:PRK14900 565 LAALTAQGRDIKLAKERIEGY--RAFANKLWN-ASRFALM---NLSGYQERGEDPARlartpADRWILARLQRAVNETVE 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1129126296 404 EMNALAIHKALAAIIALV-SEGDRYFAGQEPWALKKTDPARMATVLYVTAEVVRQIALLLQPFMP 467
Cdd:PRK14900 639 ALEAFRFNDAANAVYAFVwHELCDWYIELAKEALASEDPEARRSVQAVLVHCLQTSYRLLHPFMP 703
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
223-338 |
3.38e-12 |
|
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: 68.98 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 223 DPDhVMYVWVD-ALTNYVTaTGYLTDETGPRAKFWPADLHMIGKDIIRFhtvyWPAFLMSAGLPL----P-KRVFAHGFL 296
Cdd:pfam00133 483 DED-VLDTWFSsGSWPFST-LGWPFVNTEEFKKFFPADMLLEGSDQTRG----WFYRMIMLSTALtgsvPfKNVLVHGLV 556
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1129126296 297 LN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRyFFLREVSFGQD 338
Cdd:pfam00133 557 RDeQGRKMSKSLGNVIDPLDVIDKYGADALR-LWLANSDYGRD 598
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
15-142 |
1.31e-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: 67.05 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 15 YPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQ--TAK-------------RENMTAK------ELA 73
Cdd:pfam00133 33 NATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQvvEKKlgikekktrhkygREEFREKcrewkmEYA 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129126296 74 DRNSAEFRKMGQLLNASNDDFirTTEPRHHEAVTAIWKRMAANGDIYKDSYSGWYSVRDEAYYQEDETE 142
Cdd:pfam00133 113 DEIRKQFRRLGRSIDWDREYF--TMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNTALSNLEVE 179
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
290-467 |
1.98e-11 |
|
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: 66.61 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 290 VFAHGFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFflrEVSFG---QDGSYSEEGIAtrinadlanGignlASRSL 366
Cdd:COG0495 577 VGKDGVVIGGIEKMSKSKGNVVDPDEIIEKYGADTLRLF---EMFAGppeRDLEWSDSGVE---------G----AYRFL 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 367 S----MIVKNCEGAVPVCGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSegdryfagqepwALKKTDPA 442
Cdd:COG0495 641 NrvwrLVVDEAEALKLDVADLSEADKELRRALHKTIKKVTEDIERLRFNTAIAALMELVN------------ALYKAKDS 708
|
170 180
....*....|....*....|....*
gi 1129126296 443 RMATvLYVTAEVVRQIALLLQPFMP 467
Cdd:COG0495 709 GEAD-RAVLREALETLVLLLAPFAP 732
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
9-82 |
4.63e-10 |
|
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: 57.87 E-value: 4.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1129126296 9 ITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRK 82
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKE 74
|
|
| Anticodon_3 |
pfam19303 |
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ... |
377-504 |
1.66e-09 |
|
Anticodon binding domain of methionyl tRNA ligase; This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase.
Pssm-ID: 437135 [Multi-domain] Cd Length: 152 Bit Score: 56.36 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 377 VPVCGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFAGQEPWALKKTDPARMATVLYVTAEVVR 456
Cdd:pfam19303 1 VPEGGAYGEAEAALIADLTTRLAAYEGHMEAMEVRKAAAELRAIWVAGNEYLQEAAPWTTFKTDPEAAAAQVRLALNLIR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1129126296 457 QIALLLQPFMPGSSAKLLDlvAVPEEKRSFAFLGQA--GRLVAGTPLSAP 504
Cdd:pfam19303 81 LYAVLSAPFIPDAAAAMLA--AMGTDDAAWPDDVAAalTALPAGHAFTVP 128
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
228-467 |
2.72e-09 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 59.78 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 228 MYVWVDALTNYvtaTGYLTDETGPRakfWPADLHMIGKDIIR--FHTvywpAFLMS---AGLPLPKRVFAHGFLLN-KGE 301
Cdd:PLN02843 541 MDVWFDSGSSW---AGVLGSREGLS---YPADLYLEGSDQHRgwFQS----SLLTSvatKGKAPYKSVLTHGFVLDeKGF 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 302 KMSKSLGNVVDPVNLVE---------HFGLDQIRYF-----FLREVSFGQDGSYSEEGIATRINADLANGIGNLASRsls 367
Cdd:PLN02843 611 KMSKSLGNVVDPRLVIEggknqkqepAYGADVLRLWvasvdYTGDVLIGPQILKQMSDIYRKLRGTLRYLLGNLHDW--- 687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 368 mivkNCEGAVPVCgDLSEADAAILATADALVETVRAEMNALAIHKALAAI--IALVSEGDRYF--AGQEPWALKKTDPAR 443
Cdd:PLN02843 688 ----KPDNAVPYE-DLPSIDKYALFQLENVVNEIEESYDNYQFFKIFQILqrFTIVDLSNFYLdvAKDRLYVGGTTSFTR 762
|
250 260
....*....|....*....|....*.
gi 1129126296 444 MA--TVLyvtAEVVRQIALLLQPFMP 467
Cdd:PLN02843 763 RScqTVL---AAHLLSLLRAIAPILP 785
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
254-486 |
7.38e-09 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 58.41 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 254 KFWPADLHMIGKDIIRFhtvyWPAFLMSAGL----PLP-KRVFAHGFLLN-KGEKMSKSLGNVVDPVNLVEHFGLDQIRy 327
Cdd:PLN02943 533 KFYPTTVLETGHDILFF----WVARMVMMGIeftgTVPfSYVYLHGLIRDsQGRKMSKTLGNVIDPLDTIKEFGTDALR- 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 328 FFLREVSFGQDGSYSEEGIATriNADLANGIGNLAsrslSMIVKNcegaVPVCGDLSEADAAILATADALVETVRAEMNA 407
Cdd:PLN02943 608 FTLALGTAGQDLNLSTERLTS--NKAFTNKLWNAG----KFVLQN----LPSQSDTSAWEHILACKFDKEESLLSLPLPE 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 408 LAIHKALAAIIALVSEG-DRYF---AGQEPWALKKTD---------PARM-------------ATVLYVTAEVVRqialL 461
Cdd:PLN02943 678 CWVVSKLHELIDSVTTSyDKYFfgdVGREIYDFFWSDfadwyieasKTRLyhsgdnsalsraqAVLLYVFENILK----L 753
|
250 260
....*....|....*....|....*
gi 1129126296 462 LQPFMPGSSAKLLDlvAVPEEKRSF 486
Cdd:PLN02943 754 LHPFMPFVTEELWQ--ALPYRKEAL 776
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
293-454 |
3.27e-08 |
|
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: 55.88 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 293 HGFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFL----REVsfgQDgsYSEEGIATrinadlangignlASRSLSM 368
Cdd:COG0215 256 NGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahyRSP---LD--FSEEALEE-------------AEKALER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 369 IvkncEGAVPVCGDLSEADAAILATADALVETVRAEMNA-LAIHKALAAIIALVSEGDRYFAGQEpwalKKTDPARMATV 447
Cdd:COG0215 318 L----YNALRRLEEALGAADSSAEEIEELREEFIAAMDDdFNTPEALAVLFELVREINKALDEGE----DKAALAALAAL 389
|
....*..
gi 1129126296 448 LYVTAEV 454
Cdd:COG0215 390 LRALGGV 396
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
2-177 |
3.96e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 55.98 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 2 TTKTPYYITTAISYPNGRP-HIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEF 80
Cdd:PLN02563 107 TSKPKFYVLDMFPYPSGAGlHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARF 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 81 RKMGQLLNASND--DFIRTTEPRHHEAVTAIWKRMAANGDIYKDSYS-GWYSVRDEAYYQEDETelraDGV-RYGpqGTP 156
Cdd:PLN02563 187 RSQLKSLGFSYDwdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPvNWCPALGTVLANEEVV----DGLsERG--GHP 260
|
170 180
....*....|....*....|.
gi 1129126296 157 VEWVEEASYFFRLSDYQDRLL 177
Cdd:PLN02563 261 VIRKPMRQWMLKITAYADRLL 281
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
247-323 |
1.52e-07 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 54.24 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 247 DETGPRAKFWPADLHMIGKDIIRFhtvyWPA--FLMSAGL--PLP-KRVFAHGFLLNK-GEKMSKSLGNVVDPVNLVEHF 320
Cdd:PTZ00419 528 DQTDDLQRFFPTSLLETGSDILFF----WVArmVMMSLHLtdKLPfKTVFLHAMVRDSqGEKMSKSKGNVIDPLEVIEGI 603
|
...
gi 1129126296 321 GLD 323
Cdd:PTZ00419 604 SLQ 606
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
289-330 |
2.77e-07 |
|
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: 51.43 E-value: 2.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1129126296 289 RVFAH-GFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFL 330
Cdd:cd00672 160 RYWLHtGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALL 202
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
20-347 |
2.97e-06 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 48.90 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 20 PHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELADRNSAEFRKMGQLLNASNDDFirttE 99
Cdd:pfam01406 23 SHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALNVLPPDL----E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 100 PRHHEAVTAIwKRM------------AANGDIYkdsysgwYSVRDEAYYQE------DETELRADGVRYGPQGTPVEWVe 161
Cdd:pfam01406 99 PRVTEHIDEI-IEFierlikkgyayvSDNGDVY-------FDVSSFPDYGKlsgqnlEQLEAGARGEVSEGKRDPLDFA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 162 easyffrlsdyqdrLLKLYEE-QPDFIGPaerrnevisfvksglkdlsvsrttfdWGIPVPDdpdhvmyvWvdALTNYVT 240
Cdd:pfam01406 170 --------------LWKASKEgEPSWDSP--------------------------WGKGRPG--------W--HIECSAM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 241 ATGYLTDETgprakfwpaDLHMIGKDIIRFHTVYWPAFLMSAGLPLPKRVFAH-GFLLNKGEKMSKSLGNVVDPVNLVEH 319
Cdd:pfam01406 200 ARKYLGDQI---------DIHGGGIDLAFPHHENEIAQSEAAFDKQLANYWLHnGHVMIDGEKMSKSLGNFFTIRDVLKR 270
|
330 340
....*....|....*....|....*...
gi 1129126296 320 FGLDQIRYFFLrEVSFGQDGSYSEEGIA 347
Cdd:pfam01406 271 YDPEILRYFLL-SVHYRSPLDFSEELLE 297
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
223-323 |
6.48e-06 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 49.13 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 223 DPDhVMYVWVDALTNYVTATGYLTDETGPRAkFWPADLHMIGKDIIRFhtvyWPAFLMSAGLPL----P-KRVFAHGFLL 297
Cdd:PLN02381 576 DPD-VLDTWFSSGLFPLSVLGWPDDTDDLKA-FYPTSVLETGHDILFF----WVARMVMMGMQLggdvPfRKVYLHPMIR 649
|
90 100
....*....|....*....|....*..
gi 1129126296 298 NK-GEKMSKSLGNVVDPVNLVEHFGLD 323
Cdd:PLN02381 650 DAhGRKMSKSLGNVIDPLEVINGISLE 676
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
3-47 |
1.44e-05 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 47.74 E-value: 1.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1129126296 3 TKTPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFF 47
Cdd:COG0495 31 SKPKYYVLDMFPYPSGRLHMGHVRNYTIGDVVARYKRMQGYNVLH 75
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
20-88 |
3.53e-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: 44.88 E-value: 3.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129126296 20 PHIGHAYELIATDAIARFQRLDGRDVFF---LTGTDEhgqKMQQTAKRENMTAKELADRNSAEFRKMGQLLN 88
Cdd:cd00672 34 AHIGHARTYVVFDVLRRYLEDLGYKVRYvqnITDIDD---KIIKRAREEGLSWKEVADYYTKEFFEDMKALN 102
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
2-122 |
9.60e-05 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 45.28 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 2 TTKTPYYITTAISYPNGRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHGQKMQQTAKRENMTAKELA--DRNSAE 79
Cdd:PLN02381 125 SSKPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKLMRERHLTrhDIGREE 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129126296 80 F-------------------RKMGQLLNASNDDFirTTEPRHHEAVTAIWKRMAANGDIYKD 122
Cdd:PLN02381 205 FvsevwkwkdeyggtilnqlRRLGASLDWSRECF--TMDEQRSKAVTEAFVRLYKEGLIYRD 264
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
255-327 |
1.32e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 44.68 E-value: 1.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129126296 255 FW-PADLHMIGKDIIRFH---TVYWPAFLMsAGLPLPKRVFAHGFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRY 327
Cdd:PLN02959 668 YWyPFDLRVSGKDLIQNHltfAIYNHTAIW-AEEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRF 743
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
255-348 |
1.42e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 44.47 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 255 FW-PADLHMIGKDIIRFHTVYwpaFLM--SAGLP---LPKRVFAHGFLLNKGEKMSKSLGNVVdPVN-LVEHFGLDQIRY 327
Cdd:PRK12300 527 YWyPVDWRHSGKDLIPNHLTF---FIFnhVAIFPeekWPRGIVVNGFVLLEGKKMSKSKGNVI-PLRkAIEEYGADVVRL 602
|
90 100
....*....|....*....|.
gi 1129126296 328 FFLREVSFGQDGSYSEEGIAT 348
Cdd:PRK12300 603 YLTSSAELLQDADWREKEVES 623
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
355-466 |
1.87e-04 |
|
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This domain is found in a variety of class Ia aminoacyl tRNA synthetases, C-terminal to the catalytic core domain. It recognizes and specifically binds to the anticodon of the tRNA. Aminoacyl tRNA synthetases catalyze the transfer of cognate amino acids to the 3'-end of their tRNAs by specifically recognizing cognate from non-cognate amino acids. Members include valyl-, leucyl-, isoleucyl-, cysteinyl-, arginyl-, and methionyl-tRNA synthethases. This superfamily also includes a domain from MshC, an enzyme in the mycothiol biosynthetic pathway.
Pssm-ID: 153408 [Multi-domain] Cd Length: 117 Bit Score: 40.95 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 355 ANGIGNLASRSLSMIVKNCEGAVPV--CGDLSEADAAILATADALVETVRAEMNALAIHKALAAIIALVSEGDRYFAGQE 432
Cdd:cd07375 7 ARAFLNRLYRLLSFFRKALGGTQPKwdNELLEEADRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELNWYLDELK 86
|
90 100 110
....*....|....*....|....*....|....
gi 1129126296 433 PWALKKTDPARMATVLYVTAEVVRQialLLQPFM 466
Cdd:cd07375 87 PALQTEELREAVLAVLRAALVVLTK---LLAPFT 117
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
16-124 |
2.31e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 44.16 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 16 PN--GRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHG-------QKM--QQTAKRENMTAKELADRN-------- 76
Cdd:PLN02943 97 PNvtGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGiatqlvvEKMlaSEGIKRTDLGRDEFTKRVwewkekyg 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1129126296 77 ---SAEFRKMGQLLNASNDDFirTTEPRHHEAVTAIWKRMAANGDIYKDSY 124
Cdd:PLN02943 177 gtiTNQIKRLGASCDWSRERF--TLDEQLSRAVVEAFVRLHEKGLIYQGSY 225
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
254-346 |
6.05e-04 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 42.65 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 254 KFWPADLHMIGKDIIR--FHTVYWPAFLMSAGLPLpKRVFAHGFLL-NKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFL 330
Cdd:PTZ00427 670 KIFPADFIAEGLDQTRgwFYTLLVISTLLFDKAPF-KNLICNGLVLaSDGKKMSKRLKNYPDPLYILDKYGADSLRLYLI 748
|
90
....*....|....*..
gi 1129126296 331 REVSF-GQDGSYSEEGI 346
Cdd:PTZ00427 749 NSVAVrAENLKFQEKGV 765
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
291-433 |
2.61e-03 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 40.40 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 291 FAH-GFLLNKGEKMSKSLGNVVDPVNLVEHFGLDQIRYFFLReVSFGQDGSYSEEGIATRINAD--LANGIGNLASRSLS 367
Cdd:PTZ00399 303 FLHsGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLL-HKWDKPMNYSDESMDEAIEKDkvFFNFFANVKIKLRE 381
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1129126296 368 MIVKNCEGavpvcgdLSEADAAILATADALVETV-RAEMNALAIHKALAAIIALVSEGDRYFAGQEP 433
Cdd:PTZ00399 382 SELTSPQK-------WTQHDFELNELFEETKSAVhAALLDNFDTPEALQALQKLISATNTYLNSGEQ 441
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
20-51 |
3.26e-03 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 40.24 E-value: 3.26e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1129126296 20 PHIGHAYELIATDAIARFQRLDGRDVFF-----LTGT 51
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFpmafhVTGT 37
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
16-122 |
3.68e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 39.99 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 16 PN--GRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTDEHG-------QK--MQQTAK------RENMTAK--ELADRN 76
Cdd:PTZ00419 69 PNvtGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGiatqvvvEKklMKEENKtrhdlgREEFLKKvwEWKDKH 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1129126296 77 SA----EFRKMGQLLNASNDDFirTTEPRHHEAVTAIWKRMAANGDIYKD 122
Cdd:PTZ00419 149 GNnicnQLRRLGSSLDWSREVF--TMDEQRSKAVKEAFVRLYEDGLIYRD 196
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
16-52 |
6.52e-03 |
|
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: 39.26 E-value: 6.52e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1129126296 16 PN--GRPHIGHAYELIATDAIARFQRLDGRDVFFLTGTD 52
Cdd:COG0525 44 PNvtGSLHMGHALNNTLQDILIRYKRMQGYNTLWQPGTD 82
|
|
| Anticodon_Ia_Ile_ABEc |
cd07961 |
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA ... |
390-467 |
7.32e-03 |
|
Anticodon-binding domain of archaeal, bacterial, and eukaryotic cytoplasmic isoleucyl tRNA synthetases; This domain is found in isoleucyl tRNA synthetases (IleRS), 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. This family includes bacterial, archaeal, and eukaryotic cytoplasmic members. IleRS catalyzes the transfer of isoleucine to the 3'-end of its tRNA.
Pssm-ID: 153415 [Multi-domain] Cd Length: 183 Bit Score: 37.53 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129126296 390 ILATADALVETVRAEMNALAIHKALAAIIALVSE---------GDRYfagqepWALKKTDPARMA-TVLYvtaEVVRQIA 459
Cdd:cd07961 52 ILSRLNSLIKEVTEEMEAYDLYTAVRALLEFIDEltnwyirrnRKRF------WGEEGDDDKLAAyATLY---EVLLTLS 122
|
....*...
gi 1129126296 460 LLLQPFMP 467
Cdd:cd07961 123 RLMAPFTP 130
|
|
| |
