|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
27-547 |
0e+00 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 546.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 27 WQRPQGQD---TGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVFGCNVVMAMSI 103
Cdd:PTZ00399 27 WKKPSKEGkylTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRRILEDYFGYDVFYVMNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 104 TDVDDKIIKRANEMNVTPAS-LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDL 182
Cdd:PTZ00399 107 TDIDDKIIKRAREEKLSIFLeLARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 183 HA-RGDK--YGKL----VNTVpSATAEPAGD-----SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEV 250
Cdd:PTZ00399 186 EAfRKAGhvYPKLepesVADE-DRIAEGEGAlgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 251 FGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFC 330
Cdd:PTZ00399 265 LGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 331 LRTNYRSAIEYSDSTLVEAKHLLLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAV 406
Cdd:PTZ00399 343 LLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEAL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 407 NTILDLVHHANRQLRAVSKeasgPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVR 484
Cdd:PTZ00399 423 QALQKLISATNTYLNSGEQ----PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVR 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189409152 485 QYAldtpgAAGEARKRQLQERQPLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 547
Cdd:PTZ00399 498 DAA-----KAEMKLISLDKKKKQLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
|
|
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
38-538 |
2.06e-176 |
|
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: 505.79 E-value: 2.06e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILTRVfGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:COG0215 3 KLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYL-GYKVTYVRNITDVDDKIIKRAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 197
Cdd:COG0215 82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 198 S---ATAEPAGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIA 274
Cdd:COG0215 160 DdlrAGARVEVDEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 275 QSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLL 354
Cdd:COG0215 240 QSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKALE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 355 GLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSPT 434
Cdd:COG0215 317 RLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDKA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 435 VFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcDT 514
Cdd:COG0215 382 ALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-DR 441
|
490 500
....*....|....*....|....
gi 189409152 515 LRQDLVTHGINVKDrGSAASTWEL 538
Cdd:COG0215 442 IRDELAALGIVLED-TPDGTTWRR 464
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
39-417 |
3.67e-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: 413.32 E-value: 3.67e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:TIGR00435 3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYL-RYLGYKVQYVQNITDIDDKIIKRARENG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVN-TVP 197
Cdd:TIGR00435 82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKqDLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 198 SATAEPAGDSD--KRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQ 275
Cdd:TIGR00435 161 QLEAGARVDVDeaKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 276 SEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----H 351
Cdd:TIGR00435 241 SEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnaleR 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189409152 352 LLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 417
Cdd:TIGR00435 318 LYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
58-350 |
6.03e-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: 399.05 E-value: 6.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 58 VSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMA 137
Cdd:pfam01406 10 VTMYVCGPTVYDYSHIGHARSAVAFDVLRRYL-QALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 138 ALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKLVNTVPS---ATAEPAGDSDKRHSSD 214
Cdd:pfam01406 89 ALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLSGQNLEqleAGARGEVSEGKRDPLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 215 FALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQcQQWGNYFLHSGH 294
Cdd:pfam01406 168 FALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGH 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 189409152 295 LHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 350
Cdd:pfam01406 247 VMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
38-342 |
2.34e-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: 2.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 38 QVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEM 117
Cdd:cd00672 1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYL-EDLGYKVRYVQNITDIDDKIIKRAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 118 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntvp 197
Cdd:cd00672 80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 198 sataepagdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 277
Cdd:cd00672 113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189409152 278 VFHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 342
Cdd:cd00672 152 AATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
30-349 |
1.28e-91 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 291.45 E-value: 1.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 30 PQGQDTGVQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDK 109
Cdd:PLN02946 53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYL-KHLGYEVRYVRNFTDVDDK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 110 IIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKY 189
Cdd:PLN02946 132 IIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEY 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 190 GKLVNTV---PSATAEPAGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAF 266
Cdd:PLN02946 210 GKLSGRKledNRAGERVAVDSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 267 PHHENEIAQSEVfHQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTL 346
Cdd:PLN02946 290 PHHENEIAQSCA-ACCDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQL 366
|
...
gi 189409152 347 VEA 349
Cdd:PLN02946 367 ESA 369
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
39-436 |
3.09e-87 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 283.92 E-value: 3.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 39 VHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMN 118
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWL-RECGYPLTYVRNITDIDDKIIARAAENG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 119 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNT 195
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 196 VpSATAEPAGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQ 275
Cdd:PRK14535 389 L-RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQ 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 276 S--EVFHQCQQWG-------------NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 340
Cdd:PRK14535 468 SvgATGHTCGHHHaqthhgqsiashvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 341 YSDSTLVEAKHLLLGLASFVEDArayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR-- 418
Cdd:PRK14535 546 YSDAHLDDAKGALTRLYTTLKNT-----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtn 614
|
410 420
....*....|....*....|....*
gi 189409152 419 --QLRAVSKEASG-----PRSPTVF 436
Cdd:PRK14535 615 daQLAGCLKALGGiigllQRDPTEF 639
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
26-405 |
1.45e-73 |
|
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: 240.01 E-value: 1.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 26 SWQRPQ-----GQDTGVQVHNSLTGRKEPliVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMA 100
Cdd:TIGR03447 2 SWPAPAvpalpGTGPPLRLFDTADGQVRP--VEPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVW-RDAGHRVHYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 101 MSITDVDDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGS 177
Cdd:TIGR03447 79 QNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 178 VYFDLHArGDKYGKLVN----TVPSATAEPAGDSD---KRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEV 250
Cdd:TIGR03447 159 VYFSIDA-TEQFGYESGydraTMLELFAERGGDPDrpgKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 251 FGSHLDIHTGGIDLAFPHHENEIAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLF 329
Cdd:TIGR03447 238 LGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLG 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189409152 330 CLRTNYRSAIEYSDSTLVEAKHLLlglasfvedARAYVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 405
Cdd:TIGR03447 316 LLAGHYRQDRDWTDAVLAEAEARL---------ARWRAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
52-409 |
4.22e-73 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 237.91 E-value: 4.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEE 131
Cdd:PRK12418 4 VAPGGTATMYVCGITPYDATHLGHAATYLAFDLVNRVW-RDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 132 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVN----TVPSATAEPA 204
Cdd:PRK12418 83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGydraTMLELFAERG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 205 GDSD---KRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 281
Cdd:PRK12418 162 GDPDrpgKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 282 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 360
Cdd:PRK12418 242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL------- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 189409152 361 EDARAYVKgqLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 409
Cdd:PRK12418 313 ARWRAAAA--LPAGPDAADVV--------ARVRAALADDLDTPGALAAV 351
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
37-413 |
9.78e-72 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 237.51 E-value: 9.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 37 VQVHNSLTGRKEPLIVARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV---------- 106
Cdd:PRK14536 3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTL-HFLGYRVTHVMNITDVghltddadsg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 107 DDKIIKRANEMNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARG 186
Cdd:PRK14536 82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 187 DkYGKLVNTVPS---ATAEPAGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTG 260
Cdd:PRK14536 161 S-YGSLASAAVEdlqAGARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 261 GIDLAFPHHENEIAQSEVFhQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAI 339
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEAA-TGKPWVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 340 EYSDSTLVEAK----HLLLGLASFVEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPR 404
Cdd:PRK14536 317 AFSWEALKTAKaarrSLVRRVARVVDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPK 390
|
....*....
gi 189409152 405 AVNTILDLV 413
Cdd:PRK14536 391 ALSELQKLV 399
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
52-350 |
2.64e-58 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 201.62 E-value: 2.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 52 VARSDAVSWYSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDV----------DDKIIKRANEMNVTP 121
Cdd:PRK14534 16 LKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSL-RLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 122 ASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGK-----LVNTV 196
Cdd:PRK14534 95 YEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQmaginLNDFK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 197 PSATAEPAGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 273
Cdd:PRK14534 173 DMSVSRVEIDKSKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEI 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189409152 274 AQSEVFHQcQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 350
Cdd:PRK14534 253 AIAECYLN-KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKACK 327
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
292-418 |
7.10e-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: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 292 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 361
Cdd:COG0143 318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 362 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 418
Cdd:COG0143 396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
255-329 |
6.61e-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: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 255 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 323
Cdd:cd00812 225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295
|
....*.
gi 189409152 324 DVFRLF 329
Cdd:cd00812 296 DAARLY 301
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
303-413 |
2.50e-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: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 303 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 371
Cdd:COG0060 603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 189409152 372 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 413
Cdd:COG0060 683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
292-344 |
2.79e-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: 2.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 189409152 292 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 344
Cdd:cd00814 271 HGYLTVEG--KKMSKSRGNVVDPDDLLERYGADALRYYLL----RERPEGKDS 317
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
65-141 |
1.10e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 47.95 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 65 PTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMamsITDVDD---KIIKRANEMNVTPASLASLFEEEFKQDMAALKV 141
Cdd:PRK11893 10 YYPNGKPHIGHAYTTLAADVLARFK-RLRGYDVFF---LTGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI 85
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
292-418 |
8.63e-05 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 45.53 E-value: 8.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189409152 292 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 358
Cdd:PRK00133 320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189409152 359 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 418
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 |
8.96e-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: 8.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189409152 61 YSCGPTVYDHAHLGHACSYVRFDIIRRILtRVFGCNVVMAMSITDVDDKIIKRANEMNVTPASLASLFEEEFKQD 135
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIVTFDFLAQAY-RKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
292-348 |
1.67e-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: 1.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 189409152 292 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 348
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 ... |
238-308 |
2.00e-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: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189409152 238 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 308
Cdd:cd00802 77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
288-333 |
2.12e-04 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 44.10 E-value: 2.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 189409152 288 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 333
Cdd:PRK11893 287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
302-329 |
4.01e-04 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 43.32 E-value: 4.01e-04
10 20
....*....|....*....|....*...
gi 189409152 302 EKMSKSLKNYITIKDFLKTFSPDVFRLF 329
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
|
|
| DALR_2 |
pfam09190 |
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases. |
391-427 |
2.37e-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: 2.37e-03
10 20 30
....*....|....*....|....*....|....*..
gi 189409152 391 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 427
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 ... |
303-342 |
3.20e-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: 3.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 189409152 303 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 342
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
|
|
| tRNA-synt_1f |
pfam01921 |
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ... |
302-340 |
7.21e-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: 7.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 189409152 302 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 340
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
302-336 |
8.38e-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: 38.75 E-value: 8.38e-03
10 20 30
....*....|....*....|....*....|....*
gi 189409152 302 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 336
Cdd:cd00818 298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
|
|
| |
