|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
27-546 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 545.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 27 WQRPQGQD---TGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSI 103
Cdd:PTZ00399 27 WKKPSKEGkylTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 104 TDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDL 182
Cdd:PTZ00399 107 TDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 183 HA-RGDK--YGKLVNTVPSATAEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVF 250
Cdd:PTZ00399 186 EAfRKAGhvYPKLEPESVADEDRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 251 GSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCL 330
Cdd:PTZ00399 266 GDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 331 RTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVN 406
Cdd:PTZ00399 344 LHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 407 TILDLVHHANRQLRAVSKeasgPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQ 484
Cdd:PTZ00399 424 ALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRD 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1315690829 485 YAldtpgAAGEARKRQLQERQPLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 546
Cdd:PTZ00399 499 AA-----KAEMKLISLDKKKKQLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
38-537 |
4.57e-175 |
|
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: 502.33 E-value: 4.57e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:COG0215 3 KLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 197
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 198 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 272
Cdd:COG0215 160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 273 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLL 352
Cdd:COG0215 239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 353 LGLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSP 432
Cdd:COG0215 316 ERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 433 TVFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcD 512
Cdd:COG0215 381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-D 440
|
490 500
....*....|....*....|....*
gi 1315690829 513 TLRQDLVTHGINVKDrGSAASTWEL 537
Cdd:COG0215 441 RIRDELAALGIVLED-TPDGTTWRR 464
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
39-416 |
7.59e-140 |
|
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: 412.55 E-value: 7.59e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVPS 198
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 199 -----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIA 273
Cdd:TIGR00435 161 qleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 274 QSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK---- 349
Cdd:TIGR00435 240 QSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnale 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1315690829 350 HLLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 416
Cdd:TIGR00435 317 RLYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
58-349 |
3.86e-137 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 399.43 E-value: 3.86e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 58 VSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMA 137
Cdd:pfam01406 10 VTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 138 ALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSATAEPGDSDKRHSSD 213
Cdd:pfam01406 89 ALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAGARGEVSEGKRDPLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 214 FALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGH 293
Cdd:pfam01406 168 FALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1315690829 294 LHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 349
Cdd:pfam01406 247 VMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
38-341 |
1.87e-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: 325.30 E-value: 1.87e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvp 197
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 198 sataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEV 277
Cdd:cd00672 113 ----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEA 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1315690829 278 FHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 341
Cdd:cd00672 153 ATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
30-348 |
7.36e-91 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 289.52 E-value: 7.36e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 30 PQGQDTGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDK 109
Cdd:PLN02946 53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 110 IIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKY 189
Cdd:PLN02946 132 IIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 190 GKLV------NTVPSATAEpgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDL 263
Cdd:PLN02946 210 GKLSgrkledNRAGERVAV--DSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 264 AFPHHENEIAQSEVfHQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDS 343
Cdd:PLN02946 288 VFPHHENEIAQSCA-ACCDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV 364
|
....*
gi 1315690829 344 TLVEA 348
Cdd:PLN02946 365 QLESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
39-435 |
2.37e-88 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 287.00 E-value: 2.37e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNT 195
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 196 VPSATAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS 275
Cdd:PRK14535 389 LRAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQS 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 276 --EVFHQCQQWG-------------NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEY 340
Cdd:PRK14535 469 vgATGHTCGHHHaqthhgqsiashvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNY 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 341 SDSTLVEAKHLLLGLASFVEDArayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR--- 417
Cdd:PRK14535 547 SDAHLDDAKGALTRLYTTLKNT-----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtnd 615
|
410 420
....*....|....*....|....
gi 1315690829 418 -QLRAVSKEASG-----PRSPTVF 435
Cdd:PRK14535 616 aQLAGCLKALGGiigllQRDPTEF 639
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
26-404 |
3.41e-72 |
|
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: 236.16 E-value: 3.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 26 SWQRPQ-----GQDTGVQVHNSLTGRKEPliVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMA 100
Cdd:TIGR03447 2 SWPAPAvpalpGTGPPLRLFDTADGQVRP--VEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVW-RDAGHRVHYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 101 MSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGS 177
Cdd:TIGR03447 79 QNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 178 VYFDLHArGDKYGKLVN----TVPSATAE----PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEV 249
Cdd:TIGR03447 159 VYFSIDA-TEQFGYESGydraTMLELFAErggdPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 250 FGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLF 328
Cdd:TIGR03447 238 LGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1315690829 329 CLRTNYRSAIEYSDSTLVEAKHLLlglasfvedARAYVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 404
Cdd:TIGR03447 316 LLAGHYRQDRDWTDAVLAEAEARL---------ARWRAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
52-408 |
4.57e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 235.21 E-value: 4.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEE 131
Cdd:PRK12418 4 VAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVW-RDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 132 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVNTVPSATAE------ 202
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMLElfaerg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 203 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 280
Cdd:PRK12418 162 gdPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 281 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 359
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL------- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1315690829 360 EDARAYVKgqLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 408
Cdd:PRK12418 313 ARWRAAAA--LPAGPDAADVV--------ARVRAALADDLDTPGALAAV 351
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
37-412 |
9.55e-71 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 234.82 E-value: 9.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 37 VQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV---------- 106
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 107 DDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARG 186
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 187 DkYGKLVNT----VPSATAEPGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTG 259
Cdd:PRK14536 161 S-YGSLASAavedLQAGARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 260 GIDLAFPHHENEIAQSEVFhQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAI 338
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 339 EYSDSTLVEAK----HLLLGLASFVEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPR 403
Cdd:PRK14536 317 AFSWEALKTAKaarrSLVRRVARVVDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPK 390
|
....*....
gi 1315690829 404 AVNTILDLV 412
Cdd:PRK14536 391 ALSELQKLV 399
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
52-349 |
1.43e-57 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 199.69 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTP 121
Cdd:PRK14534 16 LKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 122 ASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKL----VNTVP 197
Cdd:PRK14534 95 YEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMaginLNDFK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 198 SATAEPGDSD--KRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 272
Cdd:PRK14534 173 DMSVSRVEIDksKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEI 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1315690829 273 AQSEVFHQcQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 349
Cdd:PRK14534 253 AIAECYLN-KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKACK 327
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
291-417 |
6.96e-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: 58.20 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 291 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 360
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 361 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 417
Cdd:COG0143 396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
254-328 |
6.60e-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: 51.48 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 254 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 322
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295
|
....*.
gi 1315690829 323 DVFRLF 328
Cdd:cd00812 296 DAARLY 301
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
302-412 |
2.49e-06 |
|
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: 50.46 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 302 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 370
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1315690829 371 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 412
Cdd:COG0060 683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
291-343 |
2.83e-06 |
|
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: 49.45 E-value: 2.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1315690829 291 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 343
Cdd:cd00814 271 HGYLTVEG--KKMSKSRGNVVDPDDLLERYGADALRYYLL----RERPEGKDS 317
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
65-141 |
1.09e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 47.95 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 65 PTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMamsITDVDD---KIIKRANEMNVTPASLASLFEEEFKQDMAALKV 141
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFK-RLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
291-417 |
8.61e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.53 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315690829 291 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 357
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1315690829 358 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 417
Cdd:PRK00133 392 rtagFINK---RFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANK 450
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
61-135 |
9.03e-05 |
|
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: 42.85 E-value: 9.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1315690829 61 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQD 135
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
291-347 |
1.66e-04 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 44.20 E-value: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1315690829 291 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 347
Cdd:pfam09334 315 HGYLTYEG--GKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
237-307 |
2.03e-04 |
|
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: 41.70 E-value: 2.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1315690829 237 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 307
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
287-332 |
2.11e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1315690829 287 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 332
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
301-328 |
4.00e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 43.32 E-value: 4.00e-04
10 20
....*....|....*....|....*...
gi 1315690829 301 EKMSKSLKNYITIKDFLKTFSPDVFRLF 328
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
390-426 |
2.36e-03 |
|
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
Pssm-ID: 462711 [Multi-domain] Cd Length: 63 Bit Score: 36.41 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1315690829 390 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 426
Cdd:pfam09190 1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDAEA 37
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
302-341 |
3.19e-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: 40.47 E-value: 3.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1315690829 302 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 341
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
301-339 |
7.26e-03 |
|
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.
Pssm-ID: 396483 Cd Length: 357 Bit Score: 38.78 E-value: 7.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1315690829 301 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 339
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
301-335 |
8.51e-03 |
|
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: 38.37 E-value: 8.51e-03
10 20 30
....*....|....*....|....*....|....*
gi 1315690829 301 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 335
Cdd:cd00818 298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| |
