|
Name |
Accession |
Description |
Interval |
E-value |
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
3-383 |
3.35e-154 |
|
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439932 [Multi-domain] Cd Length: 409 Bit Score: 440.62 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 3 GTAVVISREELKERLKlGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLS 82
Cdd:COG0162 11 GLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 83 REQVLENAETYTKQAFKILDRD--RTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYP 159
Cdd:COG0162 90 EEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 160 IMQGWDSVEI----RSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVDE---APEM 232
Cdd:COG0162 170 LLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEektSPYE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 233 MFGKMMSASDELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLaA 302
Cdd:COG0162 249 FYQKWMNISDADVWRYLKLFtflpleeieeLEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGEL-P 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 303 ADLPEVEIASLPAGMNAL-ALVAFLFEnvfqvkKSNGVLRKeHFTPGAIQLNDAKVTDPAAVPELAPGS-----VLRLSK 376
Cdd:COG0162 328 DDLPEVELSAAEGGIPLVdLLVEAGLA------ASKSEARR-LIKQGGVSVNGEKVTDPDAVLTAGDLLhggylVLRVGK 400
|
....*..
gi 524688481 377 KHAVRFK 383
Cdd:COG0162 401 KKFALVK 407
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
10-383 |
3.25e-130 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 379.63 E-value: 3.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 10 REELKERLKLGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLEN 89
Cdd:PRK13354 21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 90 AETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVE 168
Cdd:PRK13354 101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 169 IR----SDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEA---PEMMFGKMMSAS 241
Cdd:PRK13354 181 LNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 242 DELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAAADLPEVEIA 311
Cdd:PRK13354 260 DRDVVKYLKLFtdlspdeideLEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFEVS 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688481 312 SlpagmNALALVAFLFENVFQvkKSNGVLRkEHFTPGAIQLNDAKVTDPAAVPELAP-----GSVLRLSKKHAVRFK 383
Cdd:PRK13354 340 A-----ETKNLVDLLVDLGLE--PSKREAR-RLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLVK 408
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
6-360 |
4.38e-103 |
|
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272976 [Multi-domain] Cd Length: 378 Bit Score: 309.33 E-value: 4.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 6 VVISREELKERLK-LGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSRE 84
Cdd:TIGR00234 14 EVQTPEEEKDLLKlLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 85 QVLENAETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVLKLNSR-VTMQQMLAREDFKARVEggKEVRLHEMQYPIMQG 163
Cdd:TIGR00234 94 EVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFE--ENISLHEFIYPLLQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 164 WDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEAPEMMFGKMMSASDE 243
Cdd:TIGR00234 172 YDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE-KMGKSLGGAVSLDEGKYDFYQKVINTPDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 244 LMDRYYQVL----LGEKRDM----GLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAaadlPEVEIASLPA 315
Cdd:TIGR00234 251 LVKKYLKLFtflgLEEIEQLvelkGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP----DEVPIFRPEK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 524688481 316 GMNALALVAFLFENVFQVKKSNGvlrKEHFTPGAIQLNDAKVTDP 360
Cdd:TIGR00234 327 FGGPITLADLLVLSGLFPSKSEA---RRDIKNGGVYINGEKVEDL 368
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
23-277 |
5.02e-91 |
|
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173902 [Multi-domain] Cd Length: 269 Bit Score: 274.48 E-value: 5.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 23 LRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILD 102
Cdd:cd00805 1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RD---RTEIVYNGDWFRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTD 179
Cdd:cd00805 81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYV--GVDEAPEMMFGKMMSASDELMDRYYQVLL---- 253
Cdd:cd00805 161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTfldy 239
|
250 260 270
....*....|....*....|....*....|.
gi 524688481 254 -------GEKRDmGLHPMEAKKLLAWKITAR 277
Cdd:cd00805 240 eeieeleEEHAE-GPLPRDAKKALAEELTKL 269
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
18-279 |
1.05e-75 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 236.02 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 18 KLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgRSVTRPPLSREQVLENAetYTKQA 97
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 98 FKILDRDRTEIVYNGDWFRKMTYEEVLKLNSRV-TMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELG 176
Cdd:pfam00579 77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 177 GTDQLFNILVGRDLQK---EEGMLPQIAMTMPLLEGLDGVRKMSKSYGN----YVGVDEAPEMMFGKMMSASDELMDRYY 249
Cdd:pfam00579 157 GSDQWGNIELGRDLARrfnKKIFKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 524688481 250 QVLLGE-----KRDMGLH----PMEAKKLLAWKITARYH 279
Cdd:pfam00579 237 KLFTFLsneeiEILEAELgkspYREAEELLAREVTGLVH 275
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
3-383 |
3.35e-154 |
|
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439932 [Multi-domain] Cd Length: 409 Bit Score: 440.62 E-value: 3.35e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 3 GTAVVISREELKERLKlGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLS 82
Cdd:COG0162 11 GLIEQITDEELREKLA-GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 83 REQVLENAETYTKQAFKILDRD--RTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYP 159
Cdd:COG0162 90 EEQVAENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 160 IMQGWDSVEI----RSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVDE---APEM 232
Cdd:COG0162 170 LLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEektSPYE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 233 MFGKMMSASDELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLaA 302
Cdd:COG0162 249 FYQKWMNISDADVWRYLKLFtflpleeieeLEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGEL-P 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 303 ADLPEVEIASLPAGMNAL-ALVAFLFEnvfqvkKSNGVLRKeHFTPGAIQLNDAKVTDPAAVPELAPGS-----VLRLSK 376
Cdd:COG0162 328 DDLPEVELSAAEGGIPLVdLLVEAGLA------ASKSEARR-LIKQGGVSVNGEKVTDPDAVLTAGDLLhggylVLRVGK 400
|
....*..
gi 524688481 377 KHAVRFK 383
Cdd:COG0162 401 KKFALVK 407
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
10-383 |
3.25e-130 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 379.63 E-value: 3.25e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 10 REELKERLKLGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLEN 89
Cdd:PRK13354 21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQVQHN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 90 AETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVL-KLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVE 168
Cdd:PRK13354 101 AKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYDFVH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 169 IR----SDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEA---PEMMFGKMMSAS 241
Cdd:PRK13354 181 LNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAIWLDPEktsPYEFYQFWMNID 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 242 DELMDRYYQVL----------LGEKRDMGLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAAADLPEVEIA 311
Cdd:PRK13354 260 DRDVVKYLKLFtdlspdeideLEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFEVS 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 524688481 312 SlpagmNALALVAFLFENVFQvkKSNGVLRkEHFTPGAIQLNDAKVTDPAAVPELAP-----GSVLRLSKKHAVRFK 383
Cdd:PRK13354 340 A-----ETKNLVDLLVDLGLE--PSKREAR-RLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLVK 408
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
6-360 |
4.38e-103 |
|
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272976 [Multi-domain] Cd Length: 378 Bit Score: 309.33 E-value: 4.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 6 VVISREELKERLK-LGRPLRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSRE 84
Cdd:TIGR00234 14 EVQTPEEEKDLLKlLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 85 QVLENAETYTKQAFKILDRDRTEIVYNGDWFRKMTYEEVLKLNSR-VTMQQMLAREDFKARVEggKEVRLHEMQYPIMQG 163
Cdd:TIGR00234 94 EVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFE--ENISLHEFIYPLLQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 164 WDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYVGVDEAPEMMFGKMMSASDE 243
Cdd:TIGR00234 172 YDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE-KMGKSLGGAVSLDEGKYDFYQKVINTPDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 244 LMDRYYQVL----LGEKRDM----GLHPMEAKKLLAWKITARYHDSAAADAARADWETRFSKRDLAaadlPEVEIASLPA 315
Cdd:TIGR00234 251 LVKKYLKLFtflgLEEIEQLvelkGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP----DEVPIFRPEK 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 524688481 316 GMNALALVAFLFENVFQVKKSNGvlrKEHFTPGAIQLNDAKVTDP 360
Cdd:TIGR00234 327 FGGPITLADLLVLSGLFPSKSEA---RRDIKNGGVYINGEKVEDL 368
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
23-277 |
5.02e-91 |
|
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173902 [Multi-domain] Cd Length: 269 Bit Score: 274.48 E-value: 5.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 23 LRVKLGVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILD 102
Cdd:cd00805 1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RD---RTEIVYNGDWFRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTD 179
Cdd:cd00805 81 FIppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGVrKMSKSYGNYV--GVDEAPEMMFGKMMSASDELMDRYYQVLL---- 253
Cdd:cd00805 161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG-KMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTfldy 239
|
250 260 270
....*....|....*....|....*....|.
gi 524688481 254 -------GEKRDmGLHPMEAKKLLAWKITAR 277
Cdd:cd00805 240 eeieeleEEHAE-GPLPRDAKKALAEELTKL 269
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
18-279 |
1.05e-75 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 236.02 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 18 KLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgRSVTRPPLSREQVLENAetYTKQA 97
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 98 FKILDRDRTEIVYNGDWFRKMTYEEVLKLNSRV-TMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELG 176
Cdd:pfam00579 77 ACGLDPEKAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 177 GTDQLFNILVGRDLQK---EEGMLPQIAMTMPLLEGLDGVRKMSKSYGN----YVGVDEAPEMMFGKMMSASDELMDRYY 249
Cdd:pfam00579 157 GSDQWGNIELGRDLARrfnKKIFKKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDL 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 524688481 250 QVLLGE-----KRDMGLH----PMEAKKLLAWKITARYH 279
Cdd:pfam00579 237 KLFTFLsneeiEILEAELgkspYREAEELLAREVTGLVH 275
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
28-275 |
1.55e-31 |
|
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS)/Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. These enzymes attach Tyr or Trp, respectively, to the appropriate tRNA. These class I enzymes are homodimers, 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 class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173893 [Multi-domain] Cd Length: 273 Bit Score: 120.49 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 28 GVDPTAPDIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSGRSVTRPPLSREQVLENAETYTKQAFKILDRD--- 104
Cdd:cd00395 5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFEdpt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 105 RTEIVYNGDWFRKMTYEEVLK-LNSRVTMQQMLAREDFKARVEGGkeVRLHEMQYPIMQGWD----SVEIRSDVELGGTD 179
Cdd:cd00395 85 QATLFNNSDWPGPLAHIQFLRdLGKHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPGGSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 180 QLFNILVGRDL-QKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGNYVGVD---EAPEMMFGKMMSASDELMDRYYQVL--- 252
Cdd:cd00395 163 QWGNITLGRELaRRFNGFTIAEGLTIPLVTKLDG-PKFGKSESGPKWLDtekTSPYEFYQFWINAVDSDVINILKYFtfl 241
|
250 260 270
....*....|....*....|....*....|
gi 524688481 253 -------LGEKRDMGLHPMEAKKLLAWKIT 275
Cdd:cd00395 242 skeeierLEQEQYEAPGYRVAQKTLAEEVT 271
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
4-240 |
1.17e-27 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 111.11 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 4 TAVVISREELKERLKLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTATIGDPSgrsvtrpplSR 83
Cdd:PRK08560 12 TEEVVTEEELRELLESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLNDKG---------DL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 84 EQVLENAEtYTKQAFKI--LDRDRTEIVYNGDWFRKMTY-EEVLKLNSRVTMQQM------LAREDfkarveggKEVRLH 154
Cdd:PRK08560 82 EEIRKVAE-YNKKVFEAlgLDPDKTEFVLGSEFQLDKEYwLLVLKLAKNTTLARArrsmtiMGRRM--------EEPDVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 155 EMQYPIMQGWDSVEIRSDVELGGTDQLFNILVGRDLQKEEGMLPQIAMTMPLLEGLDGV-RKMSKS-YGNYVGVDEAPEM 232
Cdd:PRK08560 153 KLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgIKMSKSkPGSAIFVHDSPEE 232
|
....*...
gi 524688481 233 MFGKMMSA 240
Cdd:PRK08560 233 IRRKIKKA 240
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
28-240 |
5.73e-13 |
|
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the 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 class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding
Pssm-ID: 173903 [Multi-domain] Cd Length: 280 Bit Score: 68.38 E-value: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 28 GVDPTAPdIHLGHTV-AIEKLRQFQELGHQAILLIGD---FTATIGDPSGRsvtrpplsREQVLENAETYtkqafkI--- 100
Cdd:cd00806 5 GIQPSGS-LHLGHYLgAFRFWVWLQEAGYELFFFIADlhaLTVKQLDPEEL--------RQNTRENAKDY------Lacg 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 101 LDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKEVRLHEMQYPIMQGWDSVEIRSDVELGGTDQ 180
Cdd:cd00806 70 LDPEKSTIFFQSD--VPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 524688481 181 L------------FNILVGRDLQKEEGMLPQIAMTMPLLeglDGVRKMSKSYG-NYVGVDEAPEMMFGKMMSA 240
Cdd:cd00806 148 DphleltrdiarrFNKLYGEIFPKPAALLSKGAFLPGLQ---GPSKKMSKSDPnNAIFLTDSPKEIKKKIMKA 217
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
28-222 |
3.77e-10 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 60.51 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 28 GVDPTApDIHLGHTV-AIE-KLRQFQELGHQAILLIGDFTA--TIGDPSG-RSVTRpplsreqvlENAETYTKQAfkiLD 102
Cdd:PRK12556 9 GIKPTG-YPHLGNYIgAIKpALQMAKNYEGKALYFIADYHAlnAVHDPEQfRSYTR---------EVAATWLSLG---LD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 103 RDRTeIVYngdwfRKMTYEEVLKLN---SRVTMQQMLAR-EDFKARVEGGKE--------VRLHEMQYPIMQGWDSVEIR 170
Cdd:PRK12556 76 PEDV-IFY-----RQSDVPEIFELAwilSCLTPKGLMNRaHAYKAKVDQNKEagldldagVNMGLYTYPILMAADILLFQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 524688481 171 SDVELGGTDQL------------FNILVGRDLQKEEGMLPQIAMTMPlleGLDGvRKMSKSYGN 222
Cdd:PRK12556 150 ATHVPVGKDQIqhieiardiatyFNHTFGDTFTLPEYVIQEEGAILP---GLDG-RKMSKSYGN 209
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
22-240 |
8.18e-07 |
|
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272975 [Multi-domain] Cd Length: 327 Bit Score: 50.41 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 22 PLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGD---FTATIGDPSGRsvtrpplsREQVLENAETYTKQAF 98
Cdd:TIGR00233 2 KFRVLTGIQPSGK-MHLGHYLGAIQTKWLQQFGVELFICIADlhaITVKQTDPDAL--------RKAREELAADYLAVGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 99 kilDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGgKEVRLHEMQYPIMQGWDSVEIRSDVELGGT 178
Cdd:TIGR00233 73 ---DPEKTFIFLQSD--YPEHYELAWLLSCQVTFGELKRMTQFKDKSQA-ENVPIGLLSYPVLQAADILLYQADLVPVGI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 524688481 179 DQ------------LFNILVGRDLQKEEGMLPQiamTMPLLEGLDGvRKMSKSYGN-YVGVDEAPEMMFGKMMSA 240
Cdd:TIGR00233 147 DQdqhleltrdlaeRFNKKFKNFFPKPESLISK---FFPRLMGLSG-KKMSKSDPNsAIFLTDTPKQIKKKIRKA 217
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
182-240 |
2.17e-06 |
|
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tryptophanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439950 [Multi-domain] Cd Length: 330 Bit Score: 48.89 E-value: 2.17e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 524688481 182 FNILVGRDLQKEEGMLPQIAMTMPlleGLDGVRKMSKSYGNYVGVDEAPEMMFGKMMSA 240
Cdd:COG0180 165 FNHRYGEVFPEPEALIPEEGARIP---GLDGRKKMSKSYGNTINLLDDPKEIRKKIKSA 220
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
158-240 |
6.53e-05 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 44.46 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 158 YPIMQGWDSVEIRSDVELGGTDQL------------FNILVGRDLQKE-EGMLPQiamtMPLLEGLDGVRKMSKSYGNYV 224
Cdd:PRK12282 130 YPVSQAADITAFKATLVPVGDDQLpmieqtreivrrFNSLYGTDVLVEpEALLPE----AGRLPGLDGKAKMSKSLGNAI 205
|
90
....*....|....*.
gi 524688481 225 GVDEAPEMMFGKMMSA 240
Cdd:PRK12282 206 YLSDDADTIKKKVMSM 221
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
198-231 |
4.49e-04 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 41.86 E-value: 4.49e-04
10 20 30
....*....|....*....|....*....|....*...
gi 524688481 198 PQIAMT----MPlleGLDGvRKMSKSYGNYVGVDEAPE 231
Cdd:PRK12283 247 PQALLTeaskMP---GLDG-QKMSKSYGNTIGLREDPE 280
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
15-240 |
1.18e-03 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 40.62 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 15 ERLKLGRPLRVKLGVDPTAPdIHLGHTVAIEKLRQFQELGHQAILLIGDFTAtigdpsgRSVTRppLSREQVLENAETYT 94
Cdd:PRK12285 59 EAYRNGKPFAVYTGFMPSGP-MHIGHKMVFDELKWHQEFGANVYIPIADDEA-------YAARG--LSWEETREWAYEYI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 524688481 95 KQAFKI-LDRDRTEIVYNGDwfRKMTYEEVLKLNSRVTMQQMLAREDFKARVEGGKevrlheMQYPIMQGWD------SV 167
Cdd:PRK12285 129 LDLIALgFDPDKTEIYFQSE--NIKVYDLAFELAKKVNFSELKAIYGFTGETNIGH------IFYPATQAADilhpqlEE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 524688481 168 EIRSDVELGGTDQLFNILVGRD----LQKEEGMLPQIAMTMPLLEGLDGvRKMSKSYGN-YVGVDEAPEMMFGKMMSA 240
Cdd:PRK12285 201 GPKPTLVPVGIDQDPHIRLTRDiaerLHGGYGFIKPSSTYHKFMPGLTG-GKMSSSKPEsAIYLTDDPETVKKKIMKA 277
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
180-222 |
5.47e-03 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 38.45 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 524688481 180 QLFNILVGRDLQkeegMLP--QIAMTMPLLEGLDGvRKMSKSYGN 222
Cdd:PRK12284 170 QRFNHLYGGEFF----VLPeaVIEESVATLPGLDG-RKMSKSYDN 209
|
|
|