|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
5-528 |
0e+00 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 746.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 5 AKPTPQLELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKII 84
Cdd:PLN02946 54 ASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKII 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 85 KRANEAGETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEGDVYFSVDTFPEYLSLS 164
Cdd:PLN02946 134 ARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVDGDVYFSVDKFPEYGKLS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 165 GRKLDHNLAGSRVAVDTRKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHE 244
Cdd:PLN02946 214 GRKLEDNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 245 NELAQSRAAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEIASDRV 324
Cdd:PLN02946 294 NEIAQSCAACCDSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESASERI 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 325 YYIYQTLYDCEEVLSQYRGENISVPVPVEEQDMVNKHHSEFLESMADDLRTTDVLDGFTDLLKAINSNLNdfkklqqkle 404
Cdd:PLN02946 374 FYIYQTLHDCEESLQQHDSTFEKDSVPPDTLNCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLH---------- 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 405 qqkkkqqqqkqqkqkqQQAQKQPEEYIQAMFALETEIKNKISILGLMPPsSLAEALKQLKDKALKRAGLTEELLQEQIEQ 484
Cdd:PLN02946 444 ----------------TRKGKKQEKRLESLAALEKKIRDVLSVLGLMPT-SYSEALQQLREKALRRAKLTEEQVLQKIEE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1002256975 485 RTAARKNKQFDVSDQIRKQLGSKGIALMDEPTGTVWRPCEPESE 528
Cdd:PLN02946 507 RTVARKNKEYEKSDAIRKDLAAVGIALMDSPDGTTWRPAIPLAL 550
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
11-521 |
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: 685.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 11 LELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEA 90
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 91 GETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEGDVYFSVDTFPEYLSLSGRKLDH 170
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEADGDVYFDVRSFPDYGKLSGRNLDD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 171 NLAGSRVAVDTRKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENELAQS 250
Cdd:COG0215 162 LRAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 251 RAAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEIASDRVYYIYQT 330
Cdd:COG0215 242 EAATGKPFARYWMHNGFLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALERLYNA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 331 LYDCEEVLSQyrgenisvpvPVEEQDMVNKHHSEFLESMADDLRTTDVLDGFTDLLKAINSNLNDfkklqqkleqqkkkq 410
Cdd:COG0215 322 LRRLEEALGA----------ADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDE--------------- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 411 qqqkqqkqkqQQAQKQPEEYIQAMFALEteiknkiSILGLMPPSSLAEalkqlkdKALKRAGLTEELLQEQIEQRTAARK 490
Cdd:COG0215 377 ----------GEDKAALAALAALLRALG-------GVLGLLLLEPEAW-------QGAAEDELLDALIEALIEERAEARK 432
|
490 500 510
....*....|....*....|....*....|.
gi 1002256975 491 NKQFDVSDQIRKQLGSKGIALMDEPTGTVWR 521
Cdd:COG0215 433 AKDFARADRIRDELAALGIVLEDTPDGTTWR 463
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
11-521 |
0e+00 |
|
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: 518.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 11 LELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEA 90
Cdd:TIGR00435 1 LKLYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRAREN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 91 GETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAME-GDVYFSVDTFPEYLSLSGRKLD 169
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDnGDVYFDVSKFKDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 170 HNLAGSRVAVDTRKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENELAQ 249
Cdd:TIGR00435 161 QLEAGARVDVDEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 250 SRAAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEIASDRVYYIYQ 329
Cdd:TIGR00435 241 SEAAFGKQLAKYWMHNGFLMIDNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALERLYK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 330 TLYDCEEVLSqYRGENISVPVPVEEQdmvnkHHSEFLESMADDLRTTDVLDGFTDLLKAINSNLNDfkklqqkleqqkkk 409
Cdd:TIGR00435 321 ALRVLDTSLA-YSGNQSLNKFPDEKE-----FEARFVEAMDDDLNTANALAVLFELAKSINLTFVS-------------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 410 qqqqkqqkqkqqqaqkqpeeyIQAMFALETEIKNKISILGLMppssLAEALKQLKDKALKRAGLTEELlqeqIEQRTAAR 489
Cdd:TIGR00435 381 ---------------------KADAALLIEHLIFLESRLGLL----LGLPSKPVQAGSNDDLGEIEAL----IEERSIAR 431
|
490 500 510
....*....|....*....|....*....|..
gi 1002256975 490 KNKQFDVSDQIRKQLGSKGIALMDEPTGTVWR 521
Cdd:TIGR00435 432 KEKDFAKADEIRDELAKKGIVLEDTPQGTTWR 463
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
23-320 |
2.69e-161 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 460.30 E-value: 2.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 23 LFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEAGETVTSLSSRFI 102
Cdd:pfam01406 1 FFVPLHQGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 103 NEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAME-GDVYFSVDTFPEYLSLSGRKLDHNLAGSRVAVDT 181
Cdd:pfam01406 81 EAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDnGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 182 RKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENELAQSRAAYPESEVKC 261
Cdd:pfam01406 161 GKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDKQLANY 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256975 262 WMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEIA 320
Cdd:pfam01406 241 WLHNGHVMIDGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQA 299
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
11-526 |
2.26e-125 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 380.91 E-value: 2.26e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 11 LELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLK-FLGYEVEYVRNFTDIDDKIIKRANE 89
Cdd:PTZ00399 40 LKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEdYFGYDVFYVMNITDIDDKIIKRARE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 90 AG-ETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEGDVYFSVDTF----------- 157
Cdd:PTZ00399 120 EKlSIFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYESNGSVYFDVEAFrkaghvypkle 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 158 PEYLSLSGRKLDHNlaGSRVAVDTRKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKD 237
Cdd:PTZ00399 200 PESVADEDRIAEGE--GALGKVSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGID 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 238 LIFPHHENELAQSRAAYPESE-VKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKA 316
Cdd:PTZ00399 278 LKFPHHDNELAQSEAYFDKHQwVNYFLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDES 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 317 LE--IASDRVYY-IYQTlydceeVLSQYRGENISVPVPVEEQDM-VNKHHSEFL----ESMADDLRTTDVLDGFTDLLKA 388
Cdd:PTZ00399 358 MDeaIEKDKVFFnFFAN------VKIKLRESELTSPQKWTQHDFeLNELFEETKsavhAALLDNFDTPEALQALQKLISA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 389 INSNLNdfkklqqkleqqkkkqqqqkqqkqkqqqaqkqPEEYIQAmfALETEIKNKI----SILGLMPPSSLAEALKQlK 464
Cdd:PTZ00399 432 TNTYLN--------------------------------SGEQPSA--PLLRSVAQYVtkilSIFGLVEGSDGLGSQGQ-N 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002256975 465 DKALKRAGLTEELLQEQIEQRTAARKNKQFDV-----------SDQIR-KQLGSKGIALMDEPTG-TVWRPCEPE 526
Cdd:PTZ00399 477 STSENFKPLLEALLRFRDEVRDAAKAEMKLISldkkkkqllqlCDKLRdEWLPNLGIRIEDKPDGpSVWKLDDKE 551
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
9-521 |
8.05e-122 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 373.28 E-value: 8.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 9 PQLELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRAN 88
Cdd:PRK14535 226 PMTTIYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 89 EAGETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAY-AMEGDVYFSVDTFPEYLSLSGRK 167
Cdd:PRK14535 306 ENGETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYpAANGDVYYAVREFAAYGQLSGKS 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 168 LDHNLAGSRVAVDTRKRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENEL 247
Cdd:PRK14535 386 LDDLRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEI 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 248 AQSRAAYPE----------------SEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVN 311
Cdd:PRK14535 466 AQSVGATGHtcghhhaqthhgqsiaSHVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 312 HSDKALEIASDRVYYIYQTLYDceevlsqyrgeniSVPVPVEEQDMVNKHHSEFLESMADDLRTTDVLDGFTDLLKAINS 391
Cdd:PRK14535 546 YSDAHLDDAKGALTRLYTTLKN-------------TPAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNK 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 392 NlNDFKklqqkleqqkkkqqqqkqqkqkqqqaqkqpeeyiqamfaLETEIKNKISILGLMP--PSSLAEAlkqlkdkALK 469
Cdd:PRK14535 613 T-NDAQ---------------------------------------LAGCLKALGGIIGLLQrdPTEFLQG-------GAA 645
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002256975 470 RAGLTEELLQEQIEQRTAARKNKQFDVSDQIRKQLGSKGIALMDEPTGTVWR 521
Cdd:PRK14535 646 SDGLSNEEIEDLIARRKQARADKNWAESDRIRDLLNEHKIILEDNAGGTTWR 697
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
11-521 |
8.34e-120 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 361.55 E-value: 8.34e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 11 LELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDI----------D 80
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 81 DKIIKRANEAGETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEGDVYFSVDTFPEY 160
Cdd:PRK14536 83 DKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGNVYFDIRTFPSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 161 LSLSGRKLDHNLAGSRVAVDTRKRNPADFALWKAAKEGEP---FWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKD 237
Cdd:PRK14536 163 GSLASAAVEDLQAGARIEHDTNKRNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 238 LIFPHHENELAQSRAAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDL-YHPMALRFFLMRTHYRGDVNHSDKA 316
Cdd:PRK14536 243 HIRVHHTNEIAQCEAATGKPWVRYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQLAFSWEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 317 LEIAS-------DRVYYIYQTLYDCEEVLSQYRGENISVPVPVEEQDMVNKHHSEFLESMADDLRTTDVLDGFTDLLKai 389
Cdd:PRK14536 323 LKTAKaarrslvRRVARVVDAARATTGSVRGTLAECAAERVAESRASESELLLTDFRAALEDDFSTPKALSELQKLVK-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 390 nsnlndfkklqqkleqqkkkqqqqkqqkqkqqQAQKQPEEYIQAMFALETeiknkisILGLmppSSLAEALKQLKDKAlk 469
Cdd:PRK14536 401 --------------------------------DTSVPPSLCLSVLQAMDT-------VLGL---GLIQEATASLSAQV-- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002256975 470 RAGLTEELLQEQIEQRTAARKNKQFDVSDQIRKQLGSKGIALMDEPTGTVWR 521
Cdd:PRK14536 437 PAGPSEEEIGQLIEARAHARQTKDFPLADEIRDKLKAEGIELEDTHLGTIWK 488
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
12-313 |
6.27e-109 |
|
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: 323.38 E-value: 6.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 12 ELFNSMTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEAG 91
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 92 ETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVtdhiehiielitkimengkayamegdvyfsvdtfpeylslsgrkldhn 171
Cdd:cd00672 81 LSWKEVADYYTKEFFEDMKALNVLPPDVVPRV------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 172 lagsrvavdtrkrnpadfalwkaakegepfwdspwgrgrpgWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENELAQSR 251
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256975 252 AAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHS 313
Cdd:cd00672 152 AATGKPFARYWLHTGHLTIDGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
9-380 |
2.65e-96 |
|
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: 298.18 E-value: 2.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 9 PQLELFNSMTKKKELFEPLVEgkVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRAN 88
Cdd:TIGR03447 16 PPLRLFDTADGQVRPVEPGPE--AGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 89 EAGETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEG----DVYFSVDTFPEYLSLS 164
Cdd:TIGR03447 94 RDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGpeypDVYFSIDATEQFGYES 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 165 G--RKLDHNLAGSRVAVDTR--KRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIF 240
Cdd:TIGR03447 174 GydRATMLELFAERGGDPDRpgKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 241 PHHENELAQSRAAYPESEV-KCWMHNGFVNKDDQKMSKSDKNF-FTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALE 318
Cdd:TIGR03447 254 PHHEFSAAHAEAATGVRRMaRHYVHAGMIGLDGEKMSKSLGNLvFVSKLRAAGVDPAAIRLGLLAGHYRQDRDWTDAVLA 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002256975 319 IASDRvyyiyqtlydceevLSQYRGENISVPVPvEEQDMVNKHHSEflesMADDLRTTDVLD 380
Cdd:TIGR03447 334 EAEAR--------------LARWRAALALPDAP-DATDLIARLRQH----LANDLDTPAALA 376
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
30-375 |
3.86e-94 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 291.83 E-value: 3.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 30 GKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEAGETVTSLSSRFINEFLLDM 109
Cdd:PRK12418 8 GTATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 110 AQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEG----DVYFSVDTFPEYLSLSGrkLDHN----LAGSRVAVDT 181
Cdd:PRK12418 88 EALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDeeypDVYFSVDATPQFGYESG--YDRAtmleLFAERGGDPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 182 R--KRNPADFALWKAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGGKDLIFPHHENELAQSRAAYPESE- 258
Cdd:PRK12418 166 RpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRf 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 259 VKCWMHNGFVNKDDQKMSKSDKNF-FTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEIASDRvyyiyqtlydceev 337
Cdd:PRK12418 246 ARHYVHAGMIGLDGEKMSKSRGNLvFVSRLRAAGVDPAAIRLALLAGHYRADREWTDAVLAEAEAR-------------- 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002256975 338 LSQYRgENISVPVPVEEQDMVnkhhSEFLESMADDLRT 375
Cdd:PRK12418 312 LARWR-AAAALPAGPDAADVV----ARVRAALADDLDT 344
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
11-518 |
1.90e-67 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 225.12 E-value: 1.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 11 LELFNsmTKKKELFEPLVEGKVRMYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDI----------D 80
Cdd:PRK14534 3 LKLYN--TKTKDLSELKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 81 DKIIKRANEAGETVTSLSSRFINEFLLDMAQLQCLPPTCEPRVTDHIEHIIELITKIMENGKAYAMEGDVYFSVDTFPEY 160
Cdd:PRK14534 81 DKVVKAARERGLTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGNVYFDTSCFKSY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 161 LSLSGRKLD--HNLAGSRVAVDTRKRNPADFALW---KAAKEGEPFWDSPWGRGRPGWHIECSAMSAHYLGHVFDIHGGG 235
Cdd:PRK14534 161 GQMAGINLNdfKDMSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 236 KDLIFPHHENELAQSRAAYPESEVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDL-YHPMALRFFLMRTHYRGDVN--- 311
Cdd:PRK14534 241 VDHIGVHHINEIAIAECYLNKKWCDMFVHGEFLIMEYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKftf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 312 HSDKALEIASD----RVYYIYQTLYDCEEVLSQYRGENIsvpvpveEQDMVNKHHSEFLESMADDLRTTDVLDGFTDLLK 387
Cdd:PRK14534 321 NNLKACKIAREnmlnKLTYFYSSLDQFDLNLLNKDLENI-------EFSLEKEYYDSFLEKIAFDLNIPQGLALLWDIIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 388 AINsnlndfkklqqkleqqkkkqqqqkqqkqkqqqaqkqpeeyIQAMFALETEIK-NKISILGLMppsslAEALKQLKDK 466
Cdd:PRK14534 394 DDN----------------------------------------LSFLSKLRLAFKfDEVLSLGLR-----EEILREIENH 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1002256975 467 ALkragLTEELLQEQIEQRTAARKNKQFDVSDQIRKQLGSKGIALMDEPTGT 518
Cdd:PRK14534 429 RI----VIDDNMKSLIEERRLAKCEKDFKRADEIREYFASKGFVLIDTEEGT 476
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
34-279 |
9.98e-19 |
|
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: 82.91 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 34 MYVCGVTPYDFSHIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEAGEtvtslssrfineflldmaqlq 113
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGE--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 114 clpptCEPRVTDH-IEHIIELItkimengkayamegdvyfsvdtfpeylslsgrkldhnlagsrvavdtrkrnpadfalw 192
Cdd:cd00802 60 -----NAKAFVERwIERIKEDV---------------------------------------------------------- 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 193 kaakegepfwdspwgrgrpGWHIECSAMSAHYLGHVFDIHGGGKDLIFpHHENELAQSRAAYPEsEVKCWMHNGFVNKDD 272
Cdd:cd00802 77 -------------------EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGGP-ARPFGLTFGRVMGAD 135
|
....*...
gi 1002256975 273 -QKMSKSD 279
Cdd:cd00802 136 gTKMSKSK 143
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
428-521 |
5.29e-15 |
|
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: 72.59 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 428 EEYIQAM-------------FALETEIkNKISILGLMPPSSLAEALKQLKD--------------KALKRAGLTEELLQE 480
Cdd:cd07963 36 ERFIAAMdddfntpealavlFELAREI-NRLKKEDIEKAAALAALLKALGGvlgllqqdpeaflqGGTGEGGLSVAEIEA 114
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1002256975 481 QIEQRTAARKNKQFDVSDQIRKQLGSKGIALMDEPTGTVWR 521
Cdd:cd07963 115 LIAQRNQARKAKDWAEADRIRDELAAQGIILEDSPEGTTWR 155
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
46-303 |
1.52e-08 |
|
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: 56.39 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYVrnfTDIDD---KIIKRANEAGETVTSLSSRFINEFLLDMAQLQ-------Cl 115
Cdd:cd00814 16 HLGHLYGTVLADVFARYQRLRGYDVLFV---TGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNisfdyfiR- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 116 ppTCEPRvtdHIEHIIELITKIMENGKAYAMEGDVYFSV--DTF-PE-------YLSLSgrKLDHNLagsrvaVDTRKRN 185
Cdd:cd00814 92 --TTSPR---HKEIVQEFFKKLYENGYIYEGEYEGLYCVscERFlPEwreeehyFFRLS--KFQDRL------LEWLEKN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 186 PAdfALWKAA---------KEGEPFWD-----SPWG-------------------------------RGRPGWHIEcsam 220
Cdd:cd00814 159 PD--FIWPENarnevlswlKEGLKDLSitrdlFDWGipvpldpgkviyvwfdaligyisatgyyneeWGNSWWWKD---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 221 sahylGHVFDIHGGGKDlIFPHHE-----NELAqsrAAYPEseVKCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPM 295
Cdd:cd00814 233 -----GWPELVHFIGKD-IIRFHAiywpaMLLG---AGLPL--PTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGAD 301
|
....*...
gi 1002256975 296 ALRFFLMR 303
Cdd:cd00814 302 ALRYYLLR 309
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
46-302 |
1.90e-08 |
|
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: 56.10 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYVRNFTDIDDKIIKRANEAGETVTSLSSRFINEFLLDMAQL------QCLPPTC 119
Cdd:cd00812 16 HVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMgfsydwRREFTTC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 120 EPRVTDHIEHiieLITKIMENGKAYAMEGDVYFSVDT---FPEYLSLSGRKLDHN-LAGSRVAVDTRK---RNPADFA-- 190
Cdd:cd00812 96 DPEYYKFTQW---LFLKLYEKGLAYKKEAPVNWCKLLdqwFLKYSETEWKEKLLKdLEKLDGWPEEVRamqENWIGCSrq 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 191 -LWkaakeGEPFwdsPWGrgrpgWHIECSAMS---------AHYLGHV-----------------FDIHGGGKDLIFPHh 243
Cdd:cd00812 173 rYW-----GTPI---PWT-----DTMESLSDStwyyarytdAHNLEQPyegdlefdreefeywypVDIYIGGKEHAPNH- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002256975 244 eneLAQSR----AAYPESEV-----KCWMHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLM 302
Cdd:cd00812 239 ---LLYSRfnhkALFDEGLVtdeppKGLIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYIL 303
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
46-309 |
2.25e-08 |
|
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: 55.89 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYVRNfTD--------------IDDKIIKRANEAGETVTSLSSRFINEFLLDMAQ 111
Cdd:cd00668 16 HLGHALTHIIADFIARYKRMRGYEVPFLPG-WDthglpielkaerkgGRKKKTIWIEEFREDPKEFVEEMSGEHKEDFRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 112 LQCLPPTCEPRVTDHIEHI--IELITKIM-ENGKAYAMEGDVYFSVDTFPEYLSLSGRKLDHNLAGSRVAVDTRKRNPAD 188
Cdd:cd00668 95 LGISYDWSDEYITTEPEYSkaVELIFSRLyEKGLIYRGTHPVRITEQWFFDMPKFKEKLLKALRRGKIVPEHVKNRMEAW 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 189 FAL---WKAAKegepfwDSPWGRGRPGWHIE----CSAMSAHYLGHVF-----------DIHGGGKDLIFPHHENELAQS 250
Cdd:cd00668 175 LESlldWAISR------QRYWGTPLPEDVFDvwfdSGIGPLGSLGYPEekewfkdsypaDWHLIGKDILRGWANFWITML 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 251 RAAYPESEVKCWMHNGFV-NKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGD 309
Cdd:cd00668 249 VALFGEIPPKNLLVHGFVlDEGGQKMSKSKGNVIDPSDVVEKYGADALRYYLTSLAPYGD 308
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
265-303 |
3.82e-08 |
|
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: 55.89 E-value: 3.82e-08
10 20 30
....*....|....*....|....*....|....*....
gi 1002256975 265 NGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMR 303
Cdd:COG0143 318 HGFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLLR 356
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
235-330 |
1.01e-06 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 51.79 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 235 GKDLI--------FpHHenelaqsRAAYPEsevKCW----MHNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLM 302
Cdd:PRK12300 537 GKDLIpnhltffiF-NH-------VAIFPE---EKWprgiVVNGFVLLEGKKMSKSKGNVIPLRKAIEEYGADVVRLYLT 605
|
90 100
....*....|....*....|....*....
gi 1002256975 303 RT-HYRGDVNHSDKALEIASDRVYYIYQT 330
Cdd:PRK12300 606 SSaELLQDADWREKEVESVRRQLERFYEL 634
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
46-155 |
5.11e-06 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 49.11 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYVrnfTDIDD---KIIKRANEAGETVTSLSSRFINEFLLDMAQLQC-----LPP 117
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNIsyddfIRT 93
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1002256975 118 TcEPRvtdHIEHIIELITKIMENGKAY--AMEGdvYFSVD 155
Cdd:PRK11893 94 T-DPR---HKEAVQEIFQRLLANGDIYlgKYEG--WYCVR 127
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
265-303 |
9.07e-06 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 48.06 E-value: 9.07e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1002256975 265 NGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMR 303
Cdd:pfam09334 315 HGYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLAR 353
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
229-301 |
1.89e-05 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 47.76 E-value: 1.89e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002256975 229 FDIHGGGKDLIFPHHENELAQSRAAYPESE----VKCwmhNGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFL 301
Cdd:PLN02959 672 FDLRVSGKDLIQNHLTFAIYNHTAIWAEEHwprgFRC---NGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
46-160 |
3.55e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 46.33 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYVrnfTDID---DKIIKRANEAGET----VTSLSSRFIN----------EFLld 108
Cdd:PRK12267 20 HIGHAYTTIAADALARYKRLQGYDVFFL---TGTDehgQKIQQAAEKAGKTpqeyVDEISAGFKElwkkldisydKFI-- 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1002256975 109 maqlqclpptcepRVTD--HIEHIIELITKIMENgkayameGDVYFSvdtfpEY 160
Cdd:PRK12267 95 -------------RTTDerHKKVVQKIFEKLYEQ-------GDIYKG-----EY 123
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
265-332 |
5.63e-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: 42.76 E-value: 5.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002256975 265 NGFVN-KDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHSDKALEiasdRVYYIYQTLY 332
Cdd:COG0060 593 HGFVLdEDGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILK----EVRDVYRRLR 657
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
265-313 |
7.65e-04 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 42.01 E-value: 7.65e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1002256975 265 NGFVNKDD-QKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGDVNHS 313
Cdd:pfam00133 553 HGLVRDEQgRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
267-304 |
2.83e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 39.94 E-value: 2.83e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1002256975 267 FVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRT 304
Cdd:pfam01921 272 ILLKGGGKMSSSKGNVITPEDWLEYAPPESLRFLMFRT 309
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
263-309 |
3.50e-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: 39.92 E-value: 3.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1002256975 263 MHNGFV-NKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMRTHYRGD 309
Cdd:cd00817 331 YLHGLVrDEDGRKMSKSLGNVIDPLDVIDGYGADALRFTLASAATQGR 378
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
265-302 |
3.70e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 40.14 E-value: 3.70e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1002256975 265 NGFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLM 302
Cdd:PRK00133 320 HGFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYLA 357
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
273-303 |
4.52e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 39.79 E-value: 4.52e-03
10 20 30
....*....|....*....|....*....|.
gi 1002256975 273 QKMSKSDKNFFTIRDIIDLYHPMALRFFLMR 303
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR 316
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
46-73 |
5.09e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 39.75 E-value: 5.09e-03
10 20
....*....|....*....|....*...
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEYV 73
Cdd:PRK00133 18 HLGHLVEYIQADIWVRYQRMRGHEVLFV 45
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
46-81 |
5.99e-03 |
|
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: 38.31 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1002256975 46 HIGHARAYVAFDVLYRYLKFLGYEVEyVRNFtdIDD 81
Cdd:cd00671 16 HVGHLRNAIIGDSLARILEFLGYDVT-REYY--IND 48
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
266-303 |
9.22e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 9.22e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1002256975 266 GFVNKDDQKMSKSDKNFFTIRDIIDLYHPMALRFFLMR 303
Cdd:PRK12267 291 GWWLMKDGKMSKSKGNVVDPEELVDRYGLDALRYYLLR 328
|
|
| |
