|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
5-331 |
5.28e-166 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 465.33 E-value: 5.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 5 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 84
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYEC-FFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 85 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLA 164
Cdd:PRK00927 80 QSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 165 QGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPPGRA 241
Cdd:PRK00927 160 RRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 319
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 2462502115 320 VCQEVKKLVGFL 331
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-331 |
1.36e-159 |
|
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: 448.73 E-value: 1.36e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILF 83
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYEC-FFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 84 QQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 162
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 163 LAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPPGRA 241
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAY 318
Cdd:COG0180 236 EVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAA 315
|
330
....*....|...
gi 2462502115 319 TVCQEVKKLVGFL 331
Cdd:COG0180 316 KTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
7-283 |
3.80e-134 |
|
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: 382.70 E-value: 3.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 7 RVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSILFQQ 85
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 86 SQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 165
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 166 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPPGRAGVSN 245
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462502115 246 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 283
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
4-330 |
3.60e-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: 298.09 E-value: 3.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVlYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSIL 82
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELF-ICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 83 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 162
Cdd:TIGR00233 80 FLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 163 LAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPPGRA 241
Cdd:TIGR00233 158 LAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAK 314
Cdd:TIGR00233 234 GVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKAR 311
|
330
....*....|....*.
gi 2462502115 315 ELAYTVCQEVKKLVGF 330
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
1-286 |
3.71e-68 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 214.83 E-value: 3.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 1 MKDSKKRVFSGIQPTGILHLGnYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAV---LRQSILDMTAV---LLACG 74
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPerkLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 75 INPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 152
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 153 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 232
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462502115 233 VTYDPPGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 286
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
5-331 |
5.28e-166 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 465.33 E-value: 5.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 5 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 84
Cdd:PRK00927 1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYEC-FFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 85 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLA 164
Cdd:PRK00927 80 QSHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 165 QGFNKKYGEFFPVPESILTSMK-KVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT--SEVTYDPPGRA 241
Cdd:PRK00927 160 RRFNNLYGEVFPVPEPLIPKVGaRVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSErlREIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVTGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYT 319
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAeyEAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 2462502115 320 VCQEVKKLVGFL 331
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
4-331 |
1.36e-159 |
|
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: 448.73 E-value: 1.36e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILF 83
Cdd:COG0180 2 SKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYEC-FFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 84 QQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 162
Cdd:COG0180 81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKENvNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 163 LAQGFNKKYGEFFPVPESILT-SMKKVKSLrDPSAKMSKSDpdkLATVRITDSPEEIVQKFRKAVTDfTSEVTYDPPGRA 241
Cdd:COG0180 161 IARRFNHRYGEVFPEPEALIPeEGARIPGL-DGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTD-SERLRYDDPGKP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVTG-LSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAY 318
Cdd:COG0180 236 EVCNLFTIYSAFSGkEEVEELEAeyRAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAA 315
|
330
....*....|...
gi 2462502115 319 TVCQEVKKLVGFL 331
Cdd:COG0180 316 KTLAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
7-283 |
3.80e-134 |
|
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: 382.70 E-value: 3.80e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 7 RVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSILFQQ 85
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 86 SQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDgTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDLAQ 165
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESV-NIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 166 GFNKKYGEFFPVPESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPPGRAGVSN 245
Cdd:cd00806 160 RFNKLYGEIFPKPAALLSKGAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462502115 246 IVAVHAAVTGLSVEEVVR----RSAGMNTARYKLAVADAVIE 283
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
5-331 |
1.79e-113 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 334.09 E-value: 1.79e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 5 KKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 84
Cdd:PLN02886 46 KKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDT-FFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 85 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQ-KHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQDL 163
Cdd:PLN02886 125 QSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 164 AQGFNKKYG------------EFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDKLATVRITDSPEEIVQKFRKAVTDFT 230
Cdd:PLN02886 205 AERVNNLYGgrkwkklggrggSVFKVPEAlIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 231 SEVTYDPPGRAGVSNIVAVHAAVTGLSVEEVVRRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGS 310
Cdd:PLN02886 285 PGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGA 364
|
330 340
....*....|....*....|.
gi 2462502115 311 AKAKELAYTVCQEVKKLVGFL 331
Cdd:PLN02886 365 DAAAEIADRTLANVYQAMGFV 385
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
4-330 |
3.60e-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: 298.09 E-value: 3.60e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVlYSIVDLHSITVPQ-DPAVLRQSILDMTAVLLACGINPEKSIL 82
Cdd:TIGR00233 1 KKFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELF-ICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 83 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtkQKHDGTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELVQD 162
Cdd:TIGR00233 80 FLQSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 163 LAQGFNKKYGEFFPVPESILT-SMKKVKSLRDpsAKMSKSDPDklATVRITDSPEEIVQKFRKAVTDFTSEVTYDPPGRA 241
Cdd:TIGR00233 158 LAERFNKKFKNFFPKPESLISkFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 242 GVSNIVAVHAAVT-----GLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEklKLDKDHLEKVLQIGSAKAK 314
Cdd:TIGR00233 234 GVPNLLVIYQYLSfflidDDKLKEIYEayKSGKLGYGECKKALIEVLQEFLKEIQERRA--EIAEEILDKILEPGAKKAR 311
|
330
....*....|....*.
gi 2462502115 315 ELAYTVCQEVKKLVGF 330
Cdd:TIGR00233 312 ETANKTLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
4-329 |
3.47e-76 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 237.06 E-value: 3.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSVLYsIVDLHSIT-VPQDPAVLRQSILDMTAVLLACGINPEKSIL 82
Cdd:PRK12282 1 TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVL-IADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 83 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTtKQKHDG---TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMEL 159
Cdd:PRK12282 80 FIQSQIPELAELTMYYMNLVTVARLERNPTVKTEI-AQKGFGrsiPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 160 VQDLAQGFNKKYG-EFFPVPESILTSMKKVKSLrDPSAKMSKSDPDKLAtvrITDSPEEIVQKFRKAVTDfTSEVTYDPP 238
Cdd:PRK12282 159 TREIVRRFNSLYGtDVLVEPEALLPEAGRLPGL-DGKAKMSKSLGNAIY---LSDDADTIKKKVMSMYTD-PNHIRVEDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 239 GRAGVSNIVAVHAAV--TGLSVEEVVR--RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAK 314
Cdd:PRK12282 234 GKVEGNVVFTYLDAFdpDKAEVAELKAhyQRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKAR 313
|
330
....*....|....*
gi 2462502115 315 ELAYTVCQEVKKLVG 329
Cdd:PRK12282 314 EVAAQTLSEVKDAMG 328
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
1-286 |
3.71e-68 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 214.83 E-value: 3.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 1 MKDSKKRVFSGIQPTGILHLGnYLGAIESWVRLQDEYDSVLYSIVDLHSITVPQDPAV---LRQSILDMTAV---LLACG 74
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPerkLLSRETVLENAikaQLACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 75 INPEKSILFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG--TVGLLTYPVLQAADILLYKSTHVPVGED 152
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGPgiSLGEFTYPLLQAYDILLLKADLQPGGSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 153 QVQHMELVQDLAQGFNKKygeFFPVPESILTsmkKVKSLRDPSAKMSKSDPdkLATVRITDSPEEIVQKFRKAVTDFTSE 232
Cdd:pfam00579 160 QWGNIELGRDLARRFNKK---IFKKPVGLTN---PLLTGLDGGKKMSKSAG--NSAIFLDDDPESVYKKIQKAYTDPDRE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462502115 233 VTYDPPGRAGVSN-IVAVHAAVTGLSV---------EEVVRRSAGMNtarYKLAVADAVIEKFA 286
Cdd:pfam00579 232 VRKDLKLFTFLSNeEIEILEAELGKSPyreaeellaREVTGLVHGGD---LKKAAAEAVNKLLQ 292
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
3-330 |
6.00e-68 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 215.74 E-value: 6.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 3 DSKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSV-LYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSI 81
Cdd:PRK12556 1 MSEKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGKaLYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 82 LFQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQV 154
Cdd:PRK12556 81 FYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEAGldldagvNMGLYTYPILMAADILLFQATHVPVGKDQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 155 QHMELVQDLAQGFNKKYGEFFPVPESILTSMKKVKSLRDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDFTsevt 234
Cdd:PRK12556 161 QHIEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGLD-GRKMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSS---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 235 ydPPGRAGVSNIVAVHAAVTGLSVEEVV-----RRSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIG 309
Cdd:PRK12556 233 --LPNEPKDPETSALFTIYKEFATEEEVqsmreKYETGIGWGDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKG 310
|
330 340
....*....|....*....|.
gi 2462502115 310 SAKAKELAYTVCQEVKKLVGF 330
Cdd:PRK12556 311 AERAREIAKPNLAEIKKAIGF 331
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
4-329 |
6.99e-59 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 194.40 E-value: 6.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLGAIESWVRLQDEYDSvLYSIVDLHSITVP-QDPAVLRQSILDMTAVLLACGINPEKSIL 82
Cdd:PRK12283 1 FPDRVLSGMRPTGRLHLGHYHGVLKNWVKLQHEYEC-FFFVADWHALTTHyETPEVIEKNVWDMVIDWLAAGVDPAQATL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 83 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHD--GTVGLLTYPVLQAADILLYKSTHVPVGEDQVQHMELV 160
Cdd:PRK12283 80 FIQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 161 QDLAQGFNKKYG-------------------------------------------------------------------- 172
Cdd:PRK12283 160 REIARRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddealeqarallqeqqnlsmgdrerlfgylega 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 173 --EFFPVPESILTSMKKVKSLrDpSAKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDfTSEVTYDPPGRAGVSNIVAVH 250
Cdd:PRK12283 240 gkIILPEPQALLTEASKMPGL-D-GQKMSKSYGN---TIGLREDPESVTKKIRTMPTD-PARVRRTDPGDPEKCPVWQLH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 251 AAVTGLSVEEVVR---RSAGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIGSAKAKELAYTVCQEVKKL 327
Cdd:PRK12283 314 QVYSDEETKEWVQkgcRSAGIGCLECKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVREA 393
|
..
gi 2462502115 328 VG 329
Cdd:PRK12283 394 MG 395
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
7-329 |
3.36e-50 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 172.50 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 7 RVFSGIQPTGILHLGNYLGAIESWVR--LQDEYDSvLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACGINPEKSILFQ 84
Cdd:PRK12284 4 RVLTGITTTGTPHLGNYAGAIRPAIAasRQPGVES-FYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 85 QSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTKQKHDG-------TVGLLTYPVLQAADILLYKSTHVPVGEDQVQHM 157
Cdd:PRK12284 83 QSDIPEIPELTWLLTCVAGKGLLNRAHAYKAAVDKNVAAGedpdagvTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 158 ELVQDLAQGFNKKYG-EFFPVPESILTsmKKVKSL-----RdpsaKMSKSDPDklaTVRITDSPEEIVQKFRKAVTDftS 231
Cdd:PRK12284 163 EMARDIAQRFNHLYGgEFFVLPEAVIE--ESVATLpgldgR----KMSKSYDN---TIPLFAPREELKKAIFSIVTD--S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 232 EVTYDPPGRAGvSNIVAVHAAVTGLSVEEVVRRS--AGMNTARYKLAVADAVIEKFAPIKREIEKLKLDKDHLEKVLQIG 309
Cdd:PRK12284 232 RAPGEPKDTEG-SALFQLYQAFATPEETAAFRQAlaDGIGWGDAKQRLFERIDRELAPMRERYEALIARPADIEDILLAG 310
|
330 340
....*....|....*....|
gi 2462502115 310 SAKAKELAYTVCQEVKKLVG 329
Cdd:PRK12284 311 AAKARRIATPFLAELREAVG 330
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
8-283 |
2.24e-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: 2.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 8 VFSGIQPTG-ILHLGNYLGaIESWVRLQDEYDSVLYSIVDLHSITV----------PQDPAVLRQSILDMTAVLLACGI- 75
Cdd:cd00395 2 LYCGIDPTAdSLHIGHLIG-LLTFRRFQHAGHRPIFLIGGQTGIIGdpsgkksertLNDPEEVRQNIRRIAAQYLAVGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 76 -NPEKSILFQQSQV---SEHTQLSWILSCMVRLPRLQHLHQWKAKTtkqKHDGTVGLLTYPVLQAADILLYKSTH----V 147
Cdd:cd00395 81 eDPTQATLFNNSDWpgpLAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 148 PVGEDQVQHMELVQDLAQGFNkkygeFFPVPESILTSMkkVKSLRDPsaKMSKSDPDKLATVRITDSPEEIVQKFRKAVt 227
Cdd:cd00395 158 PGGSDQWGNITLGRELARRFN-----GFTIAEGLTIPL--VTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 228 dftsevtydppgragVSNIVAVHAAVTGLSVEEVVRRSAGMNTAR----YKLAVADAVIE 283
Cdd:cd00395 228 ---------------DSDVINILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
8-227 |
1.07e-20 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 91.46 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 8 VFSGIQPTGILHLGNYLGAIESwVRLQDEYDSVLYSIVDLHS-----ITVPQDPAVLRQSILDmtavLLACGINPEKSIL 82
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKMVFDEL-KWHQEFGANVYIPIADDEAyaargLSWEETREWAYEYILD----LIALGFDPDKTEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 83 FQQSQVSEHTQLSWILSCMVRLPRLQHLHQWKAKTTkqkhdgtVGLLTYPVLQAADILL------YKSTHVPVGEDQVQH 156
Cdd:PRK12285 144 YFQSENIKVYDLAFELAKKVNFSELKAIYGFTGETN-------IGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPH 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462502115 157 MELVQDLAQGFNKKYGefFPVPESILtsMKKVKSLRdpSAKMSKSDPDklATVRITDSPEEIVQKFRKAVT 227
Cdd:PRK12285 217 IRLTRDIAERLHGGYG--FIKPSSTY--HKFMPGLT--GGKMSSSKPE--SAIYLTDDPETVKKKIMKALT 279
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
4-239 |
5.22e-12 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 65.66 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 4 SKKRVFSGIQPTGILHLGNYLgaiesWVR----LQDE-YDSVLYsIVDLHS-ITVPQDPAVLRQSILDMTAVLLACGINP 77
Cdd:PRK08560 29 EEPKAYIGFEPSGKIHLGHLL-----TMNkladLQKAgFKVTVL-LADWHAyLNDKGDLEEIRKVAEYNKKVFEALGLDP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 78 EKS--IL---FQQSqvSEHTQLSWILSCMVRLPRLQHlhqwkAKT--TKQKHDGTVGLLTYPVLQAADILlYKSTHVPV- 149
Cdd:PRK08560 103 DKTefVLgseFQLD--KEYWLLVLKLAKNTTLARARR-----SMTimGRRMEEPDVSKLVYPLMQVADIF-YLDVDIAVg 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 150 GEDQVQ-HMeLVQDLAQGFNkkygefFPVPESILTSMkkVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQKFRKAvtd 228
Cdd:PRK08560 175 GMDQRKiHM-LAREVLPKLG------YKKPVCIHTPL--LTGLDGGGIKMSKSKPG--SAIFVHDSPEEIRRKIKKA--- 240
|
250
....*....|.
gi 2462502115 229 ftsevtYDPPG 239
Cdd:PRK08560 241 ------YCPPG 245
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
129-239 |
2.58e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 48.53 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 129 LTYPVLQAADILLYKSTHVPVGEDQVQhmelVQDLAqgfnKKYGEFFPVPES-ILTSMKKVKSLRDPSAKMSKSDPDklA 207
Cdd:PTZ00126 196 ILYPCMQCADIFYLKADICQLGMDQRK----VNMLA----REYCDKKKIKKKpIILSHHMLPGLLEGQEKMSKSDPN--S 265
|
90 100 110
....*....|....*....|....*....|..
gi 2462502115 208 TVRITDSPEEIVQKFRKAvtdftsevtYDPPG 239
Cdd:PTZ00126 266 AIFMEDSEEDVNRKIKKA---------YCPPG 288
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
66-236 |
3.01e-06 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 48.74 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 66 MTAVLLACGINPEKSI-LFQQSQVSEHTQLSWILscMVRLPRLQHLHQWKAKTT---KQKHDGTVGLLTYPVLQAADILL 141
Cdd:PTZ00348 96 LIEVWKAAGMDMDKVLfLWSSEEITNHANTYWRT--VLDIGRQNTIARIKKCCTimgKTEGTLTAAQVLYPLMQCADIFF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 142 YKSTHVPVGEDQVQHMELVQDLAQGFNKKYgeffpvpESILTSMKKVKSLRDPSAKMSKSDPDklATVRITDSPEEIVQK 221
Cdd:PTZ00348 174 LKADICQLGLDQRKVNMLAREYCDLIGRKL-------KPVILSHHMLAGLKQGQAKMSKSDPD--SAIFMEDTEEDVARK 244
|
170
....*....|....*....
gi 2462502115 222 FRKA----VTDFTSEVTYD 236
Cdd:PTZ00348 245 IRQAycprVKQSASEITDD 263
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
2-233 |
3.08e-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: 45.08 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 2 KDSKKRVFSGIQPTGI-LHLGNYLgAIESWVRLQDEYDSVLYSIVDLHS-ITVPQDPAVLRQsILDMTAVL--------- 70
Cdd:TIGR00234 28 LERPLKLYLGFDPTAPsLHLGHLV-PLLKLRDFQQAGHEVIVLLGDFTAlIGDPTGKSEVRK-ILTREEVQenaenikkq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 71 LACGINPEKSILFQQSqvsehtqlSWILSC----MVR-LPRLQHLHQWKAK---TTKQKHDGTVGLLTYPVLQAADIL-L 141
Cdd:TIGR00234 106 IARFLDFEKAKFVYNS--------EWLLKLnytdFIRlLGKIFTVNRMLRRdafSSRFEENISLHEFIYPLLQAYDFVyL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 142 YKSTHVPvGEDQVQHMELVQDLAQGFNKKYGEFFPVPesILTSMKKVKSLRDPSAKMSkSDPDKLAT-VRITDSPEEIVQ 220
Cdd:TIGR00234 178 NVDLQLG-GSDQWFNIRKGRDLARENLPSLQFGLTVP--LLTPADGEKMGKSLGGAVS-LDEGKYDFyQKVINTPDELVK 253
|
250
....*....|...
gi 2462502115 221 KFRKAVTDFTSEV 233
Cdd:TIGR00234 254 KYLKLFTFLGLEE 266
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
6-225 |
3.83e-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: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 6 KRVFSGIQPTGI-LHLGNYLgAIESWVRLQDEYDSVLYSIVDLHS-ITVPQDPAVLRqSILDMTAVLLACginpeKSILF 83
Cdd:cd00805 1 LKVYIGFDPTAPsLHLGHLV-PLMKLRDFQQAGHEVIVLIGDATAmIGDPSGKSEER-KLLDLELIRENA-----KYYKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 84 Q-----QSQVSEHTQL----SWILSC----MVRLPRLQHLHQWKAK-TTKQKHDGTVGL----LTYPVLQAADIL-LYKS 144
Cdd:cd00805 74 QlkailDFIPPEKAKFvnnsDWLLSLytldFLRLGKHFTVNRMLRRdAVKVRLEEEEGIsfseFIYPLLQAYDFVyLDVD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 145 THVPvGEDQVQHMELVQDLAQGFNKK--YGEFFPvpesILTSMKkvkslrdpSAKMSKSDPDKlATVRITDSPEEIVQKF 222
Cdd:cd00805 154 LQLG-GSDQRGNITLGRDLIRKLGYKkvVGLTTP----LLTGLD--------GGKMSKSEGNA-IWDPVLDSPYDVYQKI 219
|
...
gi 2462502115 223 RKA 225
Cdd:cd00805 220 RNA 222
|
|
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
70-224 |
7.82e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 40.88 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 70 LLACGINPEKSILFQQSQ-VSehtqlSWILSCMVRLprlqhlhqWKAKTTKQKH-----DGT--VGLLTYPVLQAA---- 137
Cdd:PLN02486 140 IIACGFDVERTFIFSDFDyVG-----GAFYKNMVKI--------AKCVTLNQVRgifgfSGEdnIGKISFPAVQAApsfp 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 138 ---DILLYKSTH----VPVGEDQVQHMELVQDLAQ--GFNKK---YGEFFPvpesiltsmkkvkSLRDPSAKMSKSDPDk 205
Cdd:PLN02486 207 ssfPHLFGGKDKlrclIPCAIDQDPYFRMTRDVAPrlGYYKPaliESRFFP-------------ALQGESGKMSASDPN- 272
|
170
....*....|....*....
gi 2462502115 206 lATVRITDSPEEIVQKFRK 224
Cdd:PLN02486 273 -SAIYVTDTPKEIKNKINK 290
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
8-202 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 8 VFSGIQPTGILHLGNYLGAIeSWVRLQDEYDSVLYSIVDLHSITvPQDPAVLRQSIldmtavllACGINPEKsilfqqsq 87
Cdd:cd00802 2 TFSGITPNGYLHIGHLRTIV-TFDFLAQAYRKLGYKVRCIALID-DAGGLIGDPAN--------KKGENAKA-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502115 88 vsehtqlswilscMVRlprlqhlhQWKAKTTKQkhdgtvglLTYPVLQAADILL---YKSTHVPVGEDQVQHMELVQDLA 164
Cdd:cd00802 64 -------------FVE--------RWIERIKED--------VEYMFLQAADFLLlyeTECDIHLGGSDQLGHIELGLELL 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462502115 165 QGFNKKYgeffpVPESILTSMKKVKSLRdpsaKMSKSD 202
Cdd:cd00802 115 KKAGGPA-----RPFGLTFGRVMGADGT----KMSKSK 143
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
8-74 |
2.27e-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: 37.13 E-value: 2.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462502115 8 VFSGIQPtGILHLGNYLGaIESWVRLQDEydsVLYSIVDLHSITVPQDPAVLRQSILDMTAVLLACG 74
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKL-ICRAKGIADQ---CVVRIDDNPPVKVWQDPHELEERKESIEEDISVCG 63
|
|
|