|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
48-543 |
1.87e-161 |
|
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: 468.04 E-value: 1.87e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRD-YFKINLVtaMNITDVDDKIIKRAQ 126
Cdd:COG0215 2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYlGYKVTYV--RNITDVDDKIIKRAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 127 LAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNYGKL--QN 204
Cdd:COG0215 80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLsgRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 205 LglseDKL--------DPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFP 276
Cdd:COG0215 159 L----DDLragarvevDEEKRDPLDFALWKAAKPG-EPSWDSPWG-RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 277 HHENEEAQCCARYKtDQWVNYWVHTGqlHMVGDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMV 356
Cdd:COG0215 233 HHENEIAQSEAATG-KPFARYWMHNG--FLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 357 TARQTLQRFRNFQADLSAYTQflkpvhllDEGALKAQLTHTVTEFDNCLRDDFDTARAISVLIDQMSSISRCINEQqvDA 436
Cdd:COG0215 310 EAEKALERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEG--ED 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 437 QEEPAYCIDLLLAAGNFinraivtFGLselqDKESLQEKVSFTDHSIDPNlLVNDVINVRGRMRER---ATSgnvknpql 513
Cdd:COG0215 380 KAALAALAALLRALGGV-------LGL----LLLEPEAWQGAAEDELLDA-LIEALIEERAEARKAkdfARA-------- 439
|
490 500 510
....*....|....*....|....*....|
gi 19922218 514 laacDELRSLLQQHGIQVRDHKQGSSWVFA 543
Cdd:COG0215 440 ----DRIRDELAALGIVLEDTPDGTTWRRK 465
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
23-552 |
9.88e-157 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 462.58 E-value: 9.88e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 23 RNISEEAPKQDSPF-KWRKPIGQ---HTGINIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQR 98
Cdd:PTZ00399 11 AGLNGTGQVSKSRLpEWKKPSKEgkyLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 99 ILRDYFKINLVTAMNITDVDDKIIKRAQLAGLD-WQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLID 177
Cdd:PTZ00399 91 ILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSiFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIID 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 178 GKQAYVTpDNSVYFDVSKSK----NYGKL--------QNLGLSEDKLDPI---KRNTADFALWKARKSGsEPTWAAPWgG 242
Cdd:PTZ00399 171 NGFAYES-NGSVYFDVEAFRkaghVYPKLepesvadeDRIAEGEGALGKVsgeKRSPNDFALWKASKPG-EPSWDSPW-G 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 243 EGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTDQWVNYWVHTGQLHMVGDreKMSKSLGNTIS 322
Cdd:PTZ00399 248 KGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL--KMSKSLKNFIT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 323 VSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQRFRNFQADLSAY--TQFLKPVHLLDEG--ALKAQLTHTV 398
Cdd:PTZ00399 326 IRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKlrESELTSPQKWTQHdfELNELFEETK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 399 TEFDNCLRDDFDTARAISVLIDQMSSISRCINE-QQVDAqeepayciDLLLAAGNFINRAIVTFGLSELQDKESLQEKVS 477
Cdd:PTZ00399 406 SAVHAALLDNFDTPEALQALQKLISATNTYLNSgEQPSA--------PLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 478 fTDHSIDPnlLVNDVINVRGRMRERATSGNV------KNPQLLAACDELRS-LLQQHGIQVRDHKQGSSWVfavsceKQD 550
Cdd:PTZ00399 478 -TSENFKP--LLEALLRFRDEVRDAAKAEMKlisldkKKKQLLQLCDKLRDeWLPNLGIRIEDKPDGPSVW------KLD 548
|
..
gi 19922218 551 DK 552
Cdd:PTZ00399 549 DK 550
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
50-540 |
1.54e-130 |
|
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: 389.05 E-value: 1.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 50 IYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAG 129
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 130 LDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE 209
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 210 ------DKLDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEA 283
Cdd:TIGR00435 162 leagarVDVDEAKRNKLDFVLWKSSKEG-EPKWDSPWG-KGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 284 QCCARYKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQ 363
Cdd:TIGR00435 240 QSEAAFGK-QLAKYWMHNGFLMI--DNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 364 RFRNfqaDLSAYTQFLKPVHLLDEGALKAQLTHTVtEFDNCLRDDFDTARAISVLIDQMSSISRcineqqvdaqeepaYC 443
Cdd:TIGR00435 317 RLYK---ALRVLDTSLAYSGNQSLNKFPDEKEFEA-RFVEAMDDDLNTANALAVLFELAKSINL--------------TF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 444 IDLLLAAGNFINraivtfgLSELQDKESLQEKVSFTDHSIDPNLLVN---DVINVRGRMRERatsgnvKNpqlLAACDEL 520
Cdd:TIGR00435 379 VSKADAALLIEH-------LIFLESRLGLLLGLPSKPVQAGSNDDLGeieALIEERSIARKE------KD---FAKADEI 442
|
490 500
....*....|....*....|
gi 19922218 521 RSLLQQHGIQVRDHKQGSSW 540
Cdd:TIGR00435 443 RDELAKKGIVLEDTPQGTTW 462
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
66-359 |
8.99e-121 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 357.83 E-value: 8.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 66 PQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQ 145
Cdd:pfam01406 7 QGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 146 DMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE------DKLDPIKRNT 219
Cdd:pfam01406 86 DMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQleagarGEVSEGKRDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 220 ADFALWKARKSGsEPTWAAPWgGEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTdQWVNYWV 299
Cdd:pfam01406 166 LDFALWKASKEG-EPSWDSPW-GKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDK-QLANYWL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 300 HTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTAR 359
Cdd:pfam01406 243 HNGHVMI--DGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
49-351 |
3.40e-106 |
|
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: 317.21 E-value: 3.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 49 NIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDYFkINLVTAMNITDVDDKIIKRAQLA 128
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 129 GLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVtttmpviiqfiqqlidgkqayvtpdnsvyfdvsksknygklqnlgls 208
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 209 edkldpikrntadfalwkarksgseptwaapwggegrpgWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCAR 288
Cdd:cd00672 113 ---------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAA 153
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922218 289 YKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYS 351
Cdd:cd00672 154 TGK-PFARYWLHTGHLTI--DGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
41-555 |
6.06e-93 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 295.30 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 41 PIGQHTGINIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVTamNITDVDD 119
Cdd:PLN02946 53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLgYEVRYVR--NFTDVDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 120 KIIKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNY 199
Cdd:PLN02946 131 KIIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVDKFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 200 GKLQNLGLSEDK------LDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDL 273
Cdd:PLN02946 210 GKLSGRKLEDNRagervaVDSRKKNPADFALWKAAKEG-EPFWDSPWG-PGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 274 RFPHHENEEAQCCARYKtDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQ 353
Cdd:PLN02946 288 VFPHHENEIAQSCAACC-DSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 354 LMVTAR-------QTLQRFRN-FQADLSAYTQFLKPVHLLDEgalkaqLTHTVTEFDNCLRDDFDTARAISVLIDQMSSI 425
Cdd:PLN02946 365 QLESASerifyiyQTLHDCEEsLQQHDSTFEKDSVPPDTLNC------INKFHDEFVTSMSDDLHTPVALAALSEPLKTI 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 426 SRCINEQQVDAQEEPaycIDLLLAAGNFINRAIVTFGLSELQDKESLQEkvsFTDHSIDPNLLVNDviNVRGRMRERATS 505
Cdd:PLN02946 439 NDLLHTRKGKKQEKR---LESLAALEKKIRDVLSVLGLMPTSYSEALQQ---LREKALRRAKLTEE--QVLQKIEERTVA 510
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 19922218 506 GNVKNPQllaACDELRSLLQQHGIQVRDHKQGSSWVFAVSCEKQDDKSKS 555
Cdd:PLN02946 511 RKNKEYE---KSDAIRKDLAAVGIALMDSPDGTTWRPAIPLALQEQVAAT 557
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
69-418 |
6.15e-79 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 253.31 E-value: 6.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 69 VTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVtaMNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQDM 147
Cdd:PRK12418 10 ATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAgHDVHYV--QNVTDVDDPLLERAARDGVDWRDLAEREIALFREDM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 148 LRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNS---VYFDVSKSKNYGKLQNLGLSE----------DKLDP 214
Cdd:PRK12418 88 EALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEypdVYFSVDATPQFGYESGYDRATmlelfaerggDPDRP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 215 IKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTDQW 294
Cdd:PRK12418 168 GKRDPLDALLWRAARPG-EPSWPSPFG-PGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 295 VNYWVHTGqlhMVG-DREKMSKSLGNTISVSELlkkyTADEF-----RMACLLSNYRNAMPYSDQLMVTARQTLQRFRNF 368
Cdd:PRK12418 246 ARHYVHAG---MIGlDGEKMSKSRGNLVFVSRL----RAAGVdpaaiRLALLAGHYRADREWTDAVLAEAEARLARWRAA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 19922218 369 QAdlsaytqflkpvhlLDEGALKAQLTHTVTEFdncLRDDFDTARAISVL 418
Cdd:PRK12418 319 AA--------------LPAGPDAADVVARVRAA---LADDLDTPGALAAV 351
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
43-418 |
8.37e-78 |
|
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: 251.18 E-value: 8.37e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 43 GQHTGINIYNHGLRQKVPLilRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVtaMNITDVDDKI 121
Cdd:TIGR03447 13 GTGPPLRLFDTADGQVRPV--EPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAgHRVHYV--QNVTDVDDPL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 122 IKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNS---VYFDVSKSKN 198
Cdd:TIGR03447 89 FERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPEypdVYFSIDATEQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 199 YGKLQNLGLSE----------DKLDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHA 268
Cdd:TIGR03447 169 FGYESGYDRATmlelfaerggDPDRPGKRDPLDALLWRAAREG-EPSWDSPFG-RGRPGWHIECSAIALNRLGAGFDIQG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 269 GGLDLRFPHHENEEAQCCARYKTDQWVNYWVHTGqlhMVG-DREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRN 346
Cdd:TIGR03447 247 GGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAG---MIGlDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQ 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922218 347 AMPYSDQLMVTARQTLQRFRNFQADLSAytqflkpvhlldegalkAQLTHTVTEFDNCLRDDFDTARAISVL 418
Cdd:TIGR03447 324 DRDWTDAVLAEAEARLARWRAALALPDA-----------------PDATDLIARLRQHLANDLDTPAALAAV 378
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
50-540 |
2.18e-73 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 247.32 E-value: 2.18e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 50 IYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDyFKINLVTAMNITDVDDKIIKRAQLAG 129
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 130 LDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE 209
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 210 DK------LDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEA 283
Cdd:PRK14535 389 LRagerveVDGFKRDPLDFVLWKAAKAG-EPAWESPWG-NGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 284 Q-------CCARYKTD--------QWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAM 348
Cdd:PRK14535 467 QsvgatghTCGHHHAQthhgqsiaSHVKYWLHNGFIRV--DGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 349 PYSDQLMVTARQTLQRFrnfqadlsaYTQfLKPVHLLDEGALKAQLTHTvTEFDNCLRDDFDTARAISVLIDQMSSISRc 428
Cdd:PRK14535 545 NYSDAHLDDAKGALTRL---------YTT-LKNTPAAEFMLSENVNDYT-RRFYAAMNDDFGTVEAVAVLFELAGEVNK- 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 429 INEQQVDAQeepaycidlLLAAGNFInraivtfGLSELQDKESLQEKVSFTDHSidpNLLVNDVINVRGRMRERatsgnv 508
Cdd:PRK14535 613 TNDAQLAGC---------LKALGGII-------GLLQRDPTEFLQGGAASDGLS---NEEIEDLIARRKQARAD------ 667
|
490 500 510
....*....|....*....|....*....|..
gi 19922218 509 KNpqlLAACDELRSLLQQHGIQVRDHKQGSSW 540
Cdd:PRK14535 668 KN---WAESDRIRDLLNEHKIILEDNAGGTTW 696
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
48-540 |
9.68e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 237.90 E-value: 9.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDV---------- 117
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLH-FLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 118 DDKIIKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNsVYFDVSKSK 197
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGN-VYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 198 NYGKLQNLGLSEDK------LDPIKRNTADFALW--KARKSGSEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAG 269
Cdd:PRK14536 161 SYGSLASAAVEDLQagarieHDTNKRNPHDFVLWftRSKFENHALTWDSPWG-RGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 270 GLDLRFPHHENEEAQCCArYKTDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRNAM 348
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLM--NKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 349 PYSDQLMVTARQTLQRFRNFQA---DLSAYTQFLKPVHLLDEGALKAQLTHT------VTEFDNCLRDDFDTARAISVLi 419
Cdd:PRK14536 317 AFSWEALKTAKAARRSLVRRVArvvDAARATTGSVRGTLAECAAERVAESRAsesellLTDFRAALEDDFSTPKALSEL- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 420 dqmssiSRCINEQQVdaqeEPAYCIDLLLAAGNFINRAIVTFGLSELQDKESLQEKVSFTDHSIdpnllvndvinvrgrm 499
Cdd:PRK14536 396 ------QKLVKDTSV----PPSLCLSVLQAMDTVLGLGLIQEATASLSAQVPAGPSEEEIGQLI---------------- 449
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 19922218 500 RERATSGNVKNPQLlaaCDELRSLLQQHGIQVRDHKQGSSW 540
Cdd:PRK14536 450 EARAHARQTKDFPL---ADEIRDKLKAEGIELEDTHLGTIW 487
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
63-351 |
2.13e-51 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 183.13 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 63 LRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDV----------DDKIIKRAQLAGLDW 132
Cdd:PRK14534 16 LKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLR-LLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 133 QKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNsVYFDVSKSKNYGKLQNLGLSEDK- 211
Cdd:PRK14534 95 YEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGN-VYFDTSCFKSYGQMAGINLNDFKd 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 212 -------LDPIKRNTADFALW--KARKSGSEPTWAAPWGGeGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEE 282
Cdd:PRK14534 174 msvsrveIDKSKRNKSDFVLWftNSKFKDQEMKWDSPWGF-GYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEI 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922218 283 A--QCcarYKTDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRNAMPYS 351
Cdd:PRK14534 253 AiaEC---YLNKKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKFT 319
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
308-427 |
2.02e-11 |
|
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: 67.03 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 308 GDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQRFRN----FQADLSAY--TQFLKP 381
Cdd:COG0060 599 EDGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNtyrfLLANLDDFdpAEDAVP 678
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 19922218 382 V---HLLDEGALkAQLTHTVTEFDNCLrDDFDTARAISVL----IDQMSS----ISR 427
Cdd:COG0060 679 YedlPELDRWIL-SRLNELIKEVTEAY-DNYDFHRAYRALhnfcVEDLSNwyldISK 733
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
72-146 |
6.83e-10 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 57.49 E-value: 6.83e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922218 72 YTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVTamNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQD 146
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLgYKVRCIA--LIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| Ile_Leu_Val_MetRS_core |
cd00668 |
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ... |
73-336 |
1.06e-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: 57.04 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 73 TCG-PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAMNIT------------DVDDKIIKRAQLAGLDWQkMARA 138
Cdd:cd00668 5 TTPpPYANGSLHLGHALTHIIADFIARYKRmRGYEVPFLPGWDTHglpielkaerkgGRKKKTIWIEEFREDPKE-FVEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 139 YEAEFRQDMLRLNVQAPDVRSHVTTTmPVIIQFIQ----QLIDGKQAY-----VTPDNSVYFDVSKsknygklqnlgLSE 209
Cdd:cd00668 84 MSGEHKEDFRRLGISYDWSDEYITTE-PEYSKAVElifsRLYEKGLIYrgthpVRITEQWFFDMPK-----------FKE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 210 DKLDPIKRNTADFALWKAR-----KSGSEptWA----APWGGEgRPGWHIECSAIAGLFfgrqldiHAGGLDLRFPHHEN 280
Cdd:cd00668 152 KLLKALRRGKIVPEHVKNRmeawlESLLD--WAisrqRYWGTP-LPEDVFDVWFDSGIG-------PLGSLGYPEEKEWF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922218 281 EEAQCCARYKT--DQ---WVNYW----VHTGQLH-----------MVGDREKMSKSLGNTISVSELLKKYTADEFR 336
Cdd:cd00668 222 KDSYPADWHLIgkDIlrgWANFWitmlVALFGEIppknllvhgfvLDEGGQKMSKSKGNVIDPSDVVEKYGADALR 297
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
264-338 |
1.62e-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: 56.49 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 264 LDIHAGGLDL--------RFPHHeneeaqccARYKTDQWVNYWVH--TGQLHMVGDREKMSKSLGNTISVSELLKKYTAD 333
Cdd:cd00812 225 VDIYIGGKEHapnhllysRFNHK--------ALFDEGLVTDEPPKglIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGAD 296
|
....*
gi 19922218 334 EFRMA 338
Cdd:cd00812 297 AARLY 301
|
|
| valS |
PRK13208 |
valyl-tRNA synthetase; Reviewed |
309-418 |
2.94e-08 |
|
valyl-tRNA synthetase; Reviewed
Pssm-ID: 237306 [Multi-domain] Cd Length: 800 Bit Score: 56.74 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 309 DREKMSKSLGNTISVSELLKKYTADEFRM----ACLLSNYrnamPYSDQLMVTARQTLQRFRN---FQADLSAYTQFLKP 381
Cdd:PRK13208 530 DGKKMSKSKGNVVTPEELLEKYGADAVRYwaasARLGSDT----PFDEKQVKIGRRLLTKLWNasrFVLHFSADPEPDKA 605
|
90 100 110
....*....|....*....|....*....|....*....
gi 19922218 382 V--HLLDEgALKAQLTHTVTEFDNCLrDDFDTARAISVL 418
Cdd:PRK13208 606 EvlEPLDR-WILAKLAKVVEKATEAL-ENYDFAKALEEI 642
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
311-415 |
3.09e-07 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 53.33 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 311 EKMSKSLGNTISVSELLKKYTADEFRMAcLLSnyrNAMPYSD-----QLMVTARQTLQRFRNFQADLSAYTqflKPVHLL 385
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY-LTS---SAELLQDadwreKEVESVRRQLERFYELAKELIEIG---GEEELR 648
|
90 100 110
....*....|....*....|....*....|.
gi 19922218 386 DEGA-LKAQLTHTVTEFDNCLrDDFDTARAI 415
Cdd:PRK12300 649 FIDKwLLSRLNRIIKETTEAM-ESFQTRDAV 678
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
73-336 |
1.46e-05 |
|
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: 47.14 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 73 TCG-PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAMnitdvdD----KIIKRAQLAGLDWQKMARAYEAEFRQD 146
Cdd:cd00814 5 TTAlPYVNGVPHLGHLYGTVLADVFARYQRlRGYDVLFVTGT------DehgtKIEQKAEEEGVTPQELCDKYHEIFKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 147 MLRLNVQ--------APDvrsHVTTTMpviiQFIQQLID-G-------KQAYVTPDNSVYFDVSKSKNY----GKLQ--- 203
Cdd:cd00814 79 FKWLNISfdyfirttSPR---HKEIVQ----EFFKKLYEnGyiyegeyEGLYCVSCERFLPEWREEEHYffrlSKFQdrl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 204 -----------------NLGLS--EDKLDP--IKRNTADF-----------------AL---------WkARKSGSEPTW 236
Cdd:cd00814 152 lewleknpdfiwpenarNEVLSwlKEGLKDlsITRDLFDWgipvpldpgkviyvwfdALigyisatgyY-NEEWGNSWWW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 237 AAPWGgegrPGWHiecsaiaglFFGRqlDI---HA-------GGLDLRFPHHeneeaqccaryktdqwvnywVH-TGQLH 305
Cdd:cd00814 231 KDGWP----ELVH---------FIGK--DIirfHAiywpamlLGAGLPLPTR--------------------IVaHGYLT 275
|
330 340 350
....*....|....*....|....*....|.
gi 19922218 306 MVGdrEKMSKSLGNTISVSELLKKYTADEFR 336
Cdd:cd00814 276 VEG--KKMSKSRGNVVDPDDLLERYGADALR 304
|
|
| LeuS |
COG0495 |
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ... |
307-337 |
5.77e-05 |
|
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440261 [Multi-domain] Cd Length: 826 Bit Score: 46.20 E-value: 5.77e-05
10 20 30
....*....|....*....|....*....|.
gi 19922218 307 VGDREKMSKSLGNTISVSELLKKYTADEFRM 337
Cdd:COG0495 584 IGGIEKMSKSKGNVVDPDEIIEKYGADTLRL 614
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
76-153 |
6.29e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 45.64 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 76 PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAmnitdVDD---KIIKRAQLAGLDWQKMARAYEAEFRQDMLRLN 151
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFKRlRGYDVFFLTG-----TDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALN 84
|
..
gi 19922218 152 VQ 153
Cdd:PRK11893 85 IS 86
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
309-337 |
1.91e-04 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 43.76 E-value: 1.91e-04
10 20
....*....|....*....|....*....
gi 19922218 309 DREKMSKSLGNTISVSELLKKYTADEFRM 337
Cdd:cd00818 296 DGRKMSKSLGNYVDPQEVVDKYGADALRL 324
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
311-343 |
2.24e-04 |
|
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: 43.95 E-value: 2.24e-04
10 20 30
....*....|....*....|....*....|...
gi 19922218 311 EKMSKSLGNTISVSELLKKYTADEFRMAcLLSN 343
Cdd:COG0143 326 EKMSKSRGNVIDPDDLLDRYGPDALRYY-LLRE 357
|
|
| ValRS_core |
cd00817 |
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ... |
294-346 |
3.18e-04 |
|
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: 43.39 E-value: 3.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922218 294 WVNYWV-----HTGQ-------LH-MV--GDREKMSKSLGNTISVSELLKKYTADEFRMAclLSNYRN 346
Cdd:cd00817 310 WVARMImrglkLTGKlpfkevyLHgLVrdEDGRKMSKSLGNVIDPLDVIDGYGADALRFT--LASAAT 375
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| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
308-351 |
9.24e-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: 9.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 19922218 308 GDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYS 351
Cdd:pfam00133 559 EQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
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| DALR_2 |
smart00840 |
This DALR domain is found in cysteinyl-tRNA-synthetases; |
400-454 |
1.41e-03 |
|
This DALR domain is found in cysteinyl-tRNA-synthetases;
Pssm-ID: 214848 [Multi-domain] Cd Length: 56 Bit Score: 37.16 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 19922218 400 EFDNCLRDDFDTARAISVLIDqmssISRCINEQQVDAQ--EEPAYCIDLLLAAGNFI 454
Cdd:smart00840 1 RFEEAMDDDFNTPEALAVLFE----LAREINRLALKATdaEELAALAALLRALGGVL 53
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