|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
17-473 |
0e+00 |
|
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: 711.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 17 LRLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADA 96
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 97 GRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDGDVYFNVATLPDYGKLSGHRIDD 176
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 177 VHQGE--GVATGKRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQA 254
Cdd:COG0215 162 LRAGArvEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 255 EAA-GDGFARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQDAVKAYAGVEDF 333
Cdd:COG0215 242 EAAtGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 334 LHRVRTRVGTVVPG-----DWTPKFAAALDDDLSVPIALAEVHAARAVGNRALDSG-DHETAMTQARSIRAMMGILGCDP 407
Cdd:COG0215 322 LRRLEEALGAADSSaeeieELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGeDKAALAALAALLRALGGVLGLLL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123368663 408 LDERWESRDETSAALAA-IDVLvrwaLDSRADARNRKDWATADQIRDRLKEAGIEVTDTADGPQWSL 473
Cdd:COG0215 402 LEPEAWQGAAEDELLDAlIEAL----IEERAEARKAKDFARADRIRDELAALGIVLEDTPDGTTWRR 464
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
30-325 |
6.37e-180 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 505.75 E-value: 6.37e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 30 FVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADAGRPWWEWAATYER 109
Cdd:pfam01406 2 FVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 110 AFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAY-TGDGDVYFNVATLPDYGKLSGHRIDDVHQGEG--VATG 186
Cdd:pfam01406 82 AYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYvSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARgeVSEG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 187 KRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQAEAAGDG-FARFW 265
Cdd:pfam01406 162 KRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKqLANYW 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 266 LHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQDAVK 325
Cdd:pfam01406 242 LHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAKS 301
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
17-471 |
5.58e-156 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 451.07 E-value: 5.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 17 LRLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADA 96
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 97 GRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAY-TGDGDVYFNVATLPDYGKLSGHRID 175
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYvSDNGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 176 DVHQGEG--VATGKRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQ 253
Cdd:TIGR00435 161 QLEAGARvdVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 254 AEAAGDG-FARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQDAVKAYAGVED 332
Cdd:TIGR00435 241 SEAAFGKqLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 333 FLHRVRTRVG---------TVVPGDWTPKFAAALDDDLSVPIALAEVHA-ARAVGNRALDSGDHETAMTQARSIRAMMGI 402
Cdd:TIGR00435 321 ALRVLDTSLAysgnqslnkFPDEKEFEARFVEAMDDDLNTANALAVLFElAKSINLTFVSKADAALLIEHLIFLESRLGL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123368663 403 LGCDPldERWESRDEtSAALAAIDVLVRwaldSRADARNRKDWATADQIRDRLKEAGIEVTDTADGPQW 471
Cdd:TIGR00435 401 LLGLP--SKPVQAGS-NDDLGEIEALIE----ERSIARKEKDFAKADEIRDELAKKGIVLEDTPQGTTW 462
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
5-471 |
2.39e-125 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 376.19 E-value: 2.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 5 ADADRPATSPTGLRLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTD 84
Cdd:PLN02946 48 ASNGAPASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 85 IDDKILNKAADAGRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDGDVYFNVATLP 164
Cdd:PLN02946 128 VDDKIIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 165 DYGKLSGHRIDDVHQGEGVA--TGKRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDL 242
Cdd:PLN02946 208 EYGKLSGRKLEDNRAGERVAvdSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 243 VFPHHENEIAQAEAAGDGFA-RFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQ 321
Cdd:PLN02946 288 VFPHHENEIAQSCAACCDSNiSYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 322 DAVKAYAGVEDFLHRVRTRVG---TVVPGDWTP------------KFAAALDDDLSVPIALAEVHAARAVGNRALDSGDH 386
Cdd:PLN02946 368 SASERIFYIYQTLHDCEESLQqhdSTFEKDSVPpdtlncinkfhdEFVTSMSDDLHTPVALAALSEPLKTINDLLHTRKG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 387 ETAMTQARSIRAM-------MGILGCDP--LDERWESRDETS---AALAAIDVLVRwaLDSRADARNRKDWATADQIRDR 454
Cdd:PLN02946 448 KKQEKRLESLAALekkirdvLSVLGLMPtsYSEALQQLREKAlrrAKLTEEQVLQK--IEERTVARKNKEYEKSDAIRKD 525
|
490
....*....|....*..
gi 123368663 455 LKEAGIEVTDTADGPQW 471
Cdd:PLN02946 526 LAAVGIALMDSPDGTTW 542
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
14-475 |
8.83e-109 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 336.62 E-value: 8.83e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 14 PTGLRLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAK-GLDVAFIRNVTDIDDKILNK 92
Cdd:PTZ00399 37 LTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYfGYDVFYVMNITDIDDKIIKR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 93 AADAGRPWW-EWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDGDVYFNVATL----PDYG 167
Cdd:PTZ00399 117 AREEKLSIFlELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFrkagHVYP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 168 KLSGHRIDDVHQ---GEGVATG----KRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGM 240
Cdd:PTZ00399 197 KLEPESVADEDRiaeGEGALGKvsgeKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 241 DLVFPHHENEIAQAEAAGD--GFARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSET 318
Cdd:PTZ00399 277 DLKFPHHDNELAQSEAYFDkhQWVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 319 ALQDAV---KAYagvEDFLHRVRTRVGTVVPGD---WTP--------------KFAAALDDDLSVPIALAEVHAARAVGN 378
Cdd:PTZ00399 357 SMDEAIekdKVF---FNFFANVKIKLRESELTSpqkWTQhdfelnelfeetksAVHAALLDNFDTPEALQALQKLISATN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 379 RALDSGDHETAmTQARSIRA----MMGILGCDPLDERWESRDETSAA---LAAIDVLVRWALDSRADARNRKDWA----- 446
Cdd:PTZ00399 434 TYLNSGEQPSA-PLLRSVAQyvtkILSIFGLVEGSDGLGSQGQNSTSenfKPLLEALLRFRDEVRDAAKAEMKLIsldkk 512
|
490 500 510
....*....|....*....|....*....|....*..
gi 123368663 447 ------TADQIRD-RLKEAGIEVTDTADGPQ-WSLLD 475
Cdd:PTZ00399 513 kkqllqLCDKLRDeWLPNLGIRIEDKPDGPSvWKLDD 549
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
17-472 |
1.76e-107 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 328.03 E-value: 1.76e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 17 LRLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDI----------D 86
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 87 DKILNKAADAGRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDGDVYFNVATLPDY 166
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFPSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 167 GKLSGHRIDDVHQGEGVA--TGKRDQRDFTLWKGAKPGEP---SWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMD 241
Cdd:PRK14536 163 GSLASAAVEDLQAGARIEhdTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 242 LVFPHHENEIAQAEAA-GDGFARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQR-VRAAELRYYLGSAHYRSMLEFSETA 319
Cdd:PRK14536 243 HIRVHHTNEIAQCEAAtGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 320 LQDA-------VKAYAGVEDFLHRVRTRVGTVVPGDWTPK---------------FAAALDDDLSVPIALAEVHaaRAVG 377
Cdd:PRK14536 323 LKTAkaarrslVRRVARVVDAARATTGSVRGTLAECAAERvaesrasesellltdFRAALEDDFSTPKALSELQ--KLVK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 378 NRALDSGDHETAMTqarsirAMMGILGCDPLDERWESRDETSAALAA---IDVLVRwaldSRADARNRKDWATADQIRDR 454
Cdd:PRK14536 401 DTSVPPSLCLSVLQ------AMDTVLGLGLIQEATASLSAQVPAGPSeeeIGQLIE----ARAHARQTKDFPLADEIRDK 470
|
490
....*....|....*...
gi 123368663 455 LKEAGIEVTDTADGPQWS 472
Cdd:PRK14536 471 LKAEGIELEDTHLGTIWK 488
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
19-471 |
1.01e-103 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 324.75 E-value: 1.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 19 LYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADAGR 98
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 99 PWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAY-TGDGDVYFNVATLPDYGKLSGHRIDDV 177
Cdd:PRK14535 310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYGQLSGKSLDDL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 178 HQGEGVATG--KRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQAE 255
Cdd:PRK14535 390 RAGERVEVDgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 256 AA--------------GDGFA---RFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSET 318
Cdd:PRK14535 470 GAtghtcghhhaqthhGQSIAshvKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 319 ALQDAVKAyagvedfLHRVRTRVGTVVPG---------DWTPKFAAALDDDLSVPIALAEVHAARAVGNRALDSgdheta 389
Cdd:PRK14535 550 HLDDAKGA-------LTRLYTTLKNTPAAefmlsenvnDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKTNDA------ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 390 mTQARSIRAMMGILGCdplderwESRDETS--AALAAIDVLVRWALDS----RADARNRKDWATADQIRDRLKEAGIEVT 463
Cdd:PRK14535 617 -QLAGCLKALGGIIGL-------LQRDPTEflQGGAASDGLSNEEIEDliarRKQARADKNWAESDRIRDLLNEHKIILE 688
|
....*...
gi 123368663 464 DTADGPQW 471
Cdd:PRK14535 689 DNAGGTTW 696
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
18-316 |
2.65e-99 |
|
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: 297.18 E-value: 2.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 18 RLYDTMTGAVRDFVPLRDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADAG 97
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 98 RPWWEWAATYERAFSAAYDALGVLPPSAEPRAtghitqmvelierlidrghaytgdgdvyfnvatlpdygklsghriddv 177
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 178 hqgegvatgkrdqrdftlwkgakpgepswptpwgrgrpgWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQAEAA 257
Cdd:cd00672 113 ---------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAA 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 258 -GDGFARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFS 316
Cdd:cd00672 154 tGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
13-402 |
3.00e-79 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 252.72 E-value: 3.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 13 SPTGLRLYDTMTGAVRDFVPlrDGHVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNK 92
Cdd:TIGR03447 14 TGPPLRLFDTADGQVRPVEP--GPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 93 AADAGRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDG----DVYFNVATLPDYGK 168
Cdd:TIGR03447 92 AERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGpeypDVYFSIDATEQFGY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 169 LSGHRIDDVHQ------GEGVATGKRDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDL 242
Cdd:TIGR03447 172 ESGYDRATMLElfaergGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 243 VFPHHENEIAQAEAA--GDGFARFWLHNGWVTMGGEKMSKSLGNVLsipaVLQRVRAA-----ELRYYLGSAHYRSMLEF 315
Cdd:TIGR03447 252 IFPHHEFSAAHAEAAtgVRRMARHYVHAGMIGLDGEKMSKSLGNLV----FVSKLRAAgvdpaAIRLGLLAGHYRQDRDW 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 316 SETALQDAvkayagvEDFLHRVRTRVGTVVPGDWTPKFA---AALDDDLSVPIALAEVHAAravGNRALDSGDHETAMTQ 392
Cdd:TIGR03447 328 TDAVLAEA-------EARLARWRAALALPDAPDATDLIArlrQHLANDLDTPAALAAVDGW---AADALSYGGSDTEAPA 397
|
410
....*....|..
gi 123368663 393 --ARSIRAMMGI 402
Cdd:TIGR03447 398 lvATAVDALLGV 409
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
38-402 |
4.36e-76 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 243.68 E-value: 4.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 38 VSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKAADAGRPWWEWAATYERAFSAAYDA 117
Cdd:PRK12418 10 ATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 118 LGVLPPSAEPRATGHITQMVELIERLIDRGHAY----TGDGDVYFNVATLPDYGKLSGHRIDDV------HQGEGVATGK 187
Cdd:PRK12418 90 LRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvddEEYPDVYFSVDATPQFGYESGYDRATMlelfaeRGGDPDRPGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 188 RDQRDFTLWKGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGGMDLVFPHHENEIAQAEAA--GDGFARFW 265
Cdd:PRK12418 170 RDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAAtgERRFARHY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 266 LHNGWVTMGGEKMSKSLGN-VLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQDAvkayagvEDFLHRVRTRVGTV 344
Cdd:PRK12418 250 VHAGMIGLDGEKMSKSRGNlVFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEA-------EARLARWRAAAALP 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123368663 345 VPGDWTPKFAA---ALDDDLSVPIALAEVHAARAvgnRALDSGDHETAMTQ--ARSIRAMMGI 402
Cdd:PRK12418 323 AGPDAADVVARvraALADDLDTPGALAAVDGWAT---DALEGGGDDAAAPAlvATAVDALLGV 382
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
17-468 |
6.49e-52 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 182.74 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 17 LRLYDTMTGAVRDFVPLRDghVSIYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDI----------D 86
Cdd:PRK14534 3 LKLYNTKTKDLSELKNFSD--VKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 87 DKILNKAADAGRPWWEWAATYERAFSAAYDALGVLPPSAEPRATGHITQMVELIERLIDRGHAYTGDGDVYFNVATLPDY 166
Cdd:PRK14534 81 DKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCFKSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 167 GKLSGHRIDDVHQGE----GVATGKRDQRDFTLW---KGAKPGEPSWPTPWGRGRPGWHTECVAMCEAYLGAEFDIHAGG 239
Cdd:PRK14534 161 GQMAGINLNDFKDMSvsrvEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 240 MDLVFPHHENEIAQAEA-AGDGFARFWLHNGWVTMGGEKMSKSLGNVLSIPAV-LQRVRAAELRYYLGSAHYRSMLEFSE 317
Cdd:PRK14534 241 VDHIGVHHINEIAIAECyLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 318 TALQDAVKA-----------YAGVEDF----LHRVRTRVGTVVPGDWTPKFAAALDDDLSVPIALAEVHaaravgnrALD 382
Cdd:PRK14534 321 NNLKACKIArenmlnkltyfYSSLDQFdlnlLNKDLENIEFSLEKEYYDSFLEKIAFDLNIPQGLALLW--------DII 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 383 SGDHETAMTQARSIRAMMGILGcdpLDERWESRDETSAALAAIDVLVRWALDSRADARNRKDWATADQIRDRLKEAGIEV 462
Cdd:PRK14534 393 KDDNLSFLSKLRLAFKFDEVLS---LGLREEILREIENHRIVIDDNMKSLIEERRLAKCEKDFKRADEIREYFASKGFVL 469
|
....*.
gi 123368663 463 TDTADG 468
Cdd:PRK14534 470 IDTEEG 475
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
317-471 |
6.55e-19 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), 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. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.
Pssm-ID: 153417 [Multi-domain] Cd Length: 156 Bit Score: 83.38 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 317 ETALQDAvkaYAGVEDFLHRVRTRVGTVVPGDW----TPKFAAALDDDLSVPIALA---EVhaARAVgNRALDSgDHETA 389
Cdd:cd07963 1 DDNLEDA---RAALERLYTALRGVPPTTVDIDWgepfAERFIAAMDDDFNTPEALAvlfEL--AREI-NRLKKE-DIEKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 390 MTQARSIRAMMGILGC---DPLDERWESRDETSAALAAIDVLVrwalDSRADARNRKDWATADQIRDRLKEAGIEVTDTA 466
Cdd:cd07963 74 AALAALLKALGGVLGLlqqDPEAFLQGGTGEGGLSVAEIEALI----AQRNQARKAKDWAEADRIRDELAAQGIILEDSP 149
|
....*
gi 123368663 467 DGPQW 471
Cdd:cd07963 150 EGTTW 154
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
47-304 |
1.98e-11 |
|
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: 64.86 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 47 VQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFirnVTDIDD---KILNKAADAGRPWWEWAATYERAFSAAYDALGVlpp 123
Cdd:cd00814 11 VNGVPHLGHLYGTVLADVFARYQRLRGYDVLF---VTGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNI--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 124 S-------AEPRatgHITQMVELIERLIDRGHAYTGDGDVYFNVAT----------------LPDYGK-----LSGHriD 175
Cdd:cd00814 85 SfdyfirtTSPR---HKEIVQEFFKKLYENGYIYEGEYEGLYCVSCerflpewreeehyffrLSKFQDrllewLEKN--P 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 176 DVHQGEGVA--------TGKRD---QRDFTLWkGAK-PGEPS-------------------WPTPWGRGRPGWHTECVam 224
Cdd:cd00814 160 DFIWPENARnevlswlkEGLKDlsiTRDLFDW-GIPvPLDPGkviyvwfdaligyisatgyYNEEWGNSWWWKDGWPE-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 225 ceaylgaefDIHAGGMDLVfPHHeneiaqaeaagdgfARFW---LH------------NGWVTMGGEKMSKSLGNVLSIP 289
Cdd:cd00814 237 ---------LVHFIGKDII-RFH--------------AIYWpamLLgaglplptrivaHGYLTVEGKKMSKSRGNVVDPD 292
|
330
....*....|....*
gi 123368663 290 AVLQRVRAAELRYYL 304
Cdd:cd00814 293 DLLERYGADALRYYL 307
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
40-282 |
2.03e-11 |
|
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: 61.73 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 40 IYLCGATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNVTDIDDKILNKaadAGRPWWEWAATYERafsaaydalg 119
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDP---ANKKGENAKAFVER---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 120 vlppsaepratghitqmveLIERLIDrghaytgdgdvyfnvatlpDYgklsghriddvhqgegvatgkrdqrdftlwkga 199
Cdd:cd00802 68 -------------------WIERIKE-------------------DV--------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 200 kpgepswptpwgrgrpGWHTECVAMCEAYLGAEFDIHAGGMDLVFpHHENEIAQAEAAGDGFARFWLHNGWVTM-GGEKM 278
Cdd:cd00802 77 ----------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGGPARPFGLTFGRVMGaDGTKM 139
|
....
gi 123368663 279 SKSL 282
Cdd:cd00802 140 SKSK 143
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
45-304 |
3.34e-11 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 65.29 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 45 ATVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIrnvTDIDD---KILNKAADAGRPWWEWAATYERAFSAAYDALGV- 120
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNIs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 121 ----LPPSAEPratgHITQMVELIERLIDRGHAYTGD-------GD-VYFNVATLPDYGKLSGHRIDDVHQ--------- 179
Cdd:PRK11893 87 yddfIRTTDPR----HKEAVQEIFQRLLANGDIYLGKyegwycvRCeEFYTESELIEDGYRCPPTGAPVEWveeesyffr 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 180 ----GEGVATGKRDQRDFTLWKGA--------KPGEP---------SW--PTPWGRGRP---------------GWHTEC 221
Cdd:PRK11893 163 lskyQDKLLELYEANPDFIQPASRrnevisfvKSGLKdlsisrtnfDWgiPVPGDPKHViyvwfdaltnyltalGYPDDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 222 VAMCEAYL-GAEFDIHAGGMDLVFPHHENEIAQAEAAG-DGFARFwLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAE 299
Cdd:PRK11893 243 ELLAELFNkYWPADVHLIGKDILRFHAVYWPAFLMAAGlPLPKRV-FAHGFLTLDGEKMSKSLGNVIDPFDLVDEYGVDA 321
|
....*
gi 123368663 300 LRYYL 304
Cdd:PRK11893 322 VRYFL 326
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
46-306 |
2.14e-10 |
|
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: 61.67 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 46 TVQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFIRNvTDI---------DDKILNKAADAGRPW-----WEWAATYERAF 111
Cdd:cd00668 10 YANGSLHLGHALTHIIADFIARYKRMRGYEVPFLPG-WDThglpielkaERKGGRKKKTIWIEEfredpKEFVEEMSGEH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 112 SAAYDALGVLPPSAEPRATGHIT--QMVELI-ERLIDRGHAYTGDGDVYFNVATLPDYGKLSGHRIDDVHQGEGVATGKR 188
Cdd:cd00668 89 KEDFRRLGISYDWSDEYITTEPEysKAVELIfSRLYEKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 189 DQrdFTLW-KGAKPGEPSWPTPWGRGRPGWHTE------------CVAMCEAYLGAEF---DIHAGGMDLVFPHHENEIA 252
Cdd:cd00668 169 NR--MEAWlESLLDWAISRQRYWGTPLPEDVFDvwfdsgigplgsLGYPEEKEWFKDSypaDWHLIGKDILRGWANFWIT 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 123368663 253 QAEAA-GDGFARFWLHNGWVTM-GGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGS 306
Cdd:cd00668 247 MLVALfGEIPPKNLLVHGFVLDeGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTS 302
|
|
| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
352-406 |
4.71e-09 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 52.18 E-value: 4.71e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 123368663 352 KFAAALDDDLSVPIALAEVH-AARAVGNRALDSGDHETAMTQARSIRAMMGILGCD 406
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFeLAREINRLALKATDAEELAALAALLRALGGVLGLL 56
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
352-404 |
1.15e-07 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 48.35 E-value: 1.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 123368663 352 KFAAALDDDLSVPIALAEVH-AARAVgNRALDSGDHETAMTQARSIRAMMGILG 404
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFeLAKEI-NRALKTNDAEAAAALAALLRELGDVLG 53
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
268-414 |
2.27e-07 |
|
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: 53.19 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 268 NGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLgsAHYRSM---LEFSETALQDAVKAyagveD-------FLHRV 337
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYL--LREVPFgqdGDFSWEDFVARVNS-----DlandlgnLASRT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 338 RTRV-----GTV-VPGDWTP-------KFAAALD------DDLSVPIALAEVHAARAVGNRALD---------SGDHE-- 387
Cdd:COG0143 391 LSMIhkyfdGKVpEPGELTEadeellaEAEAALEevaeamEAFEFRKALEEIMALARAANKYIDetapwklakDEDPErl 470
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123368663 388 -TAMTQA-RSIRA---------------MMGILGCDPLDERWES 414
Cdd:COG0143 471 aTVLYTLlEALRIlaillkpflpetaekILEQLGLEGDELTWED 514
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
47-304 |
2.28e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 49.60 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 47 VQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFirnVTDIDD---KILNKAADAGRPWWEWAATYERAFSAAYDALGVlpp 123
Cdd:pfam09334 10 ANGPPHLGHLYSYIPADIFARYLRLRGYDVLF---VCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKKFNI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 124 saEPRATGHITQMV------ELIERLIDRGHAYTGDGDVYFNVAT---LPD--------YGKLSGHRIDdvhQGEGVATg 186
Cdd:pfam09334 84 --SFDDYGRTTSERhhelvqEFFLKLYENGYIYEKEIEQFYCPSDerfLPDryvegtcpHCGSEDARGD---QCENCGR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 187 KRDQRDFTLWKGAKPGEPSWPTP-----------------W-GRGRPGWHTECVAMCEAYLGAEF-------DIHAGgmd 241
Cdd:pfam09334 158 HLEPTELINPKCVICGTTPEVKEtehyffdlskfqdklreWiEENNPEWPENVKNMVLEWLKEGLkdraisrDLDWG--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 242 LVFPHHENEI-------------AQAEAAGDG--FARFWL------------------H--------------------- 267
Cdd:pfam09334 235 IPVPGAEGKVfyvwldapigyisATKELSGNEekWKEWWPndpdtelvhfigkdiiyfHtifwpamllgagyrlpttvfa 314
|
330 340 350
....*....|....*....|....*....|....*..
gi 123368663 268 NGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYL 304
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYL 351
|
|
| metG |
TIGR00398 |
methionine--tRNA ligase; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ... |
269-337 |
2.45e-06 |
|
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: 50.07 E-value: 2.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123368663 269 GWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLgsahYRSM-----LEFSETALQDAVKA--YAGVEDFLHRV 337
Cdd:TIGR00398 319 GYLTVEGGKMSKSLGNVVDPSDLLARFGADILRYYL----LKERplgkdGDFSWEDFVERVNAdlANKLGNLLNRT 390
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
269-304 |
8.78e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 48.26 E-value: 8.78e-06
10 20 30
....*....|....*....|....*....|....*.
gi 123368663 269 GWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYL 304
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYL 326
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
268-317 |
2.05e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 47.17 E-value: 2.05e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 123368663 268 NGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELR-YYLGSAHYRSMLEFSE 317
Cdd:PRK12300 568 NGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRlYLTSSAELLQDADWRE 618
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
266-327 |
2.69e-04 |
|
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: 43.53 E-value: 2.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123368663 266 LHNGWVTMG-GEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAHYRSMLEFSETALQDAVKAY 327
Cdd:COG0060 591 LTHGFVLDEdGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVY 653
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
233-307 |
4.33e-04 |
|
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: 42.23 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123368663 233 FDIHAGGMDLVFPH------HENEIAQAEAAGDGFARFWLHNGWVTMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGS 306
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfNHKALFDEGLVTDEPPKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILF 304
|
.
gi 123368663 307 A 307
Cdd:cd00812 305 A 305
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
47-97 |
2.32e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 40.55 E-value: 2.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 123368663 47 VQGLPHIGHVRSGVAFDVLRRWLTAKGLDVAFirnVTDID---DKILNKAADAG 97
Cdd:PRK12267 15 PNGKPHIGHAYTTIAADALARYKRLQGYDVFF---LTGTDehgQKIQQAAEKAG 65
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
266-308 |
4.52e-03 |
|
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: 39.15 E-value: 4.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 123368663 266 LHNGWV-TMGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSAH 308
Cdd:cd00817 331 YLHGLVrDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAA 374
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
268-307 |
8.26e-03 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 38.64 E-value: 8.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 123368663 268 NGWVT-MGGEKMSKSLGNVLSIPAVLQRVRAAELRYYLGSA 307
Cdd:PRK13208 523 SGMVLdPDGKKMSKSKGNVVTPEELLEKYGADAVRYWAASA 563
|
|
| |
