|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
11-339 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 597.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 11 KPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTIFVQ 90
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 91 SHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIAQ 170
Cdd:PRK00927 81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 171 RFNAIYGDIFTVPDPFIPKGGARVMALQDPAKKMSKSDDNRNNVIALLEDPKAAAKKIKRAVTDSEEPPRVAYDLENKAG 250
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 251 VSNLLDILAGVTGKTIPELEAEFE--GKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGADKAKARAQTT 328
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|.
gi 490366963 329 LDKVYEAIGFI 339
Cdd:PRK00927 321 LKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-339 |
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: 534.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 9 AQKPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTIF 88
Cdd:COG0180 1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 89 VQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARH-AENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRD 167
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 168 IAQRFNAIYGDIFTVPDPFIPKGGARVMALqDPAKKMSKSDdnrNNVIALLEDPKAAAKKIKRAVTDSEeppRVAYDLEN 247
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPEEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSE---RLRYDDPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 248 KAGVSNLLDILAGVTGK-TIPELEAEFE--GKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGADKAKAR 324
Cdd:COG0180 234 KPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAI 313
|
330
....*....|....*
gi 490366963 325 AQTTLDKVYEAIGFI 339
Cdd:COG0180 314 AAKTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
13-289 |
1.19e-132 |
|
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: 379.24 E-value: 1.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 13 IVFSGAQPSGELTIGNYMGALRQWVQMQD-DYDCIYCIVDQHAITVRQ-DPTELRKRTLDTLALYLACGIDPEKSTIFVQ 90
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 91 SHVPQHAQLGWALNCYTYFGELSRMTQFKDKSArHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIAQ 170
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 171 RFNAIYGDIFTVPDPFIPKgGARVMALQDPAKKMSKSDDnrNNVIALLEDPKAAAKKIKRAVTDSEEPPRvaYDLENKAG 250
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGGRTEH--RRDGGGPG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490366963 251 VSNLLDILAGVTGKTIPELEA----EFEGKMYGHLKGAVAEAV 289
Cdd:cd00806 235 VSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAI 277
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
11-338 |
5.78e-128 |
|
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: 368.97 E-value: 5.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 11 KPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQ-DPTELRKRTLDTLALYLACGIDPEKSTIFV 89
Cdd:TIGR00233 2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 90 QSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSarHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIA 169
Cdd:TIGR00233 82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 170 QRFNAIYGDIFTVPDPFIPKGGARVMALQDpaKKMSKSDDnrNNVIALLEDPKAAAKKIKRAVTDSEEPprVAYDLENKA 249
Cdd:TIGR00233 160 ERFNKKFKNFFPKPESLISKFFPRLMGLSG--KKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV--TLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 250 GVSNLLDILAGVTGKTIP------ELEAEFEGK-MYGHLKGAVAEAVSDMLTNIQERFNTFRNDEalLNKIMKEGADKAK 322
Cdd:TIGR00233 234 GVPNLLVIYQYLSFFLIDddklkeIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAEEI--LDKILEPGAKKAR 311
|
330
....*....|....*.
gi 490366963 323 ARAQTTLDKVYEAIGF 338
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
7-294 |
1.12e-86 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 262.98 E-value: 1.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 7 KKAQKPIVFSGAQPSGELTIGnYMGALRQWVQMQDD-YDCIYCIVDQHAITVRQD---PTELRKRTLDTLAL---YLACG 79
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 80 IDPEKSTIFVQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSAR--HAENINAGLFDYPVLMAADILLYQTNQVPVGID 157
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRleQGPGISLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 158 QKQHLELSRDIAQRFNaiyGDIFTVPDPFIPKggarVMALQDPAKKMSKSDDNRnnVIALLEDPKAAAKKIKRAVTDSEE 237
Cdd:pfam00579 160 QWGNIELGRDLARRFN---KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKAYTDPDR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366963 238 ppRVAYDLENKAGVSN-LLDILAGVTGKTIP----ELEAEFEGKM--YGHLKGAVAEAVSDMLT 294
Cdd:pfam00579 231 --EVRKDLKLFTFLSNeEIEILEAELGKSPYreaeELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
11-339 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 597.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 11 KPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTIFVQ 90
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 91 SHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIAQ 170
Cdd:PRK00927 81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 171 RFNAIYGDIFTVPDPFIPKGGARVMALQDPAKKMSKSDDNRNNVIALLEDPKAAAKKIKRAVTDSEEPPRVAYDLENKAG 250
Cdd:PRK00927 161 RFNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLREIRYDLPNKPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 251 VSNLLDILAGVTGKTIPELEAEFE--GKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGADKAKARAQTT 328
Cdd:PRK00927 241 VSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASKT 320
|
330
....*....|.
gi 490366963 329 LDKVYEAIGFI 339
Cdd:PRK00927 321 LKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
9-339 |
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: 534.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 9 AQKPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTIF 88
Cdd:COG0180 1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 89 VQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARH-AENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRD 167
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 168 IAQRFNAIYGDIFTVPDPFIPKGGARVMALqDPAKKMSKSDdnrNNVIALLEDPKAAAKKIKRAVTDSEeppRVAYDLEN 247
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPEEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSE---RLRYDDPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 248 KAGVSNLLDILAGVTGK-TIPELEAEFE--GKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGADKAKAR 324
Cdd:COG0180 234 KPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAI 313
|
330
....*....|....*
gi 490366963 325 AQTTLDKVYEAIGFI 339
Cdd:COG0180 314 AAKTLAEVREAMGLL 328
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
2-340 |
1.36e-137 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 396.11 E-value: 1.36e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 2 TTSVEKKAQKPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGID 81
Cdd:PLN02886 37 KEAPPKVARKKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 82 PEKSTIFVQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARH-AENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQ 160
Cdd:PLN02886 117 PSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 161 HLELSRDIAQRFNAIYG------------DIFTVPDPFIPKGGARVMALQDPAKKMSKSDDNRNNVIALLEDPKAAAKKI 228
Cdd:PLN02886 197 HLELTRDIAERVNNLYGgrkwkklggrggSVFKVPEALIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 229 KRAVTDSEepPRVAYDLENKAGVSNLLDILAGVTGKTIPELEAEFEGKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEA 308
Cdd:PLN02886 277 KRCKTDSF--PGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPS 354
|
330 340 350
....*....|....*....|....*....|..
gi 490366963 309 LLNKIMKEGADKAKARAQTTLDKVYEAIGFIA 340
Cdd:PLN02886 355 YLDSVLKEGADAAAEIADRTLANVYQAMGFVQ 386
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
13-289 |
1.19e-132 |
|
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: 379.24 E-value: 1.19e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 13 IVFSGAQPSGELTIGNYMGALRQWVQMQD-DYDCIYCIVDQHAITVRQ-DPTELRKRTLDTLALYLACGIDPEKSTIFVQ 90
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 91 SHVPQHAQLGWALNCYTYFGELSRMTQFKDKSArHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIAQ 170
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 171 RFNAIYGDIFTVPDPFIPKgGARVMALQDPAKKMSKSDDnrNNVIALLEDPKAAAKKIKRAVTDSEEPPRvaYDLENKAG 250
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGGRTEH--RRDGGGPG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490366963 251 VSNLLDILAGVTGKTIPELEA----EFEGKMYGHLKGAVAEAV 289
Cdd:cd00806 235 VSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAI 277
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
11-338 |
5.78e-128 |
|
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: 368.97 E-value: 5.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 11 KPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVRQ-DPTELRKRTLDTLALYLACGIDPEKSTIFV 89
Cdd:TIGR00233 2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 90 QSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSarHAENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIA 169
Cdd:TIGR00233 82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 170 QRFNAIYGDIFTVPDPFIPKGGARVMALQDpaKKMSKSDDnrNNVIALLEDPKAAAKKIKRAVTDSEEPprVAYDLENKA 249
Cdd:TIGR00233 160 ERFNKKFKNFFPKPESLISKFFPRLMGLSG--KKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV--TLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 250 GVSNLLDILAGVTGKTIP------ELEAEFEGK-MYGHLKGAVAEAVSDMLTNIQERFNTFRNDEalLNKIMKEGADKAK 322
Cdd:TIGR00233 234 GVPNLLVIYQYLSFFLIDddklkeIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAEEI--LDKILEPGAKKAR 311
|
330
....*....|....*.
gi 490366963 323 ARAQTTLDKVYEAIGF 338
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
10-337 |
4.11e-87 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 265.18 E-value: 4.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 10 QKPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAIT-VRQDPTELRKRTLDTLALYLACGIDPEKSTIF 88
Cdd:PRK12282 1 TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 89 VQSHVPQHAQLGWA-LNCYTyFGELSRMTQFKDKSARH--AENINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLELS 165
Cdd:PRK12282 81 IQSQIPELAELTMYyMNLVT-VARLERNPTVKTEIAQKgfGRSIPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 166 RDIAQRFNAIYG-DIFTVPDPFIPKGGaRVMALqDPAKKMSKSDdnrNNVIALLEDPKAAAKKIKRAVTDseePPRVAYD 244
Cdd:PRK12282 160 REIVRRFNSLYGtDVLVEPEALLPEAG-RLPGL-DGKAKMSKSL---GNAIYLSDDADTIKKKVMSMYTD---PNHIRVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 245 LENKAGVSNL---LDILAGvTGKTIPELEAEFEGKMYG--HLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGAD 319
Cdd:PRK12282 232 DPGKVEGNVVftyLDAFDP-DKAEVAELKAHYQRGGLGdvKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSE 310
|
330
....*....|....*...
gi 490366963 320 KAKARAQTTLDKVYEAIG 337
Cdd:PRK12282 311 KAREVAAQTLSEVKDAMG 328
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
7-294 |
1.12e-86 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 262.98 E-value: 1.12e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 7 KKAQKPIVFSGAQPSGELTIGnYMGALRQWVQMQDD-YDCIYCIVDQHAITVRQD---PTELRKRTLDTLAL---YLACG 79
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 80 IDPEKSTIFVQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSAR--HAENINAGLFDYPVLMAADILLYQTNQVPVGID 157
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRleQGPGISLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 158 QKQHLELSRDIAQRFNaiyGDIFTVPDPFIPKggarVMALQDPAKKMSKSDDNRnnVIALLEDPKAAAKKIKRAVTDSEE 237
Cdd:pfam00579 160 QWGNIELGRDLARRFN---KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKAYTDPDR 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366963 238 ppRVAYDLENKAGVSN-LLDILAGVTGKTIP----ELEAEFEGKM--YGHLKGAVAEAVSDMLT 294
Cdd:pfam00579 231 --EVRKDLKLFTFLSNeEIEILEAELGKSPYreaeELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
10-338 |
4.52e-82 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 252.34 E-value: 4.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 10 QKPIVFSGAQPSGELTIGNYMGALRQWVQMQDDYDC--IYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTI 87
Cdd:PRK12556 2 SEKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGkaLYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 88 FVQSHVPQHAQLGWALNCYTYFGELSRMTQFKDKSARHAE-------NINAGLFDYPVLMAADILLYQTNQVPVGIDQKQ 160
Cdd:PRK12556 82 YRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEagldldaGVNMGLYTYPILMAADILLFQATHVPVGKDQIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 161 HLELSRDIAQRFNAIYGDIFTVPDPFIPKGGARVMALQdpAKKMSKSDDnrnNVIALLEDPKAAAKKIKRAVTDSeEPPR 240
Cdd:PRK12556 162 HIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD--GRKMSKSYG---NVIPLFAEQEKLRKLIFKIKTDS-SLPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 241 VAYDLENkagvSNLLDILAG-VTGKTIPELEAEFEGKM-YGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGA 318
Cdd:PRK12556 236 EPKDPET----SALFTIYKEfATEEEVQSMREKYETGIgWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKGA 311
|
330 340
....*....|....*....|
gi 490366963 319 DKAKARAQTTLDKVYEAIGF 338
Cdd:PRK12556 312 ERAREIAKPNLAEIKKAIGF 331
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
14-337 |
8.50e-60 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 197.10 E-value: 8.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 14 VFSGAQPSGELTIGNYMGALRQWVQMQDDYDCIYCIVDQHAITVR-QDPTELRKRTLDTLALYLACGIDPEKSTIFVQSH 92
Cdd:PRK12283 5 VLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTTHyETPEVIEKNVWDMVIDWLAAGVDPAQATLFIQSK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 93 VPQHAQLGWALNCYTYFGELSRMTQFKDKSARHAENINA--GLFDYPVLMAADILLYQTNQVPVGIDQKQHLELSRDIAQ 170
Cdd:PRK12283 85 VPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKDLStyGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 171 RFNAIYGDIftvPDpF-------IPKGG-------------------------ARVM----------------------- 195
Cdd:PRK12283 165 RFNHLYGRE---PG-FeekaeaaIKKLGkkraklyhelrnayqeegddealeqARALlqeqqnlsmgdrerlfgylegag 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 196 --------ALQDPA--------KKMSKSddnRNNVIALLEDPKAAAKKIKRAVTDseePPRV------------------ 241
Cdd:PRK12283 241 kiilpepqALLTEAskmpgldgQKMSKS---YGNTIGLREDPESVTKKIRTMPTD---PARVrrtdpgdpekcpvwqlhq 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 242 AY-DLENKAGVSnlldilAGVTGKTIPELEAefegkmyghlKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGADK 320
Cdd:PRK12283 315 VYsDEETKEWVQ------KGCRSAGIGCLEC----------KQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEK 378
|
410
....*....|....*..
gi 490366963 321 AKARAQTTLDKVYEAIG 337
Cdd:PRK12283 379 ARKVARETMRDVREAMG 395
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
14-337 |
1.41e-59 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 197.53 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 14 VFSGAQPSGELTIGNYMGALRQWVQ--MQDDYDCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGIDPEKSTIFVQS 91
Cdd:PRK12284 5 VLTGITTTGTPHLGNYAGAIRPAIAasRQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 92 HVPQHAQLGWALNCYTYFGELSRMTQFK---DKSARHAE----NINAGLFDYPVLMAADILLYQTNQVPVGIDQKQHLEL 164
Cdd:PRK12284 85 DIPEIPELTWLLTCVAGKGLLNRAHAYKaavDKNVAAGEdpdaGVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 165 SRDIAQRFNAIYG-DIFTVPDPFIPKGGARVMALQdpAKKMSKSDDnrnNVIALLEDPKAAAKKIKRAVTDSEEPPRvAY 243
Cdd:PRK12284 165 ARDIAQRFNHLYGgEFFVLPEAVIEESVATLPGLD--GRKMSKSYD---NTIPLFAPREELKKAIFSIVTDSRAPGE-PK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 244 DLENkagvSNLLDILAGVTGktiPELEAEF-----EGKMYGHLKGAVAEAVSDMLTNIQERFNTFRNDEALLNKIMKEGA 318
Cdd:PRK12284 239 DTEG----SALFQLYQAFAT---PEETAAFrqalaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAGA 311
|
330
....*....|....*....
gi 490366963 319 DKAKARAQTTLDKVYEAIG 337
Cdd:PRK12284 312 AKARRIATPFLAELREAVG 330
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
14-289 |
2.60e-50 |
|
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: 169.02 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 14 VFSGAQPSGE-LTIGNYMGaLRQWVQMQD-DYDCIYCIVDQHAITV----------RQDPTELRKRTLDTLALYLACGID 81
Cdd:cd00395 2 LYCGIDPTADsLHIGHLIG-LLTFRRFQHaGHRPIFLIGGQTGIIGdpsgkksertLNDPEEVRQNIRRIAAQYLAVGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 82 --PEKSTIFVQSHVP---QHAQLGWALNCYTYFGELSRMTQFKDKSarhAENINAGLFDYPVLMAADILLYQTNQ----V 152
Cdd:cd00395 81 edPTQATLFNNSDWPgplAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 153 PVGIDQKQHLELSRDIAQRFNaiygdIFTVPDPFIPkggARVMALQDPakKMSKSDDNRNNVIALLEDPkaaakkikrav 232
Cdd:cd00395 158 PGGSDQWGNITLGRELARRFN-----GFTIAEGLTI---PLVTKLDGP--KFGKSESGPKWLDTEKTSP----------- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490366963 233 tdseepprvaYDLENK---AGVSNLLDILAGVTGKTIPELEA----EFEGKMYGHLKGAVAEAV 289
Cdd:cd00395 217 ----------YEFYQFwinAVDSDVINILKYFTFLSKEEIERleqeQYEAPGYRVAQKTLAEEV 270
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
14-221 |
1.55e-17 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 82.61 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 14 VFSGAQPSGELTIGNYMgALRQWVQMQDDYDCIY-CIVDQHAITVR-QDPTELRKRTLDTLALYLACGIDPEKSTIFVQS 91
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKM-VFDELKWHQEFGANVYiPIADDEAYAARgLSWEETREWAYEYILDLIALGFDPDKTEIYFQS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 92 HVPQHAQLGWALNCYTYFGELSRMTQFKDKSarhaeniNAGLFDYPVLMAADILLYQTNQ------VPVGIDQKQHLELS 165
Cdd:PRK12285 148 ENIKVYDLAFELAKKVNFSELKAIYGFTGET-------NIGHIFYPATQAADILHPQLEEgpkptlVPVGIDQDPHIRLT 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490366963 166 RDIAQRFNAIYGdiFTVPDP----FIP--KGGarvmalqdpakKMSKSDDnrNNVIALLEDP 221
Cdd:PRK12285 221 RDIAERLHGGYG--FIKPSStyhkFMPglTGG-----------KMSSSKP--ESAIYLTDDP 267
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
13-208 |
3.79e-10 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 57.49 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 13 IVFSGAQPSGELTIGNY-----MGALRQWVQMQD-DYDCIYCIVDQHAITVRQD--PTELRKRTLDtlalylacgidpek 84
Cdd:cd00802 1 TTFSGITPNGYLHIGHLrtivtFDFLAQAYRKLGyKVRCIALIDDAGGLIGDPAnkKGENAKAFVE-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 85 stifvqshvpqhaqlgwalncytyfgelsRMtqfkdkSARHAEninagLFDYPVLMAADILLYQTNQ---VPVGIDQKQH 161
Cdd:cd00802 67 -----------------------------RW------IERIKE-----DVEYMFLQAADFLLLYETEcdiHLGGSDQLGH 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490366963 162 LELSRDIAQRFNaiygdIFTVPDPFIPkggARVMAlqDPAKKMSKSD 208
Cdd:cd00802 107 IELGLELLKKAG-----GPARPFGLTF---GRVMG--ADGTKMSKSK 143
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
11-300 |
1.82e-09 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 58.34 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 11 KPIVFSGAQPSGELTIGNYMGAlRQWVQMQD-DYDCIYCIVDQHAITVRQDPTELRKRTLDTL-ALYLACGIDPEKsTIF 88
Cdd:PRK08560 30 EPKAYIGFEPSGKIHLGHLLTM-NKLADLQKaGFKVTVLLADWHAYLNDKGDLEEIRKVAEYNkKVFEALGLDPDK-TEF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 89 V-----QSHvPQHAQLGWALNCYTyfgELSRMTQFKDKSARHAENINAGLFDYPVLMAADILlYQTNQVPV-GIDQ-KQH 161
Cdd:PRK08560 108 VlgsefQLD-KEYWLLVLKLAKNT---TLARARRSMTIMGRRMEEPDVSKLVYPLMQVADIF-YLDVDIAVgGMDQrKIH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 162 LeLSRDIAQRFNaiygdiFTVP----DPFIPkggarvmALQDPAKKMSKSDDnrNNVIAlledpkaaakkikraVTDSEE 237
Cdd:PRK08560 183 M-LAREVLPKLG------YKKPvcihTPLLT-------GLDGGGIKMSKSKP--GSAIF---------------VHDSPE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 238 pprvayDLENK-------AGVSN---LLDILA--------------------GVTGKTIPELEAEF-EGKMygH---LKG 283
Cdd:PRK08560 232 ------EIRRKikkaycpPGEVEgnpVLEIAKyhifprydpfvierpekyggDLEYESYEELERDYaEGKL--HpmdLKN 303
|
330
....*....|....*..
gi 490366963 284 AVAEAVSDMLTNIQERF 300
Cdd:PRK08560 304 AVAEYLIEILEPVREYL 320
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
14-81 |
1.33e-06 |
|
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: 46.38 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490366963 14 VFSGAQPsGELTIGNYMGaLRQWVQMQDDydCIYCIVDQHAITVRQDPTELRKRTLDTLALYLACGID 81
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKL-ICRAKGIADQ--CVVRIDDNPPVKVWQDPHELEERKESIEEDISVCGED 65
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
6-221 |
2.16e-05 |
|
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: 45.85 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 6 EKKAQKPIVFSGAQPSG-ELTIGNY--MGALRQWVQMqdDYDCIYCIVDQHAITvrQDPT---ELRK-RTLDTLALY--- 75
Cdd:TIGR00234 26 KLLERPLKLYLGFDPTApSLHLGHLvpLLKLRDFQQA--GHEVIVLLGDFTALI--GDPTgksEVRKiLTREEVQENaen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 76 ----LACGIDPEKSTIFVQSHvpqhaqlgWALNC-YTYFGEL-------SRMTQFKDKSARHAENINAGLFDYPVLMAAD 143
Cdd:TIGR00234 102 ikkqIARFLDFEKAKFVYNSE--------WLLKLnYTDFIRLlgkiftvNRMLRRDAFSSRFEENISLHEFIYPLLQAYD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490366963 144 IL-LYQTNQVPvGIDQKQHLELSRDIAQRFNAIYGdiFTVPDPFIPKGGARVMALqDPAKKMSKSDDNRNNVIALLEDP 221
Cdd:TIGR00234 174 FVyLNVDLQLG-GSDQWFNIRKGRDLARENLPSLQ--FGLTVPLLTPADGEKMGK-SLGGAVSLDEGKYDFYQKVINTP 248
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
134-292 |
4.43e-05 |
|
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: 44.52 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 134 FDYPVLMAADIL-LYQTNQVPvGIDQKQHLELSRDIAQRFNaiYGDIFTVPDPFIPKggarvmaLQdpAKKMSKSDDNrN 212
Cdd:cd00805 137 FIYPLLQAYDFVyLDVDLQLG-GSDQRGNITLGRDLIRKLG--YKKVVGLTTPLLTG-------LD--GGKMSKSEGN-A 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366963 213 NVIALLEDPkaaakkikravtdseepprvaYDLENK------AGVSNLLDILAGVTGKTIPELEAEF-EGKMYGHLKGAV 285
Cdd:cd00805 204 IWDPVLDSP---------------------YDVYQKirnafdPDVLEFLKLFTFLDYEEIEELEEEHaEGPLPRDAKKAL 262
|
....*..
gi 490366963 286 AEAVSDM 292
Cdd:cd00805 263 AEELTKL 269
|
|
| |
