|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
11-337 |
2.53e-165 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 463.79 E-value: 2.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 11 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 90
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYEC-FFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 91 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLA 170
Cdd:PRK00927 80 QSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 171 QGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRA 247
Cdd:PRK00927 160 RRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 325
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 1804892010 326 VCQEVKKLVGFL 337
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
10-337 |
2.27e-158 |
|
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: 446.03 E-value: 2.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILF 89
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYEC-FFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 90 QQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 168
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 169 LAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRA 247
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAY 324
Cdd:COG0180 236 EVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAA 315
|
330
....*....|...
gi 1804892010 325 TVCQEVKKLVGFL 337
Cdd:COG0180 316 KTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
13-289 |
1.47e-133 |
|
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: 381.16 E-value: 1.47e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 13 RVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSILFQQ 91
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 92 SQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 171
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 172 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN 251
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1804892010 252 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 289
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
10-336 |
1.43e-100 |
|
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: 299.25 E-value: 1.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVlYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSIL 88
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELF-ICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 89 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 168
Cdd:TIGR00233 80 FLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 169 LAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRA 247
Cdd:TIGR00233 158 LAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAK 320
Cdd:TIGR00233 234 GVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKAR 311
|
330
....*....|....*.
gi 1804892010 321 ELAYTVCQEVKKLVGF 336
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
7-292 |
1.93e-67 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 213.29 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 7 TKDSKKRVFSGIQPTGILHLGnYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAV---LRQSILDMTAV---LLACG 80
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPerkLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 81 INPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 158
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 159 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 238
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804892010 239 VTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 292
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
11-337 |
2.53e-165 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 463.79 E-value: 2.53e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 11 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 90
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYEC-FFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 91 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLA 170
Cdd:PRK00927 80 QSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 171 QGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPAGRA 247
Cdd:PRK00927 160 RRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 325
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 1804892010 326 VCQEVKKLVGFL 337
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
10-337 |
2.27e-158 |
|
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: 446.03 E-value: 2.27e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILF 89
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYEC-FFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 90 QQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 168
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 169 LAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPAGRA 247
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAY 324
Cdd:COG0180 236 EVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAA 315
|
330
....*....|...
gi 1804892010 325 TVCQEVKKLVGFL 337
Cdd:COG0180 316 KTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
13-289 |
1.47e-133 |
|
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: 381.16 E-value: 1.47e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 13 RVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSILFQQ 91
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 92 SQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 171
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 172 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRAGVSN 251
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1804892010 252 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 289
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
11-337 |
2.81e-112 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 331.39 E-value: 2.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 11 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 90
Cdd:PLN02886 46 KKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDT-FFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 91 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQ-KHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 169
Cdd:PLN02886 125 QSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 170 AQGFNKKYG------------EFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT 236
Cdd:PLN02886 205 AERVNNLYGgrkwkklggrggSVFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 237 SEVTYDPAGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGS 316
Cdd:PLN02886 285 PGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGA 364
|
330 340
....*....|....*....|.
gi 1804892010 317 AKAKELAYTVCQEVKKLVGFL 337
Cdd:PLN02886 365 DAAAEIADRTLANVYQAMGFV 385
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
10-336 |
1.43e-100 |
|
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: 299.25 E-value: 1.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVlYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSIL 88
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELF-ICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 89 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 168
Cdd:TIGR00233 80 FLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 169 LAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPAGRA 247
Cdd:TIGR00233 158 LAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 248 GVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAK 320
Cdd:TIGR00233 234 GVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKAR 311
|
330
....*....|....*.
gi 1804892010 321 ELAYTVCQEVKKLVGF 336
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
10-335 |
1.09e-74 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 233.21 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYsIVDLHSIT-VPQDPAVLRQSILDMTAVLLACGINPEKSIL 88
Cdd:PRK12282 1 TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVL-IADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 89 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtKQKHDG---TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMEL 165
Cdd:PRK12282 80 FIQSQIPELAELTMYYMNLVTVARLERNPTVKTEI-AQKGFGrsiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 166 VQDLAQGFNKKYG-EFFPVPESILTSMKKVKSLrDPSAKMSKSDPDKLAtvrITDSPEEIVQKFRKAVTDfTSEVTYDPA 244
Cdd:PRK12282 159 TREIVRRFNSLYGtDVLVEPEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMYTD-PNHIRVEDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 245 GRAGVSNIVAVHAAV--TGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAK 320
Cdd:PRK12282 234 GKVEGNVVFTYLDAFdpDKAEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKAR 313
|
330
....*....|....*
gi 1804892010 321 ELAYTVCQEVKKLVG 335
Cdd:PRK12282 314 EVAAQTLSEVKDAMG 328
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
7-292 |
1.93e-67 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 213.29 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 7 TKDSKKRVFSGIQPTGILHLGnYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAV---LRQSILDMTAV---LLACG 80
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPerkLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 81 INPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 158
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 159 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 238
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1804892010 239 VTYDPAGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 292
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
9-336 |
2.20e-67 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 214.59 E-value: 2.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 9 DSKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSV-LYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSI 87
Cdd:PRK12556 1 MSEKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGKaLYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 88 LFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQV 160
Cdd:PRK12556 81 FYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEAGldldagvNMGLYTYPILMAADILLFQATHVPVGKDQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 161 QHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFT-SEV 239
Cdd:PRK12556 161 QHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD-GRKMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSSlPNE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 240 TYDPAGragvSNIVAVHAA-VTGLSVEEV-VRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSA 317
Cdd:PRK12556 237 PKDPET----SALFTIYKEfATEEEVQSMrEKYETGIGWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKGAE 312
|
330
....*....|....*....
gi 1804892010 318 KAKELAYTVCQEVKKLVGF 336
Cdd:PRK12556 313 RAREIAKPNLAEIKKAIGF 331
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
10-335 |
1.59e-57 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 190.93 E-value: 1.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVP-QDPAVLRQSILDMTAVLLACGINPEKSIL 88
Cdd:PRK12283 1 FPDRVLSGMRPTGRLHLGHYHGVLKNWVKLQHEYEC-FFFVADWHALTTHyETPEVIEKNVWDMVIDWLAAGVDPAQATL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 89 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD--GTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELV 166
Cdd:PRK12283 80 FIQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 167 QDLAQGFNKKYG-------------------------------------------------------------------- 178
Cdd:PRK12283 160 REIARRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqarallqeqqnlsmgdrerlfgylega 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 179 --EFFPVPESILTSMKKVKSLrDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFTSEVTYDPaGRAGVSNIVAVH 256
Cdd:PRK12283 240 gkIILPEPQALLTEASKMPGL-D-GQKMSKSYGN---TIGLREDPESVTKKIRTMPTDPARVRRTDP-GDPEKCPVWQLH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 257 AAVTGLSVEEVVR---RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKL 333
Cdd:PRK12283 314 QVYSDEETKEWVQkgcRSAGIGCLECKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREA 393
|
..
gi 1804892010 334 VG 335
Cdd:PRK12283 394 MG 395
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
13-335 |
3.59e-50 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 172.50 E-value: 3.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 13 RVFSGIQPTGILHLGNYLGAIESWVR--LQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 90
Cdd:PRK12284 4 RVLTGITTTGTPHLGNYAGAIRPAIAasRQPGVES-FYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 91 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHM 163
Cdd:PRK12284 83 QSDIPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 164 ELVQDLAQGFNKKYG-EFFPVPESILTsmKKVKSL-----RdpsaKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDftS 237
Cdd:PRK12284 163 EMARDIAQRFNHLYGgEFFVLPEAVIE--ESVATLpgldgR----KMSKSYDN---TIPLFAPREELKKAIFSIVTD--S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 238 EVTYDPAGRAGvSNIVAVHAAVTGLSVEEVVRRS--AGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIG 315
Cdd:PRK12284 232 RAPGEPKDTEG-SALFQLYQAFATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAG 310
|
330 340
....*....|....*....|
gi 1804892010 316 SAKAKELAYTVCQEVKKLVG 335
Cdd:PRK12284 311 AAKARRIATPFLAELREAVG 330
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
14-289 |
2.35e-33 |
|
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: 124.34 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 14 VFSGIQPTG-ILHLGNYLGaIESWVRLQDEYDSVLYSIVDLHSITV----------PQDPAVLRQSILDMTAVLLACGI- 81
Cdd:cd00395 2 LYCGIDPTAdSLHIGHLIG-LLTFRRFQHAGHRPIFLIGGQTGIIGdpsgkksertLNDPEEVRQNIRRIAAQYLAVGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 82 -NPEKSILFQQSQV---SEHTQLSWILSCMVRLPRLQHLHQWKAKTtkqKHDGTVGLLTYPVLQAADILLYKSTH----V 153
Cdd:cd00395 81 eDPTQATLFNNSDWpgpLAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 154 PVGEDQVQHMELVQDLAQGFNkkygeFFPVPESILTSMkkVKSLRDPsaKMSKSDPDKLATVRITDSPEEIVQKFRKAVt 233
Cdd:cd00395 158 PGGSDQWGNITLGRELARRFN-----GFTIAEGLTIPL--VTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 234 dftsevtydpagragVSNIVAVHAAVTGLSVEEVVRRSAGMNTAR----YKLAVADAVIE 289
Cdd:cd00395 228 ---------------DSDVINILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
14-233 |
8.86e-21 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 91.85 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 14 VFSGIQPTGILHLGNYLGAIESwVRLQDEYDSVLYSIVDLHS-----ITVPQDPAVLRQSILDmtavLLACGINPEKSIL 88
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKMVFDEL-KWHQEFGANVYIPIADDEAyaargLSWEETREWAYEYILD----LIALGFDPDKTEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 89 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTkqkhdgtVGLLTYPVLQAADILL------YKSTHVPVGEDQVQH 162
Cdd:PRK12285 144 YFQSENIKVYDLAFELAKKVNFSELKAIYGFTGETN-------IGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPH 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1804892010 163 MELVQDLAQGFNKKYGefFPVPESILtsMKKVKSLRdpSAKMSKSDPDklATVRITDSPEEIVQKFRKAVT 233
Cdd:PRK12285 217 IRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKMSSSKPE--SAIYLTDDPETVKKKIMKALT 279
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
10-231 |
5.93e-12 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 65.66 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 10 SKKRVFSGIQPTGILHLGNYLgaiesWVR----LQDE-YDSVLYsIVDLHS-ITVPQDPAVLRQSILDMTAVLLACGINP 83
Cdd:PRK08560 29 EEPKAYIGFEPSGKIHLGHLL-----TMNkladLQKAgFKVTVL-LADWHAyLNDKGDLEEIRKVAEYNKKVFEALGLDP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 84 EKS--IL---FQQSqvSEHTQLSWILSCMVRLPRLQHlhqwkAKT--TKQKHDGTVGLLTYPVLQAADILlYKSTHVPV- 155
Cdd:PRK08560 103 DKTefVLgseFQLD--KEYWLLVLKLAKNTTLARARR-----SMTimGRRMEEPDVSKLVYPLMQVADIF-YLDVDIAVg 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804892010 156 GEDQVQ-HMeLVQDLAQGFNkkygefFPVPESILTSMkkVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKA 231
Cdd:PRK08560 175 GMDQRKiHM-LAREVLPKLG------YKKPVCIHTPL--LTGLDGGGIKMSKSKPG--SAIFVHDSPEEIRRKIKKA 240
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
72-244 |
1.75e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 49.52 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 72 MTAVLLACGINPEKSI-LFQQSQVSEHTQLSWILscMVRLPRLQHLHQWKAKTT---KQKHDGTVGLLTYPVLQAADILL 147
Cdd:PTZ00348 96 LIEVWKAAGMDMDKVLfLWSSEEITNHANTYWRT--VLDIGRQNTIARIKKCCTimgKTEGTLTAAQVLYPLMQCADIFF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 148 YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpvpESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQK 227
Cdd:PTZ00348 174 LKADICQLGLDQRKVNMLAREYCDLIGRKL-------KPVILSHHMLAGLKQGQAKMSKSDPD--SAIFMEDTEEDVARK 244
|
170 180
....*....|....*....|.
gi 1804892010 228 FRKA----VTDFTSEVTYDPA 244
Cdd:PTZ00348 245 IRQAycprVKQSASEITDDGA 265
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
135-231 |
8.31e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 46.99 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 135 LTYPVLQAADILLYKSTHVPVGEDQVQhmelVQDLAqgfnKKYGEFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDklA 213
Cdd:PTZ00126 196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLA----REYCDKKKIKKKpIILSHHMLPGLLEGQEKMSKSDPN--S 265
|
90
....*....|....*...
gi 1804892010 214 TVRITDSPEEIVQKFRKA 231
Cdd:PTZ00126 266 AIFMEDSEEDVNRKIKKA 283
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
6-270 |
1.65e-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: 46.24 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 6 TTKDSKKRVFSGIQPTGI-LHLGNYLgAIESWVRLQDEYDSVLYSIVDLHS-ITVPQDPAVLRQsILDMTAVL------- 76
Cdd:TIGR00234 26 KLLERPLKLYLGFDPTAPsLHLGHLV-PLLKLRDFQQAGHEVIVLLGDFTAlIGDPTGKSEVRK-ILTREEVQenaenik 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 77 --LACGINPEKSILFQQSqvsehtqlSWILSC----MVR-LPRLQHLHQWKAK---TTKQKHDGTVGLLTYPVLQAADIL 146
Cdd:TIGR00234 104 kqIARFLDFEKAKFVYNS--------EWLLKLnytdFIRlLGKIFTVNRMLRRdafSSRFEENISLHEFIYPLLQAYDFV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 147 -LYKSTHVPvGEDQVQHMELVQDLAQGFNKKYGEFFPVPesILTSMKKVKSLRDPSAKMSkSDPDKLAT-VRITDSPEEI 224
Cdd:TIGR00234 176 yLNVDLQLG-GSDQWFNIRKGRDLARENLPSLQFGLTVP--LLTPADGEKMGKSLGGAVS-LDEGKYDFyQKVINTPDEL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1804892010 225 VQKFRKAVTDFTSEVTYDpagragVSNIVAVHA-AVTGLSVEEVVRR 270
Cdd:TIGR00234 252 VKKYLKLFTFLGLEEIEQ------LVELKGPNPrEVKENLALEITKY 292
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
12-231 |
3.77e-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: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 12 KRVFSGIQPTGI-LHLGNYLgAIESWVRLQDEYDSVLYSIVDLHS-ITVPQDPAVLRqSILDMTAVLLACginpeKSILF 89
Cdd:cd00805 1 LKVYIGFDPTAPsLHLGHLV-PLMKLRDFQQAGHEVIVLIGDATAmIGDPSGKSEER-KLLDLELIRENA-----KYYKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 90 Q-----QSQVSEHTQL----SWILSC----MVRLPRLQHLHQWKAK-TTKQKHDGTVGL----LTYPVLQAADIL-LYKS 150
Cdd:cd00805 74 QlkailDFIPPEKAKFvnnsDWLLSLytldFLRLGKHFTVNRMLRRdAVKVRLEEEEGIsfseFIYPLLQAYDFVyLDVD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 151 THVPvGEDQVQHMELVQDLAQGFNKK--YGEFFPvpesILTSMKkvkslrdpSAKMSKSDPDKlATVRITDSPEEIVQKF 228
Cdd:cd00805 154 LQLG-GSDQRGNITLGRDLIRKLGYKkvVGLTTP----LLTGLD--------GGKMSKSEGNA-IWDPVLDSPYDVYQKI 219
|
...
gi 1804892010 229 RKA 231
Cdd:cd00805 220 RNA 222
|
|
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
76-230 |
8.07e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 40.88 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 76 LLACGINPEKSILFQQSQ-VSehtqlSWILSCMVRLprlqhlhqWKAKTTKQKH-----DGT--VGLLTYPVLQAA---- 143
Cdd:PLN02486 140 IIACGFDVERTFIFSDFDyVG-----GAFYKNMVKI--------AKCVTLNQVRgifgfSGEdnIGKISFPAVQAApsfp 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 144 ---DILLYKSTH----VPVGEDQVQHMELVQDLAQ--GFNKK---YGEFFPvpesiltsmkkvkSLRDPSAKMSKSDPDk 211
Cdd:PLN02486 207 ssfPHLFGGKDKlrclIPCAIDQDPYFRMTRDVAPrlGYYKPaliESRFFP-------------ALQGESGKMSASDPN- 272
|
170
....*....|....*....
gi 1804892010 212 lATVRITDSPEEIVQKFRK 230
Cdd:PLN02486 273 -SAIYVTDTPKEIKNKINK 290
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
14-80 |
1.80e-03 |
|
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: 37.52 E-value: 1.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1804892010 14 VFSGIQPtGILHLGNYLGaIESWVRLQDEydsVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACG 80
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKL-ICRAKGIADQ---CVVRIDDNPPVKVWQDPHELEERKESIEEDISVCG 63
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
14-208 |
2.11e-03 |
|
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: 37.84 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 14 VFSGIQPTGILHLGNYLGAIeSWVRLQDEYDSVLYSIVDLHSITvPQDPAVLRQSIldmtavllACGINPEKsilfqqsq 93
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIV-TFDFLAQAYRKLGYKVRCIALID-DAGGLIGDPAN--------KKGENAKA-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1804892010 94 vsehtqlswilscMVRlprlqhlhQWKAKTTKQkhdgtvglLTYPVLQAADILL---YKSTHVPVGEDQVQHMELVQDLA 170
Cdd:cd00802 64 -------------FVE--------RWIERIKED--------VEYMFLQAADFLLlyeTECDIHLGGSDQLGHIELGLELL 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 1804892010 171 QGFNKKYgeffpVPESILTSMKKVKSLRdpsaKMSKSD 208
Cdd:cd00802 115 KKAGGPA-----RPFGLTFGRVMGADGT----KMSKSK 143
|
|
| |
