|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
3-333 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 625.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIFVQ 82
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 83 SHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ 162
Cdd:PRK00927 81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 163 RFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNKAG 242
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 243 VSNLLDILSAVTGQSIPELEKQFE--GKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT 320
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|...
gi 41228 321 LKAVYQAIGFVAK 333
Cdd:PRK00927 321 LKEVREAMGLLRK 333
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-331 |
0e+00 |
|
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: 566.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 1 MTKPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF 80
Cdd:COG0180 1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 81 VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARY-AENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRD 159
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 160 IAQRFNALYGEIFKVPEPFIPKSGARVMSlLEPTKKMSKSDdnrNNVIGLLEDPKSVVKKIKRAVTDSDEppvVRYDVQN 239
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPEEGARIPG-LDGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSER---LRYDDPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 240 KAGVSNLLDILSAVTGQ-SIPELEKQFE--GKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAH 316
Cdd:COG0180 234 KPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAI 313
|
330
....*....|....*
gi 41228 317 ASRTLKAVYQAIGFV 331
Cdd:COG0180 314 AAKTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
5-284 |
8.81e-145 |
|
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: 409.67 E-value: 8.81e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 5 IVFSGAQPSGELTIGNYMGALRQWVKMQD-DYHCIYCIVDQHAITVRQ-DAQKLRKATLDTLALYLACGIDPEKSTIFVQ 82
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 83 SHVPEHAQLGWALNCYTYFGELSRMTQFKDKSArYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ 162
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 163 RFNALYGEIFKVPEPFIPKsGARVMSLLEPTKKMSKSDDnrNNVIGLLEDPKSVVKKIKRAVTDSDepPVVRYDVQNKAG 242
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGG--RTEHRRDGGGPG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41228 243 VSNLLDILSAVTGQSIPELEK----QFEGKMYGHLKGEVADAVSGM 284
Cdd:cd00806 235 VSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQEF 280
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
3-330 |
2.60e-140 |
|
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: 400.17 E-value: 2.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQ-DAQKLRKATLDTLALYLACGIDPEKSTIFV 81
Cdd:TIGR00233 2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 82 QSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSarYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIA 161
Cdd:TIGR00233 82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 162 QRFNALYGEIFKVPEPFIPKSGARVMSLlePTKKMSKSDDnrNNVIGLLEDPKSVVKKIKRAVTDSDEPpvVRYDVQNKA 241
Cdd:TIGR00233 160 ERFNKKFKNFFPKPESLISKFFPRLMGL--SGKKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV--TLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 242 GVSNLLDILSAVTGQSIP------ELEKQFEGK-MYGHLKGEVADAVSGMLTELQERYHRFRNDEAFlqQVMKDGAEKAS 314
Cdd:TIGR00233 234 GVPNLLVIYQYLSFFLIDddklkeIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAEEILD--KILEPGAKKAR 311
|
330
....*....|....*.
gi 41228 315 AHASRTLKAVYQAIGF 330
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
3-286 |
2.07e-99 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 294.95 E-value: 2.07e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGnYMGALRQWVKMQDD-YHCIYCIVDQHAITVRQD---AQKLRKATLDTLAL---YLACGIDPE 75
Cdd:pfam00579 5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 76 KSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAEN--INAGLFDYPVLMAADILLYQTNLVPVGEDQKQH 153
Cdd:pfam00579 84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGpgISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 154 LELSRDIAQRFNalyGEIFKVPEPFIPKsgarVMSLLEPTKKMSKSDDNRnnVIGLLEDPKSVVKKIKRAVTDSDEppVV 233
Cdd:pfam00579 164 IELGRDLARRFN---KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKAYTDPDR--EV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 234 RYDVQNKAGVSN-LLDILSAVTGQSIP----ELEKQFEGKM--YGHLKGEVADAVSGMLT 286
Cdd:pfam00579 233 RKDLKLFTFLSNeEIEILEAELGKSPYreaeELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
3-333 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 625.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIFVQ 82
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 83 SHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ 162
Cdd:PRK00927 81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 163 RFNALYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRYDVQNKAG 242
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 243 VSNLLDILSAVTGQSIPELEKQFE--GKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASRT 320
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|...
gi 41228 321 LKAVYQAIGFVAK 333
Cdd:PRK00927 321 LKEVREAMGLLRK 333
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
1-331 |
0e+00 |
|
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: 566.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 1 MTKPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF 80
Cdd:COG0180 1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 81 VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARY-AENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRD 159
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 160 IAQRFNALYGEIFKVPEPFIPKSGARVMSlLEPTKKMSKSDdnrNNVIGLLEDPKSVVKKIKRAVTDSDEppvVRYDVQN 239
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPEEGARIPG-LDGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSER---LRYDDPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 240 KAGVSNLLDILSAVTGQ-SIPELEKQFE--GKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAH 316
Cdd:COG0180 234 KPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAI 313
|
330
....*....|....*
gi 41228 317 ASRTLKAVYQAIGFV 331
Cdd:COG0180 314 AAKTLAEVREAMGLL 328
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
1-334 |
2.64e-150 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 428.08 E-value: 2.64e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 1 MTKPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIF 80
Cdd:PLN02886 44 ARKKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 81 VQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARY-AENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRD 159
Cdd:PLN02886 124 VQSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 160 IAQRFNALYG------------EIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKSVVKKIKRAVTDS 227
Cdd:PLN02886 204 IAERVNNLYGgrkwkklggrggSVFKVPEALIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 228 dePPVVRYDVQNKAGVSNLLDILSAVTGQSIPELEKQFEGKMYGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMK 307
Cdd:PLN02886 284 --FPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLK 361
|
330 340
....*....|....*....|....*..
gi 41228 308 DGAEKASAHASRTLKAVYQAIGFVAKR 334
Cdd:PLN02886 362 EGADAAAEIADRTLANVYQAMGFVQRR 388
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
5-284 |
8.81e-145 |
|
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: 409.67 E-value: 8.81e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 5 IVFSGAQPSGELTIGNYMGALRQWVKMQD-DYHCIYCIVDQHAITVRQ-DAQKLRKATLDTLALYLACGIDPEKSTIFVQ 82
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 83 SHVPEHAQLGWALNCYTYFGELSRMTQFKDKSArYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ 162
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 163 RFNALYGEIFKVPEPFIPKsGARVMSLLEPTKKMSKSDDnrNNVIGLLEDPKSVVKKIKRAVTDSDepPVVRYDVQNKAG 242
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGG--RTEHRRDGGGPG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41228 243 VSNLLDILSAVTGQSIPELEK----QFEGKMYGHLKGEVADAVSGM 284
Cdd:cd00806 235 VSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQEF 280
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
3-330 |
2.60e-140 |
|
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: 400.17 E-value: 2.60e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVRQ-DAQKLRKATLDTLALYLACGIDPEKSTIFV 81
Cdd:TIGR00233 2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 82 QSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSarYAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIA 161
Cdd:TIGR00233 82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 162 QRFNALYGEIFKVPEPFIPKSGARVMSLlePTKKMSKSDDnrNNVIGLLEDPKSVVKKIKRAVTDSDEPpvVRYDVQNKA 241
Cdd:TIGR00233 160 ERFNKKFKNFFPKPESLISKFFPRLMGL--SGKKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV--TLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 242 GVSNLLDILSAVTGQSIP------ELEKQFEGK-MYGHLKGEVADAVSGMLTELQERYHRFRNDEAFlqQVMKDGAEKAS 314
Cdd:TIGR00233 234 GVPNLLVIYQYLSFFLIDddklkeIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAEEILD--KILEPGAKKAR 311
|
330
....*....|....*.
gi 41228 315 AHASRTLKAVYQAIGF 330
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
3-286 |
2.07e-99 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 294.95 E-value: 2.07e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGnYMGALRQWVKMQDD-YHCIYCIVDQHAITVRQD---AQKLRKATLDTLAL---YLACGIDPE 75
Cdd:pfam00579 5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 76 KSTIFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAEN--INAGLFDYPVLMAADILLYQTNLVPVGEDQKQH 153
Cdd:pfam00579 84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGpgISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 154 LELSRDIAQRFNalyGEIFKVPEPFIPKsgarVMSLLEPTKKMSKSDDNRnnVIGLLEDPKSVVKKIKRAVTDSDEppVV 233
Cdd:pfam00579 164 IELGRDLARRFN---KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKAYTDPDR--EV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 234 RYDVQNKAGVSN-LLDILSAVTGQSIP----ELEKQFEGKM--YGHLKGEVADAVSGMLT 286
Cdd:pfam00579 233 RKDLKLFTFLSNeEIEILEAELGKSPYreaeELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
2-329 |
3.11e-96 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 288.29 E-value: 3.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 2 TKPIVFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAIT-VRQDAQKLRKATLDTLALYLACGIDPEKSTIF 80
Cdd:PRK12282 1 TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 81 VQSHVPEHAQLGWA-LNCYTyFGELSRMTQFKDKSAR--YAENINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLELS 157
Cdd:PRK12282 81 IQSQIPELAELTMYyMNLVT-VARLERNPTVKTEIAQkgFGRSIPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 158 RDIAQRFNALYG-EIFKVPEPFIPKSGaRVMSlLEPTKKMSKSDdnrNNVIGLLEDPKSVVKKIKRAVTDSDEppvVRYD 236
Cdd:PRK12282 160 REIVRRFNSLYGtDVLVEPEALLPEAG-RLPG-LDGKAKMSKSL---GNAIYLSDDADTIKKKVMSMYTDPNH---IRVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 237 VQNKAGVSNLLDILSAV--TGQSIPELEKQFEGKMYG--HLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEK 312
Cdd:PRK12282 232 DPGKVEGNVVFTYLDAFdpDKAEVAELKAHYQRGGLGdvKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEK 311
|
330
....*....|....*..
gi 41228 313 ASAHASRTLKAVYQAIG 329
Cdd:PRK12282 312 AREVAAQTLSEVKDAMG 328
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
1-330 |
7.07e-87 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 264.28 E-value: 7.07e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 1 MTKPIVFSGAQPSGELTIGNYMGALRQWVKM--QDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKST 78
Cdd:PRK12556 1 MSEKIMLTGIKPTGYPHLGNYIGAIKPALQMakNYEGKALYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 79 IFVQSHVPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAE-------NINAGLFDYPVLMAADILLYQTNLVPVGEDQK 151
Cdd:PRK12556 81 FYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEagldldaGVNMGLYTYPILMAADILLFQATHVPVGKDQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 152 QHLELSRDIAQRFNALYGEIFKVPEPFIPKSGArVMSLLEpTKKMSKSDDnrnNVIGLLEDPKSVVKKIKRAVTDSdEPP 231
Cdd:PRK12556 161 QHIEIARDIATYFNHTFGDTFTLPEYVIQEEGA-ILPGLD-GRKMSKSYG---NVIPLFAEQEKLRKLIFKIKTDS-SLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 232 VVRYDVQNkagvSNLLDILSA-VTGQSIPELEKQFEGKM-YGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDG 309
Cdd:PRK12556 235 NEPKDPET----SALFTIYKEfATEEEVQSMREKYETGIgWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKG 310
|
330 340
....*....|....*....|.
gi 41228 310 AEKASAHASRTLKAVYQAIGF 330
Cdd:PRK12556 311 AERAREIAKPNLAEIKKAIGF 331
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
6-329 |
1.19e-66 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 214.43 E-value: 1.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 6 VFSGAQPSGELTIGNYMGALRQWVKMQDDYHCIYCIVDQHAITVR-QDAQKLRKATLDTLALYLACGIDPEKSTIFVQSH 84
Cdd:PRK12283 5 VLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTTHyETPEVIEKNVWDMVIDWLAAGVDPAQATLFIQSK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 85 VPEHAQLGWALNCYTYFGELSRMTQFKDKSARYAENINA--GLFDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQ 162
Cdd:PRK12283 85 VPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKDLStyGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 163 RFNALYG-------------------------------------EIFKVPEPFIPKS----------------GARVMSL 189
Cdd:PRK12283 165 RFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddEALEQARALLQEQqnlsmgdrerlfgyleGAGKIIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 190 LEP----TK----------KMSKSddnRNNVIGLLEDPKSVVKKIKRAVTD------SD--EP---PV-----VRYDVQN 239
Cdd:PRK12283 245 PEPqallTEaskmpgldgqKMSKS---YGNTIGLREDPESVTKKIRTMPTDparvrrTDpgDPekcPVwqlhqVYSDEET 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 240 KAGVSNlldilsAVTGQSIPELEkqfegkmyghLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKASAHASR 319
Cdd:PRK12283 322 KEWVQK------GCRSAGIGCLE----------CKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARE 385
|
410
....*....|
gi 41228 320 TLKAVYQAIG 329
Cdd:PRK12283 386 TMRDVREAMG 395
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
6-329 |
5.93e-63 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 206.01 E-value: 5.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 6 VFSGAQPSGELTIGNYMGALRQWVK--MQDDYHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGIDPEKSTIFVQS 83
Cdd:PRK12284 5 VLTGITTTGTPHLGNYAGAIRPAIAasRQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 84 HVPEHAQLGWALNCYTYFGELSRMTQFK---DKSARYAE----NINAGLFDYPVLMAADILLYQTNLVPVGEDQKQHLEL 156
Cdd:PRK12284 85 DIPEIPELTWLLTCVAGKGLLNRAHAYKaavDKNVAAGEdpdaGVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 157 SRDIAQRFNALYG-EIFKVPEPFIPKSGARVMSLlePTKKMSKSDDnrnNVIGLLEDPKSVVKKIKRAVTDSDEPPVVRy 235
Cdd:PRK12284 165 ARDIAQRFNHLYGgEFFVLPEAVIEESVATLPGL--DGRKMSKSYD---NTIPLFAPREELKKAIFSIVTDSRAPGEPK- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 236 DVQNkagvSNLLDILSA-VTGQSIPELEKQFEGKM-YGHLKGEVADAVSGMLTELQERYHRFRNDEAFLQQVMKDGAEKA 313
Cdd:PRK12284 239 DTEG----SALFQLYQAfATPEETAAFRQALADGIgWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAGAAKA 314
|
330
....*....|....*.
gi 41228 314 SAHASRTLKAVYQAIG 329
Cdd:PRK12284 315 RRIATPFLAELREAVG 330
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
6-281 |
1.93e-55 |
|
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: 181.73 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 6 VFSGAQPSGE-LTIGNYMGaLRQWVKMQD-DYHCIYCIVDQHAITV----------RQDAQKLRKATLDTLALYLACGID 73
Cdd:cd00395 2 LYCGIDPTADsLHIGHLIG-LLTFRRFQHaGHRPIFLIGGQTGIIGdpsgkksertLNDPEEVRQNIRRIAAQYLAVGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 74 --PEKSTIFVQSHVP---EHAQLGWALNCYTYFGELSRMTQFKDKSaryAENINAGLFDYPVLMAADILLYQT----NLV 144
Cdd:cd00395 81 edPTQATLFNNSDWPgplAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTtegcDIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 145 PVGEDQKQHLELSRDIAQRFNalygeIFKVPEPFIPksgARVMSLLEPtkKMSKSDDNRNNVIGLLEDPKSVVKKIKRAV 224
Cdd:cd00395 158 PGGSDQWGNITLGRELARRFN-----GFTIAEGLTI---PLVTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41228 225 tdsdeppvvrydvqnkagVSNLLDILSAVTGQSIPELEK----QFEGKMYGHLKGEVADAV 281
Cdd:cd00395 228 ------------------DSDVINILKYFTFLSKEEIERleqeQYEAPGYRVAQKTLAEEV 270
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
6-292 |
4.12e-24 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 101.09 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 6 VFSGAQPSGELTIGNYM--GALRQWVKMQDDyhcIY-CIVDQHAITVR-QDAQKLRKATLDTLALYLACGIDPEKSTIFV 81
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKMvfDELKWHQEFGAN---VYiPIADDEAYAARgLSWEETREWAYEYILDLIALGFDPDKTEIYF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 82 QS---HVPEHAQlgwalncytyfgELSRMTQFKDKSARY--AENINAGLFDYPVLMAADILLYQTN------LVPVGEDQ 150
Cdd:PRK12285 146 QSeniKVYDLAF------------ELAKKVNFSELKAIYgfTGETNIGHIFYPATQAADILHPQLEegpkptLVPVGIDQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 151 KQHLELSRDIAQRFNALYGeifkvpepFIPKSG--ARVMSLLEPTkKMSKSDDnrNNVIGLLEDPKSVVKKIKRAVT--- 225
Cdd:PRK12285 214 DPHIRLTRDIAERLHGGYG--------FIKPSStyHKFMPGLTGG-KMSSSKP--ESAIYLTDDPETVKKKIMKALTggr 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 226 -----------DSDEPPVVRYDVqnkagvsnLLDILSAvtgqsiPELEKQFE----GK-MYGHLKGEVADAVSGMLTELQ 289
Cdd:PRK12285 283 atleeqrklggEPDECVVYELLL--------YHLEEDD------KELKEIYEecrsGElLCGECKKEAAEKIAEFLKEHQ 348
|
...
gi 41228 290 ERY 292
Cdd:PRK12285 349 EKR 351
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
5-200 |
2.36e-13 |
|
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: 66.35 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 5 IVFSGAQPSGELTIGNY-----MGALRQWV-KMQDDYHCIYCIVDQHAITVRQDAQKlrkatldtlalylacGIDPEKST 78
Cdd:cd00802 1 TTFSGITPNGYLHIGHLrtivtFDFLAQAYrKLGYKVRCIALIDDAGGLIGDPANKK---------------GENAKAFV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 79 IFVqshvpehaqlgwalncytyfgelsrmtqfkdkSARYAEninagLFDYPVLMAADILLYQTN---LVPVGEDQKQHLE 155
Cdd:cd00802 66 ERW--------------------------------IERIKE-----DVEYMFLQAADFLLLYETecdIHLGGSDQLGHIE 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41228 156 LSRDIAQRFNalygeIFKVPEPFIPksgARVMSllEPTKKMSKSD 200
Cdd:cd00802 109 LGLELLKKAG-----GPARPFGLTF---GRVMG--ADGTKMSKSK 143
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
3-223 |
3.23e-08 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 54.10 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 3 KPIVFSGAQPSGELTIGNYMGAlRQWVKMQD-DYHCIYCIVDQHAI--------TVRQDAQKLRKAtldtlalYLACGID 73
Cdd:PRK08560 30 EPKAYIGFEPSGKIHLGHLLTM-NKLADLQKaGFKVTVLLADWHAYlndkgdleEIRKVAEYNKKV-------FEALGLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 74 PEKsTIFV-----QSHvPEHAQLGWALNCYTyfgELSRMTQFKDKSARYAENINAGLFDYPVLMAADILLYQTNLVPVGE 148
Cdd:PRK08560 102 PDK-TEFVlgsefQLD-KEYWLLVLKLAKNT---TLARARRSMTIMGRRMEEPDVSKLVYPLMQVADIFYLDVDIAVGGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 149 DQ-KQHLeLSRDIAQRFNalygeiFKVP----EPFIPksgarvmSLLEPTKKMSKSDDnrNNVIGLLEDPKSVVKKIKRA 223
Cdd:PRK08560 177 DQrKIHM-LAREVLPKLG------YKKPvcihTPLLT-------GLDGGGIKMSKSKP--GSAIFVHDSPEEIRRKIKKA 240
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
104-281 |
5.16e-08 |
|
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: 53.38 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 104 LSRMTQFKDKSARYAENINAGL--FDYPVLMAADILLYQTNLVPVGEDQKQHLELSRDIAQRFNalYGEIFKVPEPFIPK 181
Cdd:cd00805 113 VNRMLRRDAVKVRLEEEEGISFseFIYPLLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLG--YKKVVGLTTPLLTG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 182 SGArvmslleptKKMSKSDDNrNNVIGLLEDPKSVVKKIKRAvtdSDEPpvvrydvqnkagVSNLLDILSAVTGQSIPEL 261
Cdd:cd00805 191 LDG---------GKMSKSEGN-AIWDPVLDSPYDVYQKIRNA---FDPD------------VLEFLKLFTFLDYEEIEEL 245
|
170 180
....*....|....*....|.
gi 41228 262 EKQF-EGKMYGHLKGEVADAV 281
Cdd:cd00805 246 EEEHaEGPLPRDAKKALAEEL 266
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
128-307 |
5.76e-08 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 53.93 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 128 YPVLMAADILLYQTNLVPVGEDQKQHLELSRDiaqrfnalYGEIFKVPEPFIPKSGARVMSLLEPTKKMSKSDDnrNNVI 207
Cdd:PTZ00126 198 YPCMQCADIFYLKADICQLGMDQRKVNMLARE--------YCDKKKIKKKPIILSHHMLPGLLEGQEKMSKSDP--NSAI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 208 GLLEDPKSVVKKIKRA-----VTDSDepPVVRYDVQNKAGVSNLLDILSA------VTGQSIPELEKQF-EGKMY-GHLK 274
Cdd:PTZ00126 268 FMEDSEEDVNRKIKKAycppgVIEGN--PILAYFKSIVFPAFNSFTVLRKeknggdVTYTTYEELEKDYlSGALHpGDLK 345
|
170 180 190
....*....|....*....|....*....|....*.
gi 41228 275 GEVADAVSGMLTELqeRYHrFRNDE---AFLQQVMK 307
Cdd:PTZ00126 346 PALAKYLNLMLQPV--RDH-FQNNPeakSLLSEVKS 378
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
136-200 |
5.45e-04 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 39.06 E-value: 5.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41228 136 ILLYQTNLVPVGEDQKQHLELSRDiaqrfNALYGEIFKVPEPFIPKSGArvmsllEPTKKMSKSD 200
Cdd:cd02156 52 KESIEEDISVCGEDFQQNRELYRW-----VKDNITLPVDPEQVELPRLN------LETTVMSKRK 105
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
6-73 |
6.18e-04 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 38.67 E-value: 6.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41228 6 VFSGAQPsGELTIGNYMGaLRQWVKMQDdyHCIYCIVDQHAITVRQDAQKLRKATLDTLALYLACGID 73
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKL-ICRAKGIAD--QCVVRIDDNPPVKVWQDPHELEERKESIEEDISVCGED 65
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| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
128-310 |
9.92e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 37.57 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 128 YPVLMAADILLYQTNLVPVGEDQKQHLELSRDiaqrFNALYGEIFKvpePFIpKSGARVMSLLEPTKKMSKSDDnrNNVI 207
Cdd:PTZ00348 163 YPLMQCADIFFLKADICQLGLDQRKVNMLARE----YCDLIGRKLK---PVI-LSHHMLAGLKQGQAKMSKSDP--DSAI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41228 208 GLLEDPKSVVKKIKRA-----------VTDSDEP-------PVVRY---DVQNKAGVSNLLDilsAVTGQSIPELEKQF- 265
Cdd:PTZ00348 233 FMEDTEEDVARKIRQAycprvkqsaseITDDGAPvatddrnPVLDYfqcVVYARPGAVATID---GTTYATYEDLEQAFv 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 41228 266 EGKMYGH-LKGEVADAVSGMLTELqeRYHRFRNDEA--FLQQVM---KDGA 310
Cdd:PTZ00348 310 SDEVSEEaLKSCLIDEVNALLEPV--RQHFASNPEAheLLEAVKsyrKGGA 358
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