|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
14-422 |
8.30e-132 |
|
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: 388.31 E-value: 8.30e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 14 NISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLKSRGDkYGKLVGVVP 93
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDVRSFPD-YGKLSGRNL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 94 -----GPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEI 168
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 169 AQCEVFHqCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQL 248
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 249 LALGSFLEDARAYMKGQLACGsvrevmlwERLASTRSAVKEALADDFDTPRVVDAILGLAHHGNGQLRAASkepgvprSP 328
Cdd:COG0215 316 ERLYNALRRLEEALGAADSSA--------EEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEGE-------DK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 329 AVFGAIISYFEQFFETVGISLGNQQCVSGDGSEATLRGVVEELVRFRQKVRQ---FALAkaeatgearrqqllerqplle 405
Cdd:COG0215 381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDELLDALIEALIEERAEARKakdFARA--------------------- 439
|
410
....*....|....*..
gi 1622884573 406 acDTLRQDLTAHGISIK 422
Cdd:COG0215 440 --DRIRDELAALGIVLE 454
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
20-421 |
2.73e-129 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 388.23 E-value: 2.73e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 20 LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYStAKGNVYFDLKS-RGDK--YGKLVgvvPGPV 96
Cdd:PTZ00399 128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLE---PESV 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 97 --------GEPA----DSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHH 164
Cdd:PTZ00399 204 adedriaeGEGAlgkvSGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 165 ENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHA 244
Cdd:PTZ00399 284 DNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEA 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 245 QQQLLALGSFLEDARAYMKgQLACGSVR-----EVMLWERLASTRSAVKEALADDFDTPRVVDAILGLAHHGNGQLRAAS 319
Cdd:PTZ00399 362 IEKDKVFFNFFANVKIKLR-ESELTSPQkwtqhDFELNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 320 KepgvPRSPAVFgAIISYFEQFFETVGISLGNQQCVSGD--GSEATLRGVVEELVRFRQKVRQFalAKAEATGEARRQQL 397
Cdd:PTZ00399 441 Q----PSAPLLR-SVAQYVTKILSIFGLVEGSDGLGSQGqnSTSENFKPLLEALLRFRDEVRDA--AKAEMKLISLDKKK 513
|
410 420
....*....|....*....|....*
gi 1622884573 398 lerQPLLEACDTLR-QDLTAHGISI 421
Cdd:PTZ00399 514 ---KQLLQLCDKLRdEWLPNLGIRI 535
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
14-245 |
1.33e-102 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 307.76 E-value: 1.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 14 NISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDlKSRGDKYGKLVGVVP 93
Cdd:pfam01406 69 GESFRQLAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFD-VSSFPDYGKLSGQNL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 94 GPV----GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIA 169
Cdd:pfam01406 148 EQLeagaRGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIA 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622884573 170 QCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQ 245
Cdd:pfam01406 228 QSEAAFD-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
14-405 |
2.09e-99 |
|
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: 305.46 E-value: 2.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 14 NISPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDLkSRGDKYGKLVG--- 90
Cdd:TIGR00435 81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDV-SKFKDYGKLSKqdl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 91 --VVPGPVGEPaDSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEI 168
Cdd:TIGR00435 160 dqLEAGARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 169 AQCEVFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQL 248
Cdd:TIGR00435 239 AQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNAL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 249 ----LALGSFLEDArAYMKGQLACGSVREVMLwerlastRSAVKEALADDFDTPRVVDAILGLAHHGNGQlraaskepgv 324
Cdd:TIGR00435 316 erlyKALRVLDTSL-AYSGNQSLNKFPDEKEF-------EARFVEAMDDDLNTANALAVLFELAKSINLT---------- 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 325 PRSPAVFGAIISYFEQFFETVGISLGNQQCVSGDGSEATLrGVVEELVRFRQKVRQfalAKAEATGEARRQQLLERQPLL 404
Cdd:TIGR00435 378 FVSKADAALLIEHLIFLESRLGLLLGLPSKPVQAGSNDDL-GEIEALIEERSIARK---EKDFAKADEIRDELAKKGIVL 453
|
.
gi 1622884573 405 E 405
Cdd:TIGR00435 454 E 454
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
8-421 |
7.44e-72 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 236.75 E-value: 7.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 8 LGQDwmnisPASLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTaKGNVYFDLKsRGDKYGK 87
Cdd:PLN02946 139 LGED-----PISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVD-KFPEYGK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 88 LVG--VVPGPVGE--PADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPH 163
Cdd:PLN02946 212 LSGrkLEDNRAGErvAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPH 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 164 HENEIAQ----CevfhqCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDS 239
Cdd:PLN02946 292 HENEIAQscaaC-----CDSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 240 AMLHAQQQLLALGSFLEDARAYMKGQ---LACGSVREVMLwERLASTRSAVKEALADDFDTPRVVDAILGLAHHGNGQLR 316
Cdd:PLN02946 365 QLESASERIFYIYQTLHDCEESLQQHdstFEKDSVPPDTL-NCINKFHDEFVTSMSDDLHTPVALAALSEPLKTINDLLH 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 317 AASKEPGVPRSPAvfgaiISYFEQFFETVGISLGnqqCVSGDGSEATlrgvveelvrfrQKVRQFALAKAEATGEARRQQ 396
Cdd:PLN02946 444 TRKGKKQEKRLES-----LAALEKKIRDVLSVLG---LMPTSYSEAL------------QQLREKALRRAKLTEEQVLQK 503
|
410 420 430
....*....|....*....|....*....|
gi 1622884573 397 LLERQPL-----LEACDTLRQDLTAHGISI 421
Cdd:PLN02946 504 IEERTVArknkeYEKSDAIRKDLAAVGIAL 533
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
13-237 |
1.29e-62 |
|
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: 202.04 E-value: 1.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 13 MNISPASLASLYEEDFKQDMAALKVLPPAVYLRVtenipqiisfiegiiarghaystakgnvyfdlksrgdkygklvgvv 92
Cdd:cd00672 79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 93 pgpvgepadsdkrhasdfalwkaakpqevfwaspwgpgrpgWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCE 172
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622884573 173 VFHQcEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 237
Cdd:cd00672 152 AATG-KPFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
20-312 |
6.97e-62 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 213.43 E-value: 6.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 20 LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYSTAKGNVYFDLKSRGdKYGKLVGVVPGPV--G 97
Cdd:PRK14535 314 LTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFA-AYGQLSGKSLDDLraG 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 98 EPADSD--KRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQ----- 170
Cdd:PRK14535 393 ERVEVDgfKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQsvgat 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 171 ---CEVFHQCEQWGN-------YFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSA 240
Cdd:PRK14535 473 ghtCGHHHAQTHHGQsiashvkYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDAH 550
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622884573 241 MLHAQQQLLALGSFLEDARAymkgqlacgsvREVMLWERLASTRSAVKEALADDFDTPRVVDAILGLAHHGN 312
Cdd:PRK14535 551 LDDAKGALTRLYTTLKNTPA-----------AEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVN 611
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
20-422 |
6.52e-55 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 190.13 E-value: 6.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 20 LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLKSRGDkYGKLVGVVPGPVGEP 99
Cdd:PRK14536 99 IAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPS-YGSLASAAVEDLQAG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 100 A----DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQCE 172
Cdd:PRK14536 177 AriehDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 173 VFhQCEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDFL-KTFSPDVFRFFCLRSSYRSAIDYSDSAMLHAQQQLLAL 251
Cdd:PRK14536 257 AA-TGKPWVRYWLHHEFLLM--NKGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKAARRSL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 252 GSFLedARAYMKGQLACGSVREVM---LWERLASTRSAVKE--------ALADDFDTPRVVDAILGLAhhgngqlraasK 320
Cdd:PRK14536 334 VRRV--ARVVDAARATTGSVRGTLaecAAERVAESRASESEllltdfraALEDDFSTPKALSELQKLV-----------K 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 321 EPGVPRspavfGAIISYFEQFFETVGISL--GNQQCVSGDGSEATLRGVVEELVRFRQKVRQ---FALAkaeatgearrq 395
Cdd:PRK14536 401 DTSVPP-----SLCLSVLQAMDTVLGLGLiqEATASLSAQVPAGPSEEEIGQLIEARAHARQtkdFPLA----------- 464
|
410 420
....*....|....*....|....*..
gi 1622884573 396 qllerqplleacDTLRQDLTAHGISIK 422
Cdd:PRK14536 465 ------------DEIRDKLKAEGIELE 479
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
9-326 |
2.66e-52 |
|
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: 181.46 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 9 GQDWMnispaSLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKGNVYFDLKSrGDKY 85
Cdd:TIGR03447 96 GVDWR-----ELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDA-TEQF 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 86 GKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGI 157
Cdd:TIGR03447 170 GYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 158 DLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRFFCLRSSYRSAIDY 236
Cdd:TIGR03447 250 DLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDW 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 237 SDSAMLHAQQQLlalgsfledarAYMKGQLACGSVREVmlwerlASTRSAVKEALADDFDTPRVVDAILGLAhhgNGQLR 316
Cdd:TIGR03447 328 TDAVLAEAEARL-----------ARWRAALALPDAPDA------TDLIARLRQHLANDLDTPAALAAVDGWA---ADALS 387
|
330
....*....|
gi 1622884573 317 AASKEPGVPR 326
Cdd:TIGR03447 388 YGGSDTEAPA 397
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
9-304 |
7.57e-51 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 176.66 E-value: 7.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 9 GQDWMNispasLASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAY---STAKGNVYFDLkSRGDKY 85
Cdd:PRK12418 69 GVDWRD-----LAEREIALFREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSV-DATPQF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 86 GKLVGVVPGPV--------GEPADSDKRHASDFALWKAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGI 157
Cdd:PRK12418 143 GYESGYDRATMlelfaergGDPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 158 DLAFPHHENEIAQCEVFHQCEQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKT-FSPDVFRFFCLRSSYRSAIDY 236
Cdd:PRK12418 223 DLIFPHHEFSAAHAEAATGERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREW 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622884573 237 SDSAMLHAQQQL------LALGSfLEDARAymkgqlacgsvrevmlwerlasTRSAVKEALADDFDTPRVVDAI 304
Cdd:PRK12418 301 TDAVLAEAEARLarwraaAALPA-GPDAAD----------------------VVARVRAALADDLDTPGALAAV 351
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
20-237 |
1.56e-40 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 151.16 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 20 LASLYEEDFKQDMAALKVLPPAVYLRVTENIPQIISFIEGIIARGHAYsTAKGNVYFDLkSRGDKYGKLVGVVPGPVGEP 99
Cdd:PRK14534 97 ISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMAGINLNDFKDM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 100 A------DSDKRHASDFALW---KAAKPQEVFWASPWGPGRPGWHIECSAIASMVFGSQLDIHSGGIDLAFPHHENEIAQ 170
Cdd:PRK14534 175 SvsrveiDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAI 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884573 171 CEVFHQcEQWGNYFLHSGHLHVkgKEEKMSKSLKNYITIKDF-LKTFSPDVFRFFCLRSSYRSAIDYS 237
Cdd:PRK14534 255 AECYLN-KKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFT 319
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
187-312 |
2.06e-09 |
|
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: 59.36 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 187 SGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR-SSYRSAIDYSDSAMLHAQQQLLA--LGSFLEdaRA--- 260
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLReVPFGQDGDFSWEDFVARVNSDLAndLGNLAS--RTlsm 393
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622884573 261 ---YMKGQLACGSVREVM---LWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGN 312
Cdd:COG0143 394 ihkYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAM-EAFEFRKALEEIMALARAAN 450
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
187-229 |
1.61e-07 |
|
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: 52.92 E-value: 1.61e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622884573 187 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS 229
Cdd:cd00814 271 HGYLTVEGK--KMSKSRGNVVDPDDLLERYGADALRYYLLRER 311
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
150-229 |
5.60e-07 |
|
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: 51.09 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 150 LDIHSGGIDLA--------FPHHeneiaqceVFHQCEQWGNY----FLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFS 217
Cdd:cd00812 225 VDIYIGGKEHApnhllysrFNHK--------ALFDEGLVTDEppkgLIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYG 294
|
90
....*....|..
gi 1622884573 218 PDVFRFFCLRSS 229
Cdd:cd00812 295 ADAARLYILFAA 306
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
187-239 |
6.16e-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: 6.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622884573 187 SGHLHVKGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSA-IDYSDS 239
Cdd:pfam09334 315 HGYLTYEGG--KMSKSRGNVVWPSEALDRFPPDALRYYLARNRPETKdTDFSWE 366
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
197-248 |
3.93e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.01 E-value: 3.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1622884573 197 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSS-YRSAIDYSDSAMLHAQQQL 248
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLYLTSSAeLLQDADWREKEVESVRRQL 628
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
187-322 |
4.13e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.91 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 187 SGHLHVKGkeEKMSKSlKNY-ITIKDFLKTFSPDVFRFFCL--RSSYRSAIDYSdsamLHAQQQ-----LLA-LGSFLed 257
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLRYYLAakLPETIDDLDFN----WEDFQQrvnseLVGkVVNFA-- 390
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884573 258 ARA------YMKGQLACGSVREVmLWERLASTRSAVKEALaDDFDTPRVVDAILGLAHHGNGQLraASKEP 322
Cdd:PRK00133 391 SRTagfinkRFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANKYV--DDNEP 457
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
193-304 |
1.17e-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: 44.69 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622884573 193 KGKeeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYSDSAMlhaQQQ-------------LLA-LGSFleDA 258
Cdd:COG0060 600 DGR--KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEIL---KEVrdvyrrlrntyrfLLAnLDDF--DP 672
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1622884573 259 RAYMkgqLACGSVREVMLW--ERLASTRSAVKEALaDDFDTPRVVDAI 304
Cdd:COG0060 673 AEDA---VPYEDLPELDRWilSRLNELIKEVTEAY-DNYDFHRAYRAL 716
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
183-227 |
1.39e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 1.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884573 183 YFLHsGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLR 227
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLR 328
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
178-225 |
3.70e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 43.13 E-value: 3.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1622884573 178 EQWGNYFLHSGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFC 225
Cdd:PLN02959 700 EHWPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATRFAL 745
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
194-237 |
1.15e-03 |
|
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: 41.24 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622884573 194 GKEEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAIDYS 237
Cdd:pfam00133 559 EQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
197-237 |
2.16e-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: 40.56 E-value: 2.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622884573 197 EKMSKSLKNYITIKDFLKTFSPDVFRFFCLRsSYRSAIDYS 237
Cdd:COG1384 286 EKISKSKGNGLTVEEWLEYAEPESLRYFMFR-KPKKAKDLD 325
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
191-235 |
2.77e-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: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884573 191 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRSSYRSAID 235
Cdd:pfam01921 273 LLKGGG-KMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
133-203 |
4.07e-03 |
|
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: 37.46 E-value: 4.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622884573 133 GWHIECSAIASMVFGSQLDIHSGGIDLAFpHHENEIAQCEVFHQceQWGNYFLHSGHLHVKGKeEKMSKSL 203
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAGG--PARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
191-228 |
6.45e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 38.46 E-value: 6.45e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1622884573 191 HVKGKEeKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 228
Cdd:cd00674 269 GLKGGG-KMSSSKGNVITPSDWLEVAPPEVLRYLYARR 305
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
184-228 |
8.59e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 38.63 E-value: 8.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1622884573 184 FLHsGHLHVKGkeEKMSKSLKNYITIKDFLKTFSPDVFRFFCLRS 228
Cdd:PRK12267 288 FAH-GWWLMKD--GKMSKSKGNVVDPEELVDRYGLDALRYYLLRE 329
|
|
| |
