|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
1-657 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 1238.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 1 MAKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIK 80
Cdd:PRK12267 1 MMKKTFYITTPIYYPNGKPHIGHAYTTIAADALARYKRLQGYDVFFLTGTDEHGQKIQQAAEKAGKTPQEYVDEISAGFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 81 QLWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDpqyengkiiGGKSPDSGH 160
Cdd:PRK12267 81 ELWKKLDISYDKFIRTTDERHKKVVQKIFEKLYEQGDIYKGEYEGWYCVSCETFFTESQLVD---------GGKCPDCGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 161 EVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDA 240
Cdd:PRK12267 152 EVELVKEESYFFRMSKYQDRLLEYYEENPDFIQPESRKNEMINNFIKPGLEDLSISRTSFDWGIPVPFDPKHVVYVWIDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 241 LVNYISALGYLSDDESLFNRYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPN 320
Cdd:PRK12267 232 LLNYITALGYGSDDDELFKKFWPADVHLVGKDILRFHAIYWPIMLMALGLPLPKKVFAHGWWLMKDGKMSKSKGNVVDPE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 321 ILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDGELPAyQGPLHELDEEMEAM 400
Cdd:PRK12267 312 ELVDRYGLDALRYYLLREVPFGSDGDFSPEALVERINSDLANDLGNLLNRTVAMINKYFDGEIPA-PGNVTEFDEELIAL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 401 ALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKDMLGNVMAHLVENIRYAAVLLRPFLTHAPK 480
Cdd:PRK12267 391 AEETLKNYEELMEELQFSRALEEVWKLISRANKYIDETAPWVLAKDEGKKERLATVMYHLAESLRKVAVLLSPFMPETSK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 481 EIFEQLNInNPQFMEFSSLEQYGVLTESIMVtGQPKPIFPRLDSEAEIAYIKESMQPPAT--EEEKEEIPSKPQIDIKDF 558
Cdd:PRK12267 471 KIFEQLGL-EEELTSWESLLEWGGLPAGTKV-AKGEPLFPRIDVEEEIAYIKEQMEGSAPkePEEKEKKPEKPEITIDDF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 559 DKVEIKAATIIDAEHVKKSDKLLKIQVDLDSEQ-RQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSAEK 637
Cdd:PRK12267 549 DKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEpRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAED 628
|
650 660
....*....|....*....|
gi 579670249 638 DGVLTLVSLPSAIPNGAVIK 657
Cdd:PRK12267 629 DGKLTLLTVDKEVPNGSKVK 648
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
4-531 |
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: 755.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 4 ETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLW 83
Cdd:COG0143 1 KKFLVTTAIPYANGPPHIGHLYTYIPADILARYQRLRGHDVLFVTGTDEHGTKIELAAEKEGITPQELVDRIHAEFKELF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 84 AKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESqLVD--------------------P 143
Cdd:COG0143 81 EKLGISFDNFIRTTSPEHKELVQEIFQRLYDNGDIYKGEYEGWYCPECERFLPDR-YVEgtcpkcgaedaygdqcencgA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 144 QYENGKIIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDfIQpPSRKNEMInNFIKPGLADLAVSRTsFNWG 223
Cdd:COG0143 160 TLEPTELINPRSAISGAPPELREEEHYFFRLSKYQDRLLEWIEENPD-IQ-PEVRNEVL-SWLKEGLQDLSISRD-FDWG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 224 VHVPSNPKHVVYVWIDALVNYISAL-GYLSD--DESLFNRYWPAD----IHLMAKEIVRFHSIIWPILLMALDLPLPKKV 296
Cdd:COG0143 236 IPVPGDPGKVFYVWFDALIGYISATkGYADDrgLPEDFEKYWPAPdtelVHFIGKDIIRFHAIIWPAMLMAAGLPLPKKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 297 FAHGWILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVN 376
Cdd:COG0143 316 FAHGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQDGDFSWEDFVARVNSDLANDLGNLASRTLSMIH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 377 KYFDGELPAYqGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDsQKDMLGNV 456
Cdd:COG0143 396 KYFDGKVPEP-GELTEADEELLAEAEAALEEVAEAMEAFEFRKALEEIMALARAANKYIDETAPWKLAKDE-DPERLATV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579670249 457 MAHLVENIRYAAVLLRPFLTHAPKEIFEQLNInNPQFMEFSSLEQygVLTESIMVtGQPKPIFPRLDSEAEIAYI 531
Cdd:COG0143 474 LYTLLEALRILAILLKPFLPETAEKILEQLGL-EGDELTWEDAGW--PLPAGHKI-GKPEPLFPRIEDEQIEALL 544
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
4-523 |
0e+00 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 746.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 4 ETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLW 83
Cdd:PRK11893 1 KKFYITTPIYYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFLTGTDEHGQKIQRKAEEAGISPQELADRNSAAFKRLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 84 AKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYengkiiggKSPDSGHEVE 163
Cdd:PRK11893 81 EALNISYDDFIRTTDPRHKEAVQEIFQRLLANGDIYLGKYEGWYCVRCEEFYTESELIEDGY--------RCPPTGAPVE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 164 LVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMInNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDALVN 243
Cdd:PRK11893 153 WVEEESYFFRLSKYQDKLLELYEANPDFIQPASRRNEVI-SFVKSGLKDLSISRTNFDWGIPVPGDPKHVIYVWFDALTN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 244 YISALGYLSDDESL---FNRYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPN 320
Cdd:PRK11893 232 YLTALGYPDDEELLaelFNKYWPADVHLIGKDILRFHAVYWPAFLMAAGLPLPKRVFAHGFLTLDGEKMSKSLGNVIDPF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 321 ILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDGELPAyQGPLHELDEEMEAM 400
Cdd:PRK11893 312 DLVDEYGVDAVRYFLLREIPFGQDGDFSREAFINRINADLANDLGNLAQRTLSMIAKNFDGKVPE-PGALTEADEALLEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 401 ALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKdmLGNVMAHLVENIRYAAVLLRPFLTHAPK 480
Cdd:PRK11893 391 AAALLERVRAAMDNLAFDKALEAILALVRAANKYIDEQAPWSLAKTDPER--LATVLYTLLEVLRGIAVLLQPVMPELAA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 579670249 481 EIFEQLNINNPQFMEFSSLeQYGVLTESIMVTgQPKPIFPRLD 523
Cdd:PRK11893 469 KILDQLGVEEDENRDFAAL-SWGRLAPGTTLP-KPEPIFPRLE 509
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
6-523 |
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: 593.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 6 FYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWAK 85
Cdd:TIGR00398 1 ILITTALPYANGKPHLGHAYTTILADVYARYKRLRGYEVLFVCGTDEHGTKIELKAEQEGLTPKELVDKYHEEFKDDWKW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 86 LEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDPQYENGK---------------- 149
Cdd:TIGR00398 81 LNISFDRFIRTTDEEHKEIVQKIFQKLKENGYIYEKEIKQLYCPECEMFLPDRYVEGTCPKCGSedargdhcevcgrhle 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 150 ---IIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMINNFIKPGLADLAVSRTSFNWGVHV 226
Cdd:TIGR00398 161 pteLINPRCKICGAKPELRDSEHYFFRLSAFEKELEEWIRKNPESGSPASNVKNKAQNWLKGGLKDLAITRDLVYWGIPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 227 PSNPKHVVYVWIDALVNYISALGYLSDDESLFNRYWPAD-----IHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGW 301
Cdd:TIGR00398 241 PNDPNKVVYVWFDALIGYISSLGILSGDTEDWKKWWNNDedaelIHFIGKDIVRFHTIYWPAMLMGLGLPLPTQVFSHGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 302 ILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNKYFDG 381
Cdd:TIGR00398 321 LTVEGGKMSKSLGNVVDPSDLLARFGADILRYYLLKERPLGKDGDFSWEDFVERVNADLANKLGNLLNRTLGFIKKYFNG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 382 ELPaYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKDDSQKDmlgNVMAHLV 461
Cdd:TIGR00398 401 VLP-SEDITDEEDKKLLKLINEALEQIDEAIESFEFRKALREIMKLADRGNKYIDENKPWELFKQSPRLK---ELLAVCS 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 579670249 462 ENIRYAAVLLRPFLTHAPKEIFEQLNInnpqfmefsSLEQYGVLT-ESIMVTGQPKPIFPRLD 523
Cdd:TIGR00398 477 MLIRVLSILLYPIMPKLSEKILKFLNF---------ELEWDFKLKlLEGHKLNKAEPLFSKIE 530
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
5-347 |
9.11e-171 |
|
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: 489.74 E-value: 9.11e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 5 TFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWA 84
Cdd:cd00814 1 KVLITTALPYVNGVPHLGHLYGTVLADVFARYQRLRGYDVLFVTGTDEHGTKIEQKAEEEGVTPQELCDKYHEIFKDLFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 85 KLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTesqlvdpqyengkiiggkspdsghevEL 164
Cdd:cd00814 81 WLNISFDYFIRTTSPRHKEIVQEFFKKLYENGYIYEGEYEGLYCVSCERFLP--------------------------EW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 165 VKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEMInNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDALVNY 244
Cdd:cd00814 135 REEEHYFFRLSKFQDRLLEWLEKNPDFIWPENARNEVL-SWLKEGLKDLSITRDLFDWGIPVPLDPGKVIYVWFDALIGY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 245 ISALGYLSD---DESLFNRYWPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPNI 321
Cdd:cd00814 214 ISATGYYNEewgNSWWWKDGWPELVHFIGKDIIRFHAIYWPAMLLGAGLPLPTRIVAHGYLTVEGKKMSKSRGNVVDPDD 293
|
330 340
....*....|....*....|....*.
gi 579670249 322 LIDRYGLDATRYYLMRELPFGSDGVF 347
Cdd:cd00814 294 LLERYGADALRYYLLRERPEGKDSDF 319
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
6-371 |
2.32e-161 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 468.31 E-value: 2.32e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 6 FYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWAK 85
Cdd:pfam09334 1 ILVTTALPYANGPPHLGHLYSYIPADIFARYLRLRGYDVLFVCGTDEHGTPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 86 LEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDP------------QYEN------ 147
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEFFLKLYENGYIYEKEIEQFYCPSDERFLPDRYVEGTcphcgsedargdQCENcgrhle 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 148 -GKIIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQ-NPDfiqPPSRKNEMINNFIKPGLADLAVSRTsFNWGVH 225
Cdd:pfam09334 161 pTELINPKCVICGTTPEVKETEHYFFDLSKFQDKLREWIEEnNPE---WPENVKNMVLEWLKEGLKDRAISRD-LDWGIP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 226 VPSNPKHVVYVWIDALVNYISALGYLSDDESLFNRYWPAD-----IHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHG 300
Cdd:pfam09334 237 VPGAEGKVFYVWLDAPIGYISATKELSGNEEKWKEWWPNDpdtelVHFIGKDIIYFHTIFWPAMLLGAGYRLPTTVFAHG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579670249 301 WILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRT 371
Cdd:pfam09334 317 YLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKDTDFSWEDFVERVNSELADDLGNLVNRV 387
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
8-657 |
5.77e-150 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 449.60 E-value: 5.77e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 8 ITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWAKLE 87
Cdd:PRK00133 6 VTCALPYANGPIHLGHLVEYIQADIWVRYQRMRGHEVLFVCADDAHGTPIMLKAEKEGITPEELIARYHAEHKRDFAGFG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 88 ISNDDFIRTTEERHKHVVEQVFERLLKQGDIYlgeyegwysvpdETyyTESQLVDPQ----------------------- 144
Cdd:PRK00133 86 ISFDNYGSTHSEENRELAQEIYLKLKENGYIY------------EK--TIEQLYDPEkgmflpdrfvkgtcpkcgaedqy 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 145 ----------YENGKIIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFiqPPSRKNeMINNFIKPGLADLA 214
Cdd:PRK00133 152 gdncevcgatYSPTELINPKSAISGATPVLKESEHFFFKLPRFEEFLKEWITRSGEL--QPNVAN-KMKEWLEEGLQDWD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 215 VSRTSFNWGVHVPSNPKHVVYVWIDALVNYISALGYLSD--DESLFNRYWPAD-----IHLMAKEIVRFHSIIWPILLMA 287
Cdd:PRK00133 229 ISRDAPYFGFEIPGAPGKVFYVWLDAPIGYISSTKNLCDkrGGLDWDEYWKKDsdtelYHFIGKDIIYFHTLFWPAMLEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 288 LDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGV-FTPEAFVERTNFDLANDLGN 366
Cdd:PRK00133 309 AGYRLPTNVFAHGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLAAKLPETIDDLdFNWEDFQQRVNSELVGKVVN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 367 LVNRTISMVNKYFDGELPAyqgplHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAKD 446
Cdd:PRK00133 389 FASRTAGFINKRFDGKLPD-----ALADPELLEEFEAAAEKIAEAYEAREFRKALREIMALADFANKYVDDNEPWKLAKQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 447 DSQKdmLGNVMAHLVENIRYAAVLLRPFLTHAPKEIFEQLNINNPQFMEFSSLEQYGVLTEsimvtgqPKPIFPRLDS-- 524
Cdd:PRK00133 464 DGER--LQAVCSVGLNLFRALAIYLKPVLPELAERAEAFLNLEELTWDDAQQPLAGHPINK-------FKILFTRIEDkq 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 525 -EAEIAYIKESMQ----PPATEEEKEEIPSKPQIDIKDFDKVEIKAATIIDAEHVKKSDKLLKIQVDLDSEQRQIVSGIA 599
Cdd:PRK00133 535 iEALIEASKEAAAakaaAAAAAAPLAEEPIAETISFDDFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEETRQVFSGIK 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 579670249 600 KFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSAE-KDGVLTLVSLPSAIPNGAVIK 657
Cdd:PRK00133 615 SAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGpGGGDLFLLEPDEGAKPGMRVK 673
|
|
| PLN02224 |
PLN02224 |
methionine-tRNA ligase |
4-556 |
1.27e-113 |
|
methionine-tRNA ligase
Pssm-ID: 177869 [Multi-domain] Cd Length: 616 Bit Score: 354.02 E-value: 1.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 4 ETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLW 83
Cdd:PLN02224 69 DTFVLTTPLYYVNAPPHMGSAYTTIAADSIARFQRLLGKKVIFITGTDEHGEKIATSAAANGRNPPEHCDIISQSYRTLW 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 84 AKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVdpqyENGKIIGGKSPDSGHeve 163
Cdd:PLN02224 149 KDLDIAYDKFIRTTDPKHEAIVKEFYARVFANGDIYRADYEGLYCVNCEEYKDEKELL----ENNCCPVHQMPCVAR--- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 164 lvKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNEmINNFIKPGLADLAVSRTSFNWGVHVPSNPKHVVYVWIDALVN 243
Cdd:PLN02224 222 --KEDNYFFALSKYQKPLEDILAQNPRFVQPSYRLNE-VQSWIKSGLRDFSISRALVDWGIPVPDDDKQTIYVWFDALLG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 244 YISALGYLSDDESLFNRY---WPADIHLMAKEIVRFHSIIWPILLMALDLPLPKKVFAHGWiLMKDG-KMSKSKGNVVDP 319
Cdd:PLN02224 299 YISALTEDNKQQNLETAVsfgWPASLHLIGKDILRFHAVYWPAMLMSAGLELPKMVFGHGF-LTKDGmKMGKSLGNTLEP 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 320 NILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFDLANDLGNLVNRTISMVNK------YFDGELPAYQGPLHEL 393
Cdd:PLN02224 378 FELVQKFGPDAVRYFFLREVEFGNDGDYSEDRFIKIVNAHLANTIGNLLNRTLGLLKKncestlVEDSTVAAEGVPLKDT 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 394 DEEMeamaletVKSYTESMESLQFSVALSTVWKFISRTNKYIDETTPWVLAK------DDSQKDMLgnvmaHLVENIRYA 467
Cdd:PLN02224 458 VEKL-------VEKAQTNYENLSLSSACEAVLEIGNAGNTYMDQRAPWFLFKqggvsaEEAAKDLV-----IILEVMRVI 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 468 AVLLRPFLTHAPKEIFEQLNINNPQFMEFS-SLEQYGVLTESiMVTGQPKPIFPRLDseaeiayikesMQPpateeEKEE 546
Cdd:PLN02224 526 AVALSPIAPCLSLRIYSQLGYSEDQFNSITwSDTKWGGLKGG-QVMEQASPVFARIE-----------LNP-----EKEE 588
|
570
....*....|
gi 579670249 547 IPSKPQIDIK 556
Cdd:PLN02224 589 DEKKPKVGKK 598
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
5-344 |
1.13e-76 |
|
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: 247.72 E-value: 1.13e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 5 TFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAG----KTE---------IEY 71
Cdd:cd00668 1 KFYVTTPPPYANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPGWDTHGLPIELKAERKGgrkkKTIwieefredpKEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 72 LDEMIAGIKQLWAKLEISND--DFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGwysvpdetyytesqlvdpqyengk 149
Cdd:cd00668 81 VEEMSGEHKEDFRRLGISYDwsDEYITTEPEYSKAVELIFSRLYEKGLIYRGTHPV------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 150 iiggkspdsghevelVKEESYFFNISKYTDRLLEFYDQNPdfIQPPSRKNEMINNFIKPGlaDLAVSRTSFnWGVHVPSn 229
Cdd:cd00668 137 ---------------RITEQWFFDMPKFKEKLLKALRRGK--IVPEHVKNRMEAWLESLL--DWAISRQRY-WGTPLPE- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 230 pkHVVYVWIDALVNYISALGYLSDDESlFNRYWPADIHLMAKEIVRFHSIIWPILLMALDLPLP-KKVFAHGWILMKDG- 307
Cdd:cd00668 196 --DVFDVWFDSGIGPLGSLGYPEEKEW-FKDSYPADWHLIGKDILRGWANFWITMLVALFGEIPpKNLLVHGFVLDEGGq 272
|
330 340 350
....*....|....*....|....*....|....*..
gi 579670249 308 KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSD 344
Cdd:cd00668 273 KMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGDD 309
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
3-656 |
1.68e-64 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 227.74 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 3 KETFYITTPIYYPSGNLHIGHAYSTV-AGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQ 81
Cdd:PLN02610 16 KRNILITSALPYVNNVPHLGNIIGCVlSADVFARYCRLRGYNAIYICGTDEYGTATETKALEENCTPKEICDKYHAIHKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 82 LWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYS---------------VPDETYYTESQLVDpQYE 146
Cdd:PLN02610 96 VYDWFDISFDKFGRTSTPQQTEICQAIFKKLMENNWLSENTMQQLYCdtcqkfladrlvegtCPTEGCNYDSARGD-QCE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 147 N-------GKIIGGKSPDSGHEVELVKEESYFFNISKYTDRLLEF---------YDQNPdfIQppsrkneMINNFIKPGL 210
Cdd:PLN02610 175 KcgkllnpTELIDPKCKVCKNTPRIRDTDHLFLELPLLKDKLVEYinetsvaggWSQNA--IQ-------TTNAWLRDGL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 211 ADLAVSRtSFNWGVHVPsNPKH---VVYVWIDALVNYIS-ALGYLSDDEslfnRYW--PADIHL---MAKEIVRFHSIIW 281
Cdd:PLN02610 246 KPRCITR-DLKWGVPVP-LEKYkdkVFYVWFDAPIGYVSiTACYTPEWE----KWWknPENVELyqfMGKDNVPFHTVMF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 282 PILLMALDLPlpkkvfahgWILMK-----------DGKMSKSKG------NVVDPNILIDRYgldatRYYLMRELPFGSD 344
Cdd:PLN02610 320 PSTLLGTGEN---------WTMMKtisvteylnyeGGKFSKSKGvgvfgnDAKDTNIPVEVW-----RYYLLTNRPEVSD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 345 GVFTPEAFVERTNFDLANDLGNLVNRTISMV----NKYFDGELPAYQGP-LHELDEEMEAMALETVKSYTESMESLQFSV 419
Cdd:PLN02610 386 TLFTWADLQAKLNSELLNNLGNFINRVLSFIakppGAGYGSVIPDAPGAeSHPLTKKLAEKVGKLVEQYVEAMEKVKLKQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 420 ALSTVWKFISRTNKYIDETTPWVLAKDDsqKDMLGNVMAHLVENIRYAAVLLRPFLTHAPKEIFEQLNInNPQfmEFSSL 499
Cdd:PLN02610 466 GLKTAMSISSEGNAYLQESQFWKLYKED--KPSCAIVVKTSVGLVYLLACLLEPFMPSFSKEVLKQLNL-PPE--SLSLS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 500 EQYG---------VLTESIMVTGQPKPIFPRLDSE-----------------------------------AEIAYIKESM 535
Cdd:PLN02610 541 DEKGevarakrpwELVPAGHKIGTPEPLFKELKDEeveayrekfagsqadraaraeaaeakklakqlkkkALSDGGKKKQ 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 536 QPPATEEEKEEIPSKPQIDIKdfdKVEIKAATIIDAEHVKKSDKLLKIQVDLDSEQ-RQIVSGIAKFYTPDDIIGKKVAV 614
Cdd:PLN02610 621 GKKAGGGGKSKAAAEREIDVS---RLDIRVGLIVKAEKHPDADSLYVEEIDVGEGApRTVVSGLVKYIPLEEMQNRKVCV 697
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 579670249 615 VTNLKPAKLMGQKSEGMILSA-EKDGvlTLVSL--PsaiPNGAVI 656
Cdd:PLN02610 698 LCNLKPAAMRGIKSQAMVLAAsNSDH--TKVELveP---PESAAV 737
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
553-657 |
5.36e-50 |
|
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.
Pssm-ID: 239199 [Multi-domain] Cd Length: 105 Bit Score: 169.22 E-value: 5.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 553 IDIKDFDKVEIKAATIIDAEHVKKSDKLLKIQVDLDSEQRQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMI 632
Cdd:cd02800 1 ITIDDFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEEERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMI 80
|
90 100
....*....|....*....|....*
gi 579670249 633 LSAEKDGVLTLVSLPSAIPNGAVIK 657
Cdd:cd02800 81 LAAEDGGKLKLLTPDEEVEPGSRVS 105
|
|
| Anticodon_Ia_Met |
cd07957 |
Anticodon-binding domain of methionyl tRNA synthetases; This domain is found in methionyl tRNA ... |
357-486 |
1.49e-47 |
|
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: 163.43 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 357 NFDLANDLGNLVNRTISMVNKYFDGELPAYqGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYID 436
Cdd:cd07957 2 NSELANNLGNLVNRTLNMASKYFGGVVPEF-GGLTEEDEELLEEAEELLEEVAEAMEELEFRKALEEIMELARAANKYID 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 579670249 437 ETTPWVLAKDDsQKDMLGNVMAHLVENIRYAAVLLRPFLTHAPKEIFEQL 486
Cdd:cd07957 81 ETAPWKLAKEE-DPERLATVLYVLLELLRILAILLSPFMPETAEKILDQL 129
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
525-657 |
1.00e-41 |
|
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273059 [Multi-domain] Cd Length: 137 Bit Score: 147.96 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 525 EAEIAYIKESMQPPatEEEKEEIPSKPQIDIKDFDKVEIKAATIIDAEHVKKSDKLLKIQVDLDSEQRQIVSGIAKFYTP 604
Cdd:TIGR00399 6 ELKLKGAKKKEKKD--EGEKALEPQKETITIDDFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEKRQIVSGIAGYYTP 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 579670249 605 DDIIGKKVAVVTNLKPAKLMGQKSEGMILSAEKDG-VLTLVSLPSAIPNGAVIK 657
Cdd:TIGR00399 84 EELVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGkVLFLLSPDQEAIAGERIK 137
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
4-344 |
2.51e-40 |
|
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: 151.63 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 4 ETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG----QKIQEKAQKAGKTE----------- 68
Cdd:cd00817 1 PVFVIDTPPPNVTGSLHMGHALNNTIQDIIARYKRMKGYNVLWPPGTDHAGiatqVVVEKKLGIEGKTRhdlgreeflek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 69 -IEYLDEMIAGIKQLWAKLEISND--DFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETyyTESQL-Vdpq 144
Cdd:cd00817 81 cWEWKEESGGKIREQLKRLGASVDwsREYFTMDPGLSRAVQEAFVRLYEKGLIYRDNRLVNWCPKLRT--AISDIeV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 145 yengkiiggkSPDSGHEVELVKEESYFFNISKYTDRLLEFYDQ-NPDFIqpPSRKNEMINNFIKpGLADLAVSRTSFnWG 223
Cdd:cd00817 156 ----------CSRSGDVIEPLLKPQWFVKVKDLAKKALEAVKEgDIKFV--PERMEKRYENWLE-NIRDWCISRQLW-WG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 224 VHVP----SNPKHVVYV--------------------------------WIDALVNYISALGYLSDDESlFNRYWPADIH 267
Cdd:cd00817 222 HRIPawycKDGGHWVVAreedeaidkaapeacvpcggeelkqdedvldtWFSSSLWPFSTLGWPEETKD-LKKFYPTSLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 268 LMAKEIVRFhsiiWP--ILLMALDL--PLP-KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPF 341
Cdd:cd00817 301 VTGHDIIFF----WVarMIMRGLKLtgKLPfKEVYLHGLVRDEDGrKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQ 376
|
...
gi 579670249 342 GSD 344
Cdd:cd00817 377 GRD 379
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
6-347 |
2.88e-34 |
|
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: 132.76 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 6 FYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWAK 85
Cdd:cd00812 2 FYILVMFPYPSGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 86 LEISND--DFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSvpdetyytesqlvdpqyengkiiggkspdsgheve 163
Cdd:cd00812 82 MGFSYDwrREFTTCDPEYYKFTQWLFLKLYEKGLAYKKEAPVNWC----------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 164 lVKEESYFFNIS--KYTDRLLEFYDQNPDFiqPPSRKNeMINNFIkpgladlAVSRTSFnWGVHVPsnpkhvvyvW---I 238
Cdd:cd00812 127 -KLLDQWFLKYSetEWKEKLLKDLEKLDGW--PEEVRA-MQENWI-------GCSRQRY-WGTPIP---------WtdtM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 239 DALVN-------YISA-------LGYLSDDESLFNRYWPADIHLMAKEIVRFH---SIIWPILLMALDLPL---PKKVFA 298
Cdd:cd00812 186 ESLSDstwyyarYTDAhnleqpyEGDLEFDREEFEYWYPVDIYIGGKEHAPNHllySRFNHKALFDEGLVTdepPKGLIV 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 579670249 299 HGWILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVF 347
Cdd:cd00812 266 QGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFAAPPDADFDW 314
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
2-615 |
2.26e-33 |
|
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: 136.73 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 2 AKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG----QKIQEKAQKAGKTE--------- 68
Cdd:TIGR00422 31 NKPPFCIDIPPPNVTGSLHIGHALNWSIQDIIARYKRMKGYNVLWLPGTDHAGiatqVKVEKKLGAEGKTKhdlgreefr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 69 ---IEYLDEMIAGIKQLWAKLEISND---DFIRTTEERHKhVVEQVFERLLKQGDIYLGEY------------------- 123
Cdd:TIGR00422 111 ekiWEWKEESGGTIKNQIKRLGASLDwsrERFTMDEGLSK-AVKEAFVRLYEKGLIYRGEYlvnwdpklntaisdievey 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 124 ---EG--WYSV------------------------------PDETYYTE-------------------SQLVDPQY---- 145
Cdd:TIGR00422 190 kevKGklYYIRyplangskdylvvattrpetmfgdtavavhPEDERYKHligkkvilpltgrkipiiaDEYVDMEFgtga 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 146 ---------------------------ENG-------------------KIIG------------------GKSPDSGHE 161
Cdd:TIGR00422 270 vkvtpahdfndyewgkrhnlefinildEDGllnenagkyqgltrfearkKIVEdlkeegllvkiephthnvGTCWRSGTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 162 VELVKEESYFFNISKYTDRLLE-FYDQNPDFIqpPSRKNEMINNFIKpGLADLAVSRTSFnWG-------------VHVP 227
Cdd:TIGR00422 350 VEPLLSKQWFVKVEKLADKALEaAEEGEIKFV--PKRMEKRYLNWLR-NIKDWCISRQLI-WGhripvwyckecgeVYVA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 228 SNP------------------KHVVYVWIDALVNYISALGYLSDDESlFNRYWPADIHLMAKEIVRFhsiiWP---ILL- 285
Cdd:TIGR00422 426 KEEplpddktntgpsveleqdTDVLDTWFSSSLWPFSTLGWPDETKD-LKKFYPTDLLVTGYDIIFF----WVarmIFRs 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 286 MALDLPLP-KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFdlAND 363
Cdd:TIGR00422 501 LALTGQVPfKEVYIHGLVRDEQGrKMSKSLGNVIDPLDVIEKYGADALRFTLASLVTPGDDINFDWKRVESARNF--LNK 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 364 LGNlVNRTISMvNKYFDGELPAYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFI--SRTNKYIDETTPW 441
Cdd:TIGR00422 579 LWN-ASRFVLM-NLSDDLELSGGEEKLSLADRWILSKLNRTIKEVRKALDKYRFAEAAKALYEFIwnDFCDWYIELVKYR 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 442 VLAKDDSQKDMLGNVMAHLVENiryAAVLLRPFLTHAPKEIFEQLNInnpqfmefssleqygvLTESIMVTGQPKPIFPR 521
Cdd:TIGR00422 657 LYNGNEAEKKAARDTLYYVLDK---ALRLLHPFMPFITEEIWQHFKE----------------GADSIMLQSYPVVDAEF 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 522 LDSEAEIAY------------IKESMQPPA----------TEEEKEEIPSKPQIDIK---DFDKVEIKAAT--------- 567
Cdd:TIGR00422 718 VDEEAEKAFellkeiivsirnLKAESNIPPnaplkvlliyTEAETAERLKLNAVDIKgaiNFSEVEVVIEKpevteavve 797
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 579670249 568 -------IIDAEHVKKSDKLL-KIQVDLDSEQRQIVSGIAKFYTPDDIIGKKVAVV 615
Cdd:TIGR00422 798 lvpgfeiIIPVKGLINKAKELaRLQKQLDKEKKEVIRIEGKLENEGFVKKAPKEVI 853
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
14-344 |
3.92e-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: 130.04 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 14 YPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGkteieyldemiaGIKQLWAKLEISNDDF 93
Cdd:cd00818 11 YANGLPHYGHALNKILKDIINRYKTMQGYYVPRRPGWDCHGLPIELKVEKEL------------GISGKKDIEKMGIAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 94 IRTTEE---RHKHVVEQVFERLLKQGDiylgeyegWysvpDETYYTesqlVDPQYENgKIIG--GKSPDSGHEVELVK-- 166
Cdd:cd00818 79 NAKCREfalRYVDEQEEQFQRLGVWVD--------W----ENPYKT----MDPEYME-SVWWvfKQLHEKGLLYRGYKvv 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 167 --------EESYFFNISKYTDRLLEFYDQN---PDFIQppSRKNEMINNfikpgLADLAVSRTSFnWGVHVP-----SNP 230
Cdd:cd00818 142 pwpliyraTPQWFIRVTKIKDRLLEANDKVnwiPEWVK--NRFGNWLEN-----RRDWCISRQRY-WGTPIPvwyceDCG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 231 KHVVY-------VWIDALVNYISALGYLSDDEsLFNRYWPADIHLMAKEIVR--FHSiiwpiLL----MALDLPLPKKVF 297
Cdd:cd00818 214 EVLVRrvpdvldVWFDSGSMPYAQLHYPFENE-DFEELFPADFILEGSDQTRgwFYS-----LLllstALFGKAPYKNVI 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 579670249 298 AHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSD 344
Cdd:cd00818 288 VHGFVLDEDGrKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVYAED 335
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
563-656 |
7.56e-33 |
|
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.
Pssm-ID: 239066 [Multi-domain] Cd Length: 99 Bit Score: 121.47 E-value: 7.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 563 IKAATIIDAEHVKKSDKLLKIQVDL-DSEQRQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSAE----K 637
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIgEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEelglE 80
|
90
....*....|....*....
gi 579670249 638 DGVLTLVSLPSAIPNGAVI 656
Cdd:cd02153 81 EGSVGILELPEDAPVGDRI 99
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
531-657 |
1.20e-32 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 134.60 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 531 IKESMQPPATEEEKEEIPSKPQIDIKDFDKVE----IKAATIIDAEHVKKSDKLLKIQVDLDSEQRQIVSGIAKFY---- 602
Cdd:COG0073 8 LKEYVDLDLSPEELAEKLTMAGIEVEDFEKVGgldgLRVGKVLEAEPHPNADKLLVLQVDVGEETRQIVCGAPNVYagdk 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579670249 603 TPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSA-------EKDGVLTlvsLPSAIPNGAVIK 657
Cdd:COG0073 88 VPEALVGAQVPGVVNLKPRKIRGVESEGMLCSAeelglgeDHDGILE---LPEDAPPGDDAE 146
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
3-486 |
5.79e-29 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 122.99 E-value: 5.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 3 KETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG----QKIQE----KAQKAGKTE-----I 69
Cdd:PRK13208 37 KPVYSIDTPPPTVSGSLHIGHVFSYTHTDFIARYQRMRGYNVFFPQGWDDNGlpteRKVEKyygiRKDDISREEfielcR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 70 EYLDEMIAGIKQLWAKLEISND--DFIRTTEERHKHVVEQVFERLLKQGDIYLG----------------------EYEG 125
Cdd:PRK13208 117 ELTDEDEKKFRELWRRLGLSVDwsLEYQTISPEYRRISQKSFLDLYKKGLIYRAeapvlwcprcetaiaqaeveyrEREG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 126 WY-----SVPDETYYT--------------------------------------------ESQLVDPQY----------- 145
Cdd:PRK13208 197 KLnyikfPVEDGEEIEiattrpellpacvavvvhpdderykhlvgktaivplfgvevpilADPLVDPDFgtgavmictfg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 146 --------------------ENGKI------IGGKSPDSGHE--VELVKEESY--------------------------- 170
Cdd:PRK13208 277 dktdvtwwrelnlptriiidEDGRMteaagkLAGLTIEEARKkiVEDLKSGGLlgkqepikhnvkfcercdtpleilvtr 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 171 --FFNISKYTDRLLEFYDQnPDFIqPPSRKNEMINnFIKpGLA-DLAVSRTSFnWGVHVP----SNPKHVVY-------- 235
Cdd:PRK13208 357 qwFIKVLDLKEELLERGKE-INWY-PEHMRVRLEN-WIE-GLNwDWCISRQRY-FGTPIPvwycKDCGHPILpdeedlpv 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 236 ----------------------------VWIDALVNYISALGYLSDDEsLFNRYWPADIHLMAKEIVR---FHSIIWPIL 284
Cdd:PRK13208 432 dptkdeppgykcpqcgspgfegetdvmdTWATSSITPLIVTGWERDED-LFEKVFPMDLRPQGHDIIRtwlFYTILRAYL 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 285 LMAlDLPLpKKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPfGSDGVFTPEAFveRTNFDLAND 363
Cdd:PRK13208 511 LTG-KLPW-KNIMISGMVLDPDGkKMSKSKGNVVTPEELLEKYGADAVRYWAASARL-GSDTPFDEKQV--KIGRRLLTK 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 364 LGNlVNRTISMVNKYFDGELPAyqgPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRT--NKYIDettpw 441
Cdd:PRK13208 586 LWN-ASRFVLHFSADPEPDKAE---VLEPLDRWILAKLAKVVEKATEALENYDFAKALEEIESFFWHVfcDDYLE----- 656
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 579670249 442 vLAK-----DDSQKDMLGNVMAhLVENIRYAAVLLRPFLTHAPKEIFEQL 486
Cdd:PRK13208 657 -LVKsraygEDEEEEQKSARYT-LYTVLDTLLRLLAPFLPFITEEVWSWL 704
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
563-654 |
5.22e-28 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 107.71 E-value: 5.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 563 IKAATIIDAEHVKKSDKLLKIQVDLDSEQ-RQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSAE--KDG 639
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEpRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80
|
90
....*....|....*
gi 579670249 640 VLTLVSLPSAIPNGA 654
Cdd:pfam01588 81 SVGLLEPPADVPPGT 95
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
553-654 |
9.25e-24 |
|
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.
Pssm-ID: 239197 [Multi-domain] Cd Length: 107 Bit Score: 96.16 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 553 IDIKDFDKVEIKAATIIDAE-HVKKSDKLLKIQVDL-DSEQRQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEG 630
Cdd:cd02798 1 ISYEDFEKVDLRVGTIVEVEdFPEARKPAYKLKVDFgEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEV 80
|
90 100
....*....|....*....|....*
gi 579670249 631 MILSAE-KDGVLTLVSLPSAIPNGA 654
Cdd:cd02798 81 LVLGADdEGGEVVLLVPDREVPNGA 105
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
557-656 |
8.69e-21 |
|
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.
Pssm-ID: 239198 [Multi-domain] Cd Length: 105 Bit Score: 87.67 E-value: 8.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 557 DFDKVEIKAATIIDAEHVKKSDKLLKIQVDL-DSEQRQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQKSEGMILSA 635
Cdd:cd02799 2 DPSRLDIRVGKILKVRKHPDADSLYVEEIDLgEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCA 81
|
90 100
....*....|....*....|.
gi 579670249 636 EKDGVlTLVSLPsAIPNGAVI 656
Cdd:cd02799 82 SNADH-EKVELL-EPPEGAKP 100
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
550-656 |
1.21e-17 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 79.10 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 550 KPQIDIKDFDKVEIKAATIIDAEHVKKSDKL-LKIQVDLDSEQ--RQIVSGIAKFYTPDDIIGKKVAVVTNLKPAKLMGQ 626
Cdd:PRK10089 1 METITYEDFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGEEIgvKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGF 80
|
90 100 110
....*....|....*....|....*....|.
gi 579670249 627 KSEGMILSAE-KDGVLTLVSLPSAIPNGAVI 656
Cdd:PRK10089 81 MSEVLVLGFEdEDGEVVLLTPDRPVPNGVKL 111
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
294-533 |
1.51e-17 |
|
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: 87.03 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 294 KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFdlANDLGNlVNRTI 372
Cdd:COG0525 507 KDVYIHGLVRDEQGrKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIKFDEERVEGYRNF--ANKLWN-ASRFV 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 373 SMVNKYFDGELPAYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFIsrTNKYID---ETTPWVLAKDD-S 448
Cdd:COG0525 584 LMNLEGFDPGLDPDPEELSLADRWILSRLNKTIAEVTEALEKYRFDEAAQALYDFV--WNEFCDwylELAKPRLYGGDeA 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 449 QKDMLGNVMAHLVENIryaavlLR------PFLThapKEIFEQLNINNPqfmefssleqygvlTESIMVTGQPKPIFPRL 522
Cdd:COG0525 662 AKRETRATLVYVLEQI------LRllhpfmPFIT---EEIWQKLPPRKE--------------GESIMLAPWPEADEELI 718
|
250
....*....|...
gi 579670249 523 DSEAE--IAYIKE 533
Cdd:COG0525 719 DEEAEaeFEWLKE 731
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
8-84 |
3.58e-17 |
|
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: 78.68 E-value: 3.58e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579670249 8 ITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWA 84
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKEDVE 77
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
294-533 |
6.17e-16 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 81.69 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 294 KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPFGSDGVFTPEAFVERTNFdlANDLGNlVNRTI 372
Cdd:PRK05729 505 KDVYIHGLVRDEQGrKMSKSKGNVIDPLDLIDKYGADALRFTLAALASPGRDIRFDEERVEGYRNF--ANKLWN-ASRFV 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 373 SMVNKYFDGELPAYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFIsrTNKYIDettpWV--LAK---DD 447
Cdd:PRK05729 582 LMNLEGADVGELPDPEELSLADRWILSRLNRTVAEVTEALDKYRFDEAARALYEFI--WNEFCD----WYleLAKpvlQE 655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 448 SQKDMLGNVMAHLVENIryaavlLR------PFLThapKEIFEQLNINNPQfmefssleqygvltESIMVTGQPKPIfPR 521
Cdd:PRK05729 656 AAKRATRATLAYVLEQI------LRllhpfmPFIT---EELWQKLAPLGIE--------------ESIMLAPWPEAD-EA 711
|
250
....*....|....
gi 579670249 522 LDSEAE--IAYIKE 533
Cdd:PRK05729 712 IDEAAEaeFEWLKE 725
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
3-530 |
5.38e-15 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 78.88 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 3 KETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---QKIQEKAQKagKTEI---------E 70
Cdd:PRK14900 47 RPPFSIVLPPPNVTGSLHLGHALTATLQDVLIRWKRMSGFNTLWLPGTDHAGiatQMIVEKELK--KTEKksrhdlgreA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 71 YLDEMIAGIKQ-----------LWAKLEISNDDFirTTEERHKHVVEQVFERLLKQGDIY---------------LGEYE 124
Cdd:PRK14900 125 FLERVWAWKEQygsrigeqhkaLGASLDWQRERF--TMDEGLSRAVREVFVRLHEEGLIYrekklinwcpdcrtaLSDLE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 125 G----------W---YSV--------------------------PDETYY--------------------TESQLVDPQ- 144
Cdd:PRK14900 203 VeheeahqgelWsfaYPLadgsgeivvattrpetmlgdtavavhPLDPRYmalhgkkvrhpitgrtfpivADAILVDPKf 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 145 ---------------YENGK--------IIG--------------------------------------------GKSPD 157
Cdd:PRK14900 283 gtgavkvtpahdfndFEVGKrhglemitVIGpdgrmtaeagplagldrfearkevkrllaeqgldrgakphvlplGRCQR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 158 SGHEVELVKEESYFFNISKYTDRLLEFYDQNPDFIQPPSRKNE----MINnfikpgLADLAVSRTSFnWGVHVPS----- 228
Cdd:PRK14900 363 SATILEPLLSDQWYVRIEPLARPAIEAVEQGRTRFIPEQWTNTymawMRN------IHDWCISRQLW-WGHQIPAwycpd 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 229 ----------------------NPKHVVYVWIDALVNYISALGYLSDDESLfNRYWPADIHLMAKEIVRFhsiiW--PIL 284
Cdd:PRK14900 436 ghvtvaretpeacstcgkaelrQDEDVLDTWFSSGLWPFSTMGWPEQTDTL-RTFYPTSVMETGHDIIFF----WvaRMM 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 285 LMAL----DLPLpKKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLM------RELPFGSDGVFTPEAFv 353
Cdd:PRK14900 511 MMGLhfmgEVPF-RTVYLHPMVRDEKGqKMSKTKGNVIDPLVITEQYGADALRFTLAaltaqgRDIKLAKERIEGYRAF- 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 354 ertnfdlANDLGNLVNRTISMVNKYFDGELPAYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFI--SRT 431
Cdd:PRK14900 589 -------ANKLWNASRFALMNLSGYQERGEDPARLARTPADRWILARLQRAVNETVEALEAFRFNDAANAVYAFVwhELC 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 432 NKYIdETTPWVLAKDDSQKDmlGNVMAHLVENIRYAAVLLRPFLTHAPKEIFEQLNINnpqfmefSSLEQYgvlTESIMV 511
Cdd:PRK14900 662 DWYI-ELAKEALASEDPEAR--RSVQAVLVHCLQTSYRLLHPFMPFITEELWHVLRAQ-------VGASAW---ADSVLA 728
|
730
....*....|....*....
gi 579670249 512 TGQPKPifPRLDSEAEIAY 530
Cdd:PRK14900 729 AEYPRK--GEADEAAEAAF 745
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
3-133 |
7.42e-15 |
|
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: 77.84 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 3 KETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEK------------AQKAGKTEI- 69
Cdd:pfam00133 22 KPSFTIHDGPPNATGSLHIGHALAKTLKDIVIRYKRMKGYYVLWVPGWDHHGLPTEQVvekklgikekktRHKYGREEFr 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579670249 70 ----EYLDEMIAGIKQLWAKLEISNdDFIR---TTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDET 133
Cdd:pfam00133 102 ekcrEWKMEYADEIRKQFRRLGRSI-DWDReyfTMDPELEAAVWEVFVRLHDKGLIYRGKKLVNWSPALNT 171
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
294-487 |
1.18e-14 |
|
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: 77.81 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 294 KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRElPFGSDGVFTPEAFVERTNFdlandLGNLVNrTI 372
Cdd:COG0060 588 KNVLTHGFVLDEDGrKMSKSLGNVVDPQEVIDKYGADILRLWVASS-DYWGDLRFSDEILKEVRDV-----YRRLRN-TY 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 373 SmvnkYFDGEL----PAYQGP----LHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFIS--------RTNK--- 433
Cdd:COG0060 661 R----FLLANLddfdPAEDAVpyedLPELDRWILSRLNELIKEVTEAYDNYDFHRAYRALHNFCVedlsnwylDISKdrl 736
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 579670249 434 YIDETTPwvLAKDDSQkdmlgNVMAHLVENIryaAVLLRPFLTHAPKEIFEQLN 487
Cdd:COG0060 737 YTEAADS--LDRRAAQ-----TTLYEVLETL---VRLLAPILPFTAEEIWQNLP 780
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
294-438 |
1.82e-13 |
|
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: 73.93 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 294 KKVFAHGWILM--KDG-------KMSKSKGNVVDPNILIDRYGLDATRYYLM------RELPFGSDGV-----Ftpeafv 353
Cdd:COG0495 566 KRLLTQGMVLEvgKDGvviggieKMSKSKGNVVDPDEIIEKYGADTLRLFEMfagppeRDLEWSDSGVegayrF------ 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 354 ertnfdlandlgnlVNRTISMVNKYFDGELPAyQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNK 433
Cdd:COG0495 640 --------------LNRVWRLVVDEAEALKLD-VADLSEADKELRRALHKTIKKVTEDIERLRFNTAIAALMELVNALYK 704
|
....*
gi 579670249 434 YIDET 438
Cdd:COG0495 705 AKDSG 709
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
3-206 |
1.41e-12 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 71.01 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 3 KETFYITTPIYYPSG-NLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQ 81
Cdd:PLN02563 109 KPKFYVLDMFPYPSGaGLHVGHPEGYTATDILARYKRMQGYNVLHPMGWDAFGLPAEQYAIETGTHPKITTLKNIARFRS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 82 LWAKLEISND--DFIRTTEERHKHVVEQVFERLLKQGDIYLGEYEGWYSVPDETYYTESQLVDpqyengkiigGKSPDSG 159
Cdd:PLN02563 189 QLKSLGFSYDwdREISTTEPEYYKWTQWIFLQLLKRGLAYQAEVPVNWCPALGTVLANEEVVD----------GLSERGG 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 579670249 160 HEVELVKEESYFFNISKYTDRLLEFYDqnpDFIQPPSRKnEMINNFI 206
Cdd:PLN02563 259 HPVIRKPMRQWMLKITAYADRLLEDLD---DLDWPESIK-EMQRNWI 301
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
3-44 |
1.49e-12 |
|
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: 70.85 E-value: 1.49e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 579670249 3 KETFYITT--PiyYPSGNLHIGHAYSTVAGDVIARYKRMQGYDV 44
Cdd:COG0495 32 KPKYYVLDmfP--YPSGRLHMGHVRNYTIGDVVARYKRMQGYNV 73
|
|
| valS |
PRK05729 |
valyl-tRNA synthetase; Reviewed |
17-123 |
2.46e-10 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 235582 [Multi-domain] Cd Length: 874 Bit Score: 63.59 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 17 GNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---Q-KIQEKAQKAGKT--EI---EYLD------EMIAG-IK 80
Cdd:PRK05729 49 GSLHMGHALNNTLQDILIRYKRMQGYNTLWLPGTDHAGiatQmVVERQLAAEGKSrhDLgreKFLEkvwewkEESGGtIT 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 579670249 81 QLWAKLEISND-DFIRTT--EERHKHVVEqVFERLLKQGDIYLGEY 123
Cdd:PRK05729 129 NQLRRLGASCDwSRERFTmdEGLSKAVRE-VFVRLYEKGLIYRGKR 173
|
|
| Anticodon_Ia_like |
cd07375 |
Anticodon-binding domain of class Ia aminoacyl tRNA synthetases and similar domains; This ... |
361-475 |
6.65e-10 |
|
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: 57.13 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 361 ANDLGNLVNRTISMVNKYFDGELPAYQGPLHEL-DEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYIDETT 439
Cdd:cd07375 7 ARAFLNRLYRLLSFFRKALGGTQPKWDNELLEEaDRELLARLQEFIKRTTNALEALDPTTAVQELFKFTNELNWYLDELK 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 579670249 440 PWVLAKDDSQKdmlgnVMAHLVENIRYAAVLLRPFL 475
Cdd:cd07375 87 PALQTEELREA-----VLAVLRAALVVLTKLLAPFT 117
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
568-653 |
3.04e-09 |
|
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.
Pssm-ID: 239196 [Multi-domain] Cd Length: 103 Bit Score: 54.82 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 568 IIDAEHVKKSDKLLKIQVDL-DSEQRQIVSGiakfyTPDDIIGKKVAVVTN---------LKPAKLMGQKSEGMILSA-- 635
Cdd:cd02796 6 VLEVEPHPNADKLNVCKVDIgENKPLQIVCG-----APNVRAGDKVVVALPgavlpgglkIKKRKLRGVESEGMLCSAke 80
|
90 100
....*....|....*....|...
gi 579670249 636 -----EKDGVLTlvsLPSAIPNG 653
Cdd:cd02796 81 lglgeDSDGIIE---LPEDAPVG 100
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
5-145 |
5.19e-09 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 58.15 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 5 TFYITTPIYYpsGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEIEYLDEMIAGIKQLWA 84
Cdd:pfam01406 11 TMYVCGPTVY--DYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579670249 85 KLEISNDDF-IRTTEerhkHVVEQV--FERLLKQGDIYLGEyegwysvPDETYYTESQlvDPQY 145
Cdd:pfam01406 89 ALNVLPPDLePRVTE----HIDEIIefIERLIKKGYAYVSD-------NGDVYFDVSS--FPDY 139
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
292-566 |
5.44e-09 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 59.50 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 292 LPKKVFAHGWILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLMrelpfgsdgvftpeafverTNFDLANDLG---NLV 368
Cdd:PRK12300 561 WPRGIVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT-------------------SSAELLQDADwreKEV 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 369 NRTISMVNKYFD--GELPAYQG--PLHELDEEMEAMALETVKSYTESMESLQFSVALSTVW-KFISRTNKYIDETtpwvl 443
Cdd:PRK12300 622 ESVRRQLERFYElaKELIEIGGeeELRFIDKWLLSRLNRIIKETTEAMESFQTRDAVQEAFyELLNDLRWYLRRV----- 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 444 akDDSQKDMLGNVmahlvenIRYAAVLLRPFLTHAPKEIFEQLNINnpqfmEFSSLEQYgvltesimvtgqPKPIFPRLD 523
Cdd:PRK12300 697 --GEANNKVLREV-------LEIWIRLLAPFTPHLAEELWHKLGGE-----GFVSLEKW------------PEPDESKID 750
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 579670249 524 SEAEIA--YIKesmqppATEEEKEEIPSKPQIDIKdfdKVEIKAA 566
Cdd:PRK12300 751 EEAELAeeYVK------RLIEDIREILKVAKIKPK---KVYIYVA 786
|
|
| PLN02381 |
PLN02381 |
valyl-tRNA synthetase |
2-119 |
5.57e-09 |
|
valyl-tRNA synthetase
Pssm-ID: 215214 [Multi-domain] Cd Length: 1066 Bit Score: 59.53 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 2 AKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---QKIQEKA---------QKAGKTEI 69
Cdd:PLN02381 126 SKPPFVIVLPPPNVTGALHIGHALTAAIEDTIIRWKRMSGYNALWVPGVDHAGiatQVVVEKKlmrerhltrHDIGREEF 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 579670249 70 ---------EYLDEMIAGIKQLWAKLEISNDDFirTTEERHKHVVEQVFERLLKQGDIY 119
Cdd:PLN02381 206 vsevwkwkdEYGGTILNQLRRLGASLDWSRECF--TMDEQRSKAVTEAFVRLYKEGLIY 262
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
14-64 |
1.56e-08 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 57.86 E-value: 1.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 579670249 14 YPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG--------QKIQEKAQKA 64
Cdd:PLN02843 42 YANGDLHIGHALNKILKDFINRYQLLQGKKVHYVPGWDCHGlpielkvlQSLDQEARKE 100
|
|
| PLN02563 |
PLN02563 |
aminoacyl-tRNA ligase |
308-486 |
1.73e-08 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178177 [Multi-domain] Cd Length: 963 Bit Score: 57.91 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 308 KMSKSKGNVVDPNILIDRYGLDATRYYLMRELPF---------GSDGVFTpeaFVERTNfdlandlgNLVNRTISMVNKY 378
Cdd:PLN02563 723 KMSKSRGNVVNPDDVVSEYGADSLRLYEMFMGPLrdsktwstsGVEGVHR---FLGRTW--------RLVVGAPLPDGSF 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 379 FDGELPAYQGPlhelDEEMEAMALETVKSYTESMESLQFSVALSTVWKFISRTNKYidETTPwvlakddsqkdmlgnvma 458
Cdd:PLN02563 792 RDGTVVTDEEP----SLEQLRLLHKCIAKVTEEIESTRFNTAISAMMEFTNAAYKW--DKVP------------------ 847
|
170 180
....*....|....*....|....*...
gi 579670249 459 hlVENIRYAAVLLRPFLTHAPKEIFEQL 486
Cdd:PLN02563 848 --REAIEPFVLLLSPYAPHLAEELWFRL 873
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
14-70 |
1.74e-08 |
|
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: 57.78 E-value: 1.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579670249 14 YPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG----QKIqEKAQKAGKTEIE 70
Cdd:COG0060 56 YANGDIHIGHALNKILKDIIVRYKTMRGFDVPYVPGWDCHGlpieLKV-EKELGIKKKDIE 115
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
2-119 |
2.65e-08 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 57.32 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 2 AKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---QKIQEKA--QKAGKTEIEYLDEmi 76
Cdd:PTZ00419 58 SGKKFVIVLPPPNVTGYLHIGHALTGAIQDSLIRYHRMKGDETLWVPGTDHAGiatQVVVEKKlmKEENKTRHDLGRE-- 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579670249 77 AGIKQLW------------------AKLEISNDDFirTTEERHKHVVEQVFERLLKQGDIY 119
Cdd:PTZ00419 136 EFLKKVWewkdkhgnnicnqlrrlgSSLDWSREVF--TMDEQRSKAVKEAFVRLYEDGLIY 194
|
|
| ValS |
COG0525 |
Valyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Valyl-tRNA synthetase ... |
17-123 |
4.74e-08 |
|
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: 56.21 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 17 GNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---Q-KIQEKAQKAGKT--EI---EYLDE----------MIa 77
Cdd:COG0525 48 GSLHMGHALNNTLQDILIRYKRMQGYNTLWQPGTDHAGiatQaVVERQLAEEGKSrhDLgreKFLERvwewkeesggTI- 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 579670249 78 gIKQLwAKLEISND--------DfirttEERHKHVVEqVFERLLKQGDIYLGEY 123
Cdd:COG0525 127 -TNQL-RRLGASCDwsrerftmD-----EGLSKAVRE-VFVRLYEKGLIYRGKR 172
|
|
| PLN02882 |
PLN02882 |
aminoacyl-tRNA ligase |
281-347 |
1.61e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215477 [Multi-domain] Cd Length: 1159 Bit Score: 54.73 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 281 WPILLMAL-----DLPLPKKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYYLMRE-------LPFGSDGVF 347
Cdd:PLN02882 581 WFYTLMVLstalfDKPAFKNLICNGLVLAEDGkKMSKSLKNYPDPNEVIDKYGADALRLYLINSpvvraepLRFKEEGVF 660
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
556-654 |
1.82e-07 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 54.41 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 556 KDFDKVEIkaATIIDAEHVKKSDKLLKIQVDLDSEQRQIVSG---IAKfytpddiiGKKVAVVTN---------LKPAKL 623
Cdd:PRK00629 40 AGLSGVVV--GKVLECEKHPNADKLRVCQVDVGEEPLQIVCGapnVRA--------GDKVPVALPgavlpggfkIKKAKL 109
|
90 100 110
....*....|....*....|....*....|....*...
gi 579670249 624 MGQKSEGMILSA-------EKDGVLTlvsLPSAIPNGA 654
Cdd:PRK00629 110 RGVESEGMLCSAselglsdDHDGIIE---LPEDAPVGT 144
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
2-123 |
3.75e-07 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 53.41 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 2 AKETFYITTPIYYPSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHG---QKIQEK---AQKAGKTEI------ 69
Cdd:PLN02943 86 GGDPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMKGRPTLWIPGTDHAGiatQLVVEKmlaSEGIKRTDLgrdeft 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579670249 70 --------EYLDEMIAGIKQLWAKLEISNDDFirTTEERHKHVVEQVFERLLKQGDIYLGEY 123
Cdd:PLN02943 166 krvwewkeKYGGTITNQIKRLGASCDWSRERF--TLDEQLSRAVVEAFVRLHEKGLIYQGSY 225
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
19-50 |
7.56e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 52.56 E-value: 7.56e-07
10 20 30
....*....|....*....|....*....|....*..
gi 579670249 19 LHIGHAYSTVAGDVIARYKRMQGYDVRY-----LTGT 50
Cdd:PRK12300 1 LHVGHGRTYTIGDVIARYKRMRGYNVLFpmafhVTGT 37
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
20-88 |
9.82e-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: 49.88 E-value: 9.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 579670249 20 HIGHAYSTVAGDVIARYKRMQGYDVRY---LTGTDEhgqKIQEKAQKAGKTEIEYLDEMIAGIKQLWAKLEI 88
Cdd:cd00672 35 HIGHARTYVVFDVLRRYLEDLGYKVRYvqnITDIDD---KIIKRAREEGLSWKEVADYYTKEFFEDMKALNV 103
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
20-82 |
8.31e-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: 8.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 20 HIGHAYSTVAGDVIARYKRMQGYDVRY---LTGTDEhgqKIQEKAQKAGKT--EI--EYLDEMIAGIKQL 82
Cdd:COG0215 37 HIGHARTFVVFDVLRRYLRYLGYKVTYvrnITDVDD---KIIKRAAEEGESiwELaeRYIAAFHEDMDAL 103
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
15-186 |
1.22e-05 |
|
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273085 [Multi-domain] Cd Length: 563 Bit Score: 48.49 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 15 PSGNLHIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKI-----------QEKAQKAGKTEIEYLDEMIAGIKQLW 83
Cdd:TIGR00456 123 PAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFgllalgvekfgNEALNIAVKKPDHGLEGFYVEINKRL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 84 AK---LEISNDDFIRTTEERHKHVVEqVFERLLKqgdIYLGEYEGWYS---VPDETYYTESQLVdpqyengkiiggKSPD 157
Cdd:TIGR00456 203 EEneeLEEEARELFVKLESGDEETIK-LWKRLVE---YSLEGIKETYDrlnIHFDSFVWEGESV------------KNGM 266
|
170 180
....*....|....*....|....*....
gi 579670249 158 SGHEVELVKEESYFFNISKYTDRLLEFYD 186
Cdd:TIGR00456 267 LPKVLEDLKEKGLVVEDGALWLDLTLFGD 295
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
15-125 |
1.33e-05 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 48.23 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 15 PSGNLHIGHAYSTVAGDVIARYKRMQGYDV--RYLTGtDeHGQKI-------QEKAQKAgkteieyLDEMIAGIKQLWAK 85
Cdd:PRK01611 122 PTGPLHVGHLRSAVIGDALARILEFAGYDVtrEYYVN-D-AGTQIgmliaslELLWRKA-------VDISLDEIKEDLDR 192
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 579670249 86 LEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYlGEYEG 125
Cdd:PRK01611 193 LGVHFDVWFSESELYYNGKVDEVVEDLKEKGLLY-VESDG 231
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
15-125 |
3.75e-05 |
|
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) 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. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.
Pssm-ID: 185675 [Multi-domain] Cd Length: 212 Bit Score: 45.25 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 15 PSGNLHIGHAYSTVAGDVIARYKRMQGYDV--RYLTGtdEHGQKIQEKAQKAGKTEiEYLDEMIAGIKQLWAKLEISNDD 92
Cdd:cd00671 11 PTGPLHVGHLRNAIIGDSLARILEFLGYDVtrEYYIN--DWGRQIGLLILSLEKWR-KLVEESIKADLETYGRLDVRFDV 87
|
90 100 110
....*....|....*....|....*....|...
gi 579670249 93 FirTTEERHKHVVEQVFERLLKQGDIYlgEYEG 125
Cdd:cd00671 88 W--FGESSYLGLMGKVVELLEELGLLY--EEDG 116
|
|
| PLN02843 |
PLN02843 |
isoleucyl-tRNA synthetase |
294-486 |
3.96e-05 |
|
isoleucyl-tRNA synthetase
Pssm-ID: 215452 [Multi-domain] Cd Length: 974 Bit Score: 47.07 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 294 KKVFAHGWILMKDG-KMSKSKGNVVDPNILID---------RYGLDATRYYLmrelpfgsdgvftpeAFVERTNfDLAnd 363
Cdd:PLN02843 596 KSVLTHGFVLDEKGfKMSKSLGNVVDPRLVIEggknqkqepAYGADVLRLWV---------------ASVDYTG-DVL-- 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 364 LGNLVNRTISMVNKYFDGELPAYQGPLHELDEE----------MEAMAL----ETVKSYTESMESLQFSVALSTVWKFIS 429
Cdd:PLN02843 658 IGPQILKQMSDIYRKLRGTLRYLLGNLHDWKPDnavpyedlpsIDKYALfqleNVVNEIEESYDNYQFFKIFQILQRFTI 737
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 579670249 430 --RTNKYIDETTP--WVLAKDDSQKDMLGNVMAHLVENIRYAavlLRPFLTHAPKEIFEQL 486
Cdd:PLN02843 738 vdLSNFYLDVAKDrlYVGGTTSFTRRSCQTVLAAHLLSLLRA---IAPILPHLAEDAWQNL 795
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
295-437 |
5.50e-05 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 46.25 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 295 KVFAH-----GWILMKDGKMSKSKGNVVDPNILIDRYGLDATRYYLM----RelpfgSDGVFTPEAFVE-RTNFD-LAND 363
Cdd:COG0215 247 KPFARywmhnGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLsahyR-----SPLDFSEEALEEaEKALErLYNA 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 579670249 364 LGNLVNRTismvnkyfdGELPAYQGPLHELDEE-MEAMAletvksytesmESLQFSVALSTVWKFISRTNKYIDE 437
Cdd:COG0215 322 LRRLEEAL---------GAADSSAEEIEELREEfIAAMD-----------DDFNTPEALAVLFELVREINKALDE 376
|
|
| PLN02943 |
PLN02943 |
aminoacyl-tRNA ligase |
213-439 |
1.05e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215509 [Multi-domain] Cd Length: 958 Bit Score: 45.70 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 213 LAVSRTSFNWGVHVPSNPKhVVYVWIDALVNYISALGYLSDDESLFNRYWPADIHLMAKEIVRFhsiiW--PILLMALDL 290
Cdd:PLN02943 487 LEKAREKYGKDVEIYQDPD-VLDTWFSSALWPFSTLGWPDVSAEDFKKFYPTTVLETGHDILFF----WvaRMVMMGIEF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 291 --PLP-KKVFAHGWILMKDG-KMSKSKGNVVDPNILIDRYGLDATRYylmrELPFGSDGvftpeafvertnfdlaNDLGN 366
Cdd:PLN02943 562 tgTVPfSYVYLHGLIRDSQGrKMSKTLGNVIDPLDTIKEFGTDALRF----TLALGTAG----------------QDLNL 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 579670249 367 LVNRTISmvNKYFDGEL-PAYQGPLHELDEEMEAMALETVKSYTESMESLQFSVALSTVWkFISRTNKYIDETT 439
Cdd:PLN02943 622 STERLTS--NKAFTNKLwNAGKFVLQNLPSQSDTSAWEHILACKFDKEESLLSLPLPECW-VVSKLHELIDSVT 692
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
260-335 |
2.21e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 44.68 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 260 RYW-PADIHLMAKEIVR----F----HSIIWPillmalDLPLPKKVFAHGWILMKDGKMSKSKGNVVDPNILIDRYGLDA 330
Cdd:PLN02959 667 EYWyPFDLRVSGKDLIQnhltFaiynHTAIWA------EEHWPRGFRCNGHLMLNSEKMSKSTGNFLTLRQAIEEFSADA 740
|
....*
gi 579670249 331 TRYYL 335
Cdd:PLN02959 741 TRFAL 745
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
292-324 |
2.86e-04 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 44.23 E-value: 2.86e-04
10 20 30
....*....|....*....|....*....|....*
gi 579670249 292 LP-KKVFAHGWILMKDG-KMSKSKGNVVDPNILID 324
Cdd:PTZ00419 567 LPfKTVFLHAMVRDSQGeKMSKSKGNVIDPLEVIE 601
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
20-82 |
9.56e-04 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 42.23 E-value: 9.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 579670249 20 HIGHAYSTVAGDVIARYKRMQGYDVRYLTGTDEHGQKIQEKAQKAGKTEI----EYLDEMIAGIKQL 82
Cdd:PLN02946 95 HIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGEDPIslsrRYCEEFLSDMAYL 161
|
|
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
15-125 |
9.90e-04 |
|
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439789 [Multi-domain] Cd Length: 574 Bit Score: 42.06 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 15 PSGNLHIGHAYSTVAGDVIARYKRMQGYDV---------------------RY--------LTGTDEHGQ---------- 55
Cdd:COG0018 127 PTKPLHVGHLRGAVIGDALARILEAAGYDVtrenyindagtqigklalsleRYgeeeiepeSKPDGYLGDlyvkfhkeye 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 56 ---KIQEKAQK------AGKTEI-----EYLDEMIAGIKQLWAKLEISNDDFIRTTEERHKHVVEQVFERLLKQGDIYlg 121
Cdd:COG0018 207 edpELEDIAREllaklePGDEEAlelwkKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELKEKGLLY-- 284
|
....
gi 579670249 122 EYEG 125
Cdd:COG0018 285 ESDG 288
|
|
| PTZ00427 |
PTZ00427 |
isoleucine-tRNA ligase, putative; Provisional |
258-336 |
7.03e-03 |
|
isoleucine-tRNA ligase, putative; Provisional
Pssm-ID: 173617 [Multi-domain] Cd Length: 1205 Bit Score: 39.56 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 579670249 258 FNRYWPADIHLMAKEIVR--FHSIIWPILLMALDLPLpKKVFAHGWILMKDGK-MSKSKGNVVDPNILIDRYGLDATRYY 334
Cdd:PTZ00427 668 FHKIFPADFIAEGLDQTRgwFYTLLVISTLLFDKAPF-KNLICNGLVLASDGKkMSKRLKNYPDPLYILDKYGADSLRLY 746
|
..
gi 579670249 335 LM 336
Cdd:PTZ00427 747 LI 748
|
|
| |
