|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
2-326 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 562.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:PRK00927 2 KRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFKEKSA-GKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:PRK00927 82 HVPEHAELAWILNCITPLGELERMTQFKDKSAkQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKVGARI*SLVDPTKK*SKSDPNPKAYITLLDDAKTIEKKIKSAVTDSEGT--IRYDKEAKPGI 238
Cdd:PRK00927 162 FNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLreIRYDLPNKPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 239 SNLLNIYSTLSGQSIEELERQYE--GKGYGVFKADLAQVVIETLRPIQERYHHW*ES-EELDRVLDEGAEKANRVASE*V 315
Cdd:PRK00927 242 SNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADpAYLDEILAEGAEKARAVASKTL 321
|
330
....*....|.
3FI0_A 316 RK*EQA*GLGR 326
Cdd:PRK00927 322 KEVREAMGLLR 332
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-326 |
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: 523.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:COG0180 4 KRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFKEKSA--GKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAE 159
Cdd:COG0180 84 DVPEHAELAWLLSCLTPLGELERMPQFKDKSAknGKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 160 RFNKRYGELFTIPEARIPKVGARI*SLvDPTKK*SKSDPNpkaYITLLDDAKTIEKKIKSAVTDSEGtIRYDKEAKPGIS 239
Cdd:COG0180 164 RFNHRYGEVFPEPEALIPEEGARIPGL-DGRKKMSKSYGN---TINLLDDPKEIRKKIKSAVTDSER-LRYDDPGKPEVC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 240 NLLNIYSTLSGQ-SIEELERQYE--GKGYGVFKADLAQVVIETLRPIQERYHHW*E-SEELDRVLDEGAEKANRVASE*V 315
Cdd:COG0180 239 NLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLAdPAELDEILAEGAEKARAIAAKTL 318
|
330
....*....|.
3FI0_A 316 RK*EQA*GLGR 326
Cdd:COG0180 319 AEVREAMGLLY 329
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
3-278 |
1.22e-142 |
|
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: 403.89 E-value: 1.22e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSGVITIGNYIGALRQFVELQH-EYNCYFCIVDQHAITVWQ-DPHELRQNIRRLAALYLAVGIDPTQATLFIQ 80
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 81 SEVPAHAQAAW*LQCIVYIGELER*TQFKEKSAGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKvGARI*SLVDPTKK*SKSDPNpkAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN 240
Cdd:cd00806 161 FNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
3FI0_A 241 LLNIYSTLSGQSIEELER----QYEGKGYGVFKADLAQVVIE 278
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
2-324 |
5.23e-135 |
|
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: 386.30 E-value: 5.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQ-DPHELRQNIRRLAALYLAVGIDPTQATLFIQ 80
Cdd:TIGR00233 3 FRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 81 SEVPAHAQAAW*LQCIVYIGELER*TQFKEKSAgKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:TIGR00233 83 SDYPEHYELAWLLSCQVTFGELKRMTQFKDKSQ-AENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKVGARI*SLVDptKK*SKSDPNpkAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN 240
Cdd:TIGR00233 162 FNKKFKNFFPKPESLISKFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 241 LLNIYSTLSGQSI------EELERQYEGK-GYGVFKADLAQVVIETLRPIQERYHHW*EsEELDRVLDEGAEKANRVASE 313
Cdd:TIGR00233 238 LLVIYQYLSFFLIdddklkEIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAE-EILDKILEPGAKKARETANK 316
|
330
....*....|.
3FI0_A 314 *VRK*EQA*GL 324
Cdd:TIGR00233 317 TLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
3-280 |
9.54e-88 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 264.91 E-value: 9.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSGVITIGnYIGALRQFVELQ-HEYNCYFCIVDQHAITVWQD---PHELRQNIRRLAAL---YLAVGIDPTQA 75
Cdd:pfam00579 7 RVYSGIDPTGPLHLG-YLVPLMKLRQFQqAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 76 TLFIQSEVPAHAQAAW*LQCIVYIGELER*TQFKEKS---AGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIE 152
Cdd:pfam00579 86 EIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKkrlEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 153 LTRDLAERFNKRygeLFTIPEARIPKvgarI*SLVDPTKK*SKSDPNPKayITLLDDAKTIEKKIKSAVTDSEGTIRYDK 232
Cdd:pfam00579 166 LGRDLARRFNKK---IFKKPVGLTNP----LLTGLDGGKKMSKSAGNSA--IFLDDDPESVYKKIQKAYTDPDREVRKDL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
3FI0_A 233 EAKPGISN-LLNIYSTLSGQSI----EELERQYEGK--GYGVFKADLAQVVIETL 280
Cdd:pfam00579 237 KLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGlvHGGDLKKAAAEAVNKLL 291
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
2-326 |
0e+00 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 562.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:PRK00927 2 KRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFKEKSA-GKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:PRK00927 82 HVPEHAELAWILNCITPLGELERMTQFKDKSAkQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKVGARI*SLVDPTKK*SKSDPNPKAYITLLDDAKTIEKKIKSAVTDSEGT--IRYDKEAKPGI 238
Cdd:PRK00927 162 FNNLYGEVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLreIRYDLPNKPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 239 SNLLNIYSTLSGQSIEELERQYE--GKGYGVFKADLAQVVIETLRPIQERYHHW*ES-EELDRVLDEGAEKANRVASE*V 315
Cdd:PRK00927 242 SNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADpAYLDEILAEGAEKARAVASKTL 321
|
330
....*....|.
3FI0_A 316 RK*EQA*GLGR 326
Cdd:PRK00927 322 KEVREAMGLLR 332
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
2-326 |
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: 523.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:COG0180 4 KRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFKEKSA--GKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAE 159
Cdd:COG0180 84 DVPEHAELAWLLSCLTPLGELERMPQFKDKSAknGKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 160 RFNKRYGELFTIPEARIPKVGARI*SLvDPTKK*SKSDPNpkaYITLLDDAKTIEKKIKSAVTDSEGtIRYDKEAKPGIS 239
Cdd:COG0180 164 RFNHRYGEVFPEPEALIPEEGARIPGL-DGRKKMSKSYGN---TINLLDDPKEIRKKIKSAVTDSER-LRYDDPGKPEVC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 240 NLLNIYSTLSGQ-SIEELERQYE--GKGYGVFKADLAQVVIETLRPIQERYHHW*E-SEELDRVLDEGAEKANRVASE*V 315
Cdd:COG0180 239 NLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLAdPAELDEILAEGAEKARAIAAKTL 318
|
330
....*....|.
3FI0_A 316 RK*EQA*GLGR 326
Cdd:COG0180 319 AEVREAMGLLY 329
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
3-278 |
1.22e-142 |
|
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: 403.89 E-value: 1.22e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSGVITIGNYIGALRQFVELQH-EYNCYFCIVDQHAITVWQ-DPHELRQNIRRLAALYLAVGIDPTQATLFIQ 80
Cdd:cd00806 1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 81 SEVPAHAQAAW*LQCIVYIGELER*TQFKEKSAGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:cd00806 81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKvGARI*SLVDPTKK*SKSDPNpkAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN 240
Cdd:cd00806 161 FNKLYGEIFPKPAALLSK-GAFLPGLQGPSKKMSKSDPN--NAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
3FI0_A 241 LLNIYSTLSGQSIEELER----QYEGKGYGVFKADLAQVVIE 278
Cdd:cd00806 238 LVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQE 279
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
2-323 |
1.99e-137 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 394.95 E-value: 1.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:PLN02886 47 KRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFKEKS--AGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAE 159
Cdd:PLN02886 127 HVPAHAELMWLLSCSTPIGWLNKMIQFKEKSrkAGDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 160 RFNKRYG------------ELFTIPEARIPKVGARI*SLVDPTKK*SKSDPNPKAYITLLDDAKTIEKKIKSAVTDSEGT 227
Cdd:PLN02886 207 RVNNLYGgrkwkklggrggSVFKVPEALIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 228 IRYDKEAKPGISNLLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHH-W*ESEELDRVLDEGAEK 306
Cdd:PLN02886 287 LEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEiMSDPSYLDSVLKEGADA 366
|
330
....*....|....*..
3FI0_A 307 ANRVASE*VRK*EQA*G 323
Cdd:PLN02886 367 AAEIADRTLANVYQAMG 383
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
2-324 |
5.23e-135 |
|
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: 386.30 E-value: 5.23e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQ-DPHELRQNIRRLAALYLAVGIDPTQATLFIQ 80
Cdd:TIGR00233 3 FRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFLQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 81 SEVPAHAQAAW*LQCIVYIGELER*TQFKEKSAgKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAER 160
Cdd:TIGR00233 83 SDYPEHYELAWLLSCQVTFGELKRMTQFKDKSQ-AENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 161 FNKRYGELFTIPEARIPKVGARI*SLVDptKK*SKSDPNpkAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISN 240
Cdd:TIGR00233 162 FNKKFKNFFPKPESLISKFFPRLMGLSG--KKMSKSDPN--SAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 241 LLNIYSTLSGQSI------EELERQYEGK-GYGVFKADLAQVVIETLRPIQERYHHW*EsEELDRVLDEGAEKANRVASE 313
Cdd:TIGR00233 238 LLVIYQYLSFFLIdddklkEIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEIAE-EILDKILEPGAKKARETANK 316
|
330
....*....|.
3FI0_A 314 *VRK*EQA*GL 324
Cdd:TIGR00233 317 TLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
2-324 |
1.73e-110 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 324.12 E-value: 1.73e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAIT-VWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQ 80
Cdd:PRK12282 3 PIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTIFIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 81 SEVPAHAQAAW*LQCIVYIGELER*TQFKEKSAGK---EAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDL 157
Cdd:PRK12282 83 SQIPELAELTMYYMNLVTVARLERNPTVKTEIAQKgfgRSIPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQTREI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 158 AERFNKRYG-ELFTIPEARIPKVGaRI*SLvDPTKK*SKSDPNPkayITLLDDAKTIEKKIKSAVTDSeGTIRYDKEAKP 236
Cdd:PRK12282 163 VRRFNSLYGtDVLVEPEALLPEAG-RLPGL-DGKAKMSKSLGNA---IYLSDDADTIKKKVMSMYTDP-NHIRVEDPGKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 237 GISNLLNIYSTLSG--QSIEELERQYEGKGYG--VFKADLAQVVIETLRPIQERYHHW*ES-EELDRVLDEGAEKANRVA 311
Cdd:PRK12282 237 EGNVVFTYLDAFDPdkAEVAELKAHYQRGGLGdvKCKRYLEEVLQELLAPIRERRAEFAKDpGYVLEILKAGSEKAREVA 316
|
330
....*....|...
3FI0_A 312 SE*VRK*EQA*GL 324
Cdd:PRK12282 317 AQTLSEVKDAMGL 329
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
3-279 |
2.33e-109 |
|
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: 319.25 E-value: 2.33e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSG-VITIGNYIGaLRQFVELQH-EYNCYFCIVDQHAITVWQ----------DPHELRQNIRRLAALYLAVGI 70
Cdd:cd00395 1 TLYCGIDPTAdSLHIGHLIG-LLTFRRFQHaGHRPIFLIGGQTGIIGDPsgkksertlnDPEEVRQNIRRIAAQYLAVGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 71 D--PTQATLFIQSEVP---AHAQAAW*LQCIVYIGELER*TQFKEKSagKEAVSAGLLTYPPL*AADILLYNT----DIV 141
Cdd:cd00395 80 FedPTQATLFNNSDWPgplAHIQFLRDLGKHVYVNYMERKTSFQSRS--EEGISATEFTYPPLQAADFLLLNTtegcDIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 142 PVGEDQKQHIELTRDLAERFNkrygeLFTIPEARIPkvgARI*SLVDPtkK*SKSDPNPKAYITLLDDAKTIEKKIKSAV 221
Cdd:cd00395 158 PGGSDQWGNITLGRELARRFN-----GFTIAEGLTI---PLVTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWINAV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
3FI0_A 222 tdsegtirydkeakpgISNLLNIYSTLSGQSIEELER----QYEGKGYGVFKADLAQVVIET 279
Cdd:cd00395 228 ----------------DSDVINILKYFTFLSKEEIERleqeQYEAPGYRVAQKTLAEEVTKT 273
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
3-280 |
9.54e-88 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 264.91 E-value: 9.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSGVITIGnYIGALRQFVELQ-HEYNCYFCIVDQHAITVWQD---PHELRQNIRRLAAL---YLAVGIDPTQA 75
Cdd:pfam00579 7 RVYSGIDPTGPLHLG-YLVPLMKLRQFQqAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 76 TLFIQSEVPAHAQAAW*LQCIVYIGELER*TQFKEKS---AGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIE 152
Cdd:pfam00579 86 EIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKkrlEQGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 153 LTRDLAERFNKRygeLFTIPEARIPKvgarI*SLVDPTKK*SKSDPNPKayITLLDDAKTIEKKIKSAVTDSEGTIRYDK 232
Cdd:pfam00579 166 LGRDLARRFNKK---IFKKPVGLTNP----LLTGLDGGKKMSKSAGNSA--IFLDDDPESVYKKIQKAYTDPDREVRKDL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
3FI0_A 233 EAKPGISN-LLNIYSTLSGQSI----EELERQYEGK--GYGVFKADLAQVVIETL 280
Cdd:pfam00579 237 KLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGlvHGGDLKKAAAEAVNKLL 291
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
2-325 |
5.63e-75 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 233.85 E-value: 5.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 2 KTIFSGIQPSGVITIGNYIGALRQFVELQHEYNC---YFcIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLF 78
Cdd:PRK12556 4 KIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGkalYF-IADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVIFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 79 IQSEVPAHAQAAW*LQCIVYIGELER*TQFK-----EKSAGKEA---VSAGLLTYPPL*AADILLYNTDIVPVGEDQKQH 150
Cdd:PRK12556 83 RQSDVPEIFELAWILSCLTPKGLMNRAHAYKakvdqNKEAGLDLdagVNMGLYTYPILMAADILLFQATHVPVGKDQIQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 151 IELTRDLAERFNKRYGELFTIPEARIPKVGARI*SLvdPTKK*SKSDPNpkaYITLLDDAKTIEKKIKSAVTDSEGTiry 230
Cdd:PRK12556 163 IEIARDIATYFNHTFGDTFTLPEYVIQEEGAILPGL--DGRKMSKSYGN---VIPLFAEQEKLRKLIFKIKTDSSLP--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 231 dKEAK-PGISNLLNIYSTLSGQS-IEELERQYE-GKGYGVFKADLAQVVIETLRPIQERYHHW*ES-EELDRVLDEGAEK 306
Cdd:PRK12556 235 -NEPKdPETSALFTIYKEFATEEeVQSMREKYEtGIGWGDVKKELFRVVDRELAGPREKYAMYMNEpSLLDEALEKGAER 313
|
330
....*....|....*....
3FI0_A 307 ANRVASE*VRK*EQA*GLG 325
Cdd:PRK12556 314 AREIAKPNLAEIKKAIGFE 332
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
4-325 |
2.87e-62 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 202.87 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 4 IFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITV-WQDPHELRQNIRRLAALYLAVGIDPTQATLFIQSE 82
Cdd:PRK12283 5 VLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTThYETPEVIEKNVWDMVIDWLAAGVDPAQATLFIQSK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 83 VPAHAQAAW*LQCIVYIGELER*TQFK---EKSAGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAE 159
Cdd:PRK12283 85 VPEHAELHLLLSMITPLGWLERVPTYKdqqEKLKEKDLSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 160 RFNKRYGElftIP------EARIPKVG---ARI--------------------*SLVDPTKK*SKSD------------- 197
Cdd:PRK12283 165 RFNHLYGR---EPgfeekaEAAIKKLGkkrAKLyhelrnayqeegddealeqaRALLQEQQNLSMGDrerlfgylegagk 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 198 ---PNP-------------------KAY---ITLLDDAKTIEKKIKSAVTDSEGTIRYDkeakPG------ISNLLNIYS 246
Cdd:PRK12283 242 iilPEPqallteaskmpgldgqkmsKSYgntIGLREDPESVTKKIRTMPTDPARVRRTD----PGdpekcpVWQLHQVYS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 247 tlSGQSIEELERQYEGKGYGVF--KADLAQVVIETLRPIQERYHHW*ESEELDR-VLDEGAEKANRVASE*VRK*EQA*G 323
Cdd:PRK12283 318 --DEETKEWVQKGCRSAGIGCLecKQPVIDAILREQQPMRERAQKYEDDPSLVRaIVADGCEKARKVARETMRDVREAMG 395
|
..
3FI0_A 324 LG 325
Cdd:PRK12283 396 LS 397
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
4-324 |
3.49e-56 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 187.90 E-value: 3.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 4 IFSGIQPSGVITIGNYIGALRQFVE--LQHEYNCYFCIVDQHAITVWQDPHELRQNIRRLAALYLAVGIDPTQATLFIQS 81
Cdd:PRK12284 5 VLTGITTTGTPHLGNYAGAIRPAIAasRQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 82 EVPAHAQAAW*LQCIVYIGELER*TQFK-----EKSAGKEA---VSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIEL 153
Cdd:PRK12284 85 DIPEIPELTWLLTCVAGKGLLNRAHAYKaavdkNVAAGEDPdagVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 154 TRDLAERFNKRYG-ELFTIPEARIPKVGARI*SLvdPTKK*SKSDPNPkayITLLDDAKTIEKKIKSAVTDSegtiRYDK 232
Cdd:PRK12284 165 ARDIAQRFNHLYGgEFFVLPEAVIEESVATLPGL--DGRKMSKSYDNT---IPLFAPREELKKAIFSIVTDS----RAPG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 233 EAK-PGISNLLNIYSTLSG-QSIEELERQY-EGKGYGVFKADLAQVVIETLRPIQERYHHW-*ESEELDRVLDEGAEKAN 308
Cdd:PRK12284 236 EPKdTEGSALFQLYQAFATpEETAAFRQALaDGIGWGDAKQRLFERIDRELAPMRERYEALiARPADIEDILLAGAAKAR 315
|
330
....*....|....*.
3FI0_A 309 RVASE*VRK*EQA*GL 324
Cdd:PRK12284 316 RIATPFLAELREAVGL 331
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
3-197 |
1.14e-20 |
|
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: 86.38 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPSGVITIGNYIGaLRQFVELQHEY-------NCYFCIVDQHAITVWQD-------PHELRQNIRRLAALYLav 68
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRT-IVTFDFLAQAYrklgykvRCIALIDDAGGLIGDPAnkkgenaKAFVERWIERIKEDVE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 69 gidptqatlfiqsevpahaqaaw*lqcivyigeler*tqfkeksagkeavsaglltYPPL*AADILLYNT---DIVPVGE 145
Cdd:cd00802 78 --------------------------------------------------------YMFLQAADFLLLYEtecDIHLGGS 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
3FI0_A 146 DQKQHIELTRDLAERFNkrygeLFTIPEARIPkvgARI*sLVDPTKK*SKSD 197
Cdd:cd00802 102 DQLGHIELGLELLKKAG-----GPARPFGLTF---GRV--MGADGTKMSKSK 143
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
3-197 |
2.13e-19 |
|
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: 81.82 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 3 TIFSGIQPsGVITIGNYIGaLRQFVELQheYNCYFCIVDQHAITVWQDPHELRQNIRRLAalylavgidptqatlfiqse 82
Cdd:cd02156 1 KARFPGEP-GYLHIGHAKL-ICRAKGIA--DQCVVRIDDNPPVKVWQDPHELEERKESIE-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 83 vpahaqaaw*lqcivyigeler*tqfkeksagkeavsaglltyppl*aadillynTDIVPVGEDQKQHIELTRDlaerfN 162
Cdd:cd02156 57 -------------------------------------------------------EDISVCGEDFQQNRELYRW-----V 76
|
170 180 190
....*....|....*....|....*....|....*
3FI0_A 163 KRYGELFTIPEARIPKVGAri*slvDPTKK*SKSD 197
Cdd:cd02156 77 KDNITLPVDPEQVELPRLN------LETTVMSKRK 105
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
4-222 |
6.68e-18 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 83.38 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 4 IFSGIQPSGVITIGNYIgALRQFVELQ-HEYNCYFCIVDQHAITV----WQDPHEL-RQNIRRlaalYLAVGIDPTQATL 77
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKM-VFDELKWHQeFGANVYIPIADDEAYAArglsWEETREWaYEYILD----LIALGFDPDKTEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 78 FIQSEVPahaqaaw*LQCIVYigELER*TQFKEKSA---GKEAVSAGLLTYPPL*AADILLYNTD------IVPVGEDQK 148
Cdd:PRK12285 144 YFQSENI-------KVYDLAF--ELAKKVNFSELKAiygFTGETNIGHIFYPATQAADILHPQLEegpkptLVPVGIDQD 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3FI0_A 149 QHIELTRDLAERFNKRYGelFTIPEARIPKVgarI*SLVDptKK*SKSDPNPkaYITLLDDAKTIEKKIKSAVT 222
Cdd:PRK12285 215 PHIRLTRDIAERLHGGYG--FIKPSSTYHKF---MPGLTG--GKMSSSKPES--AIYLTDDPETVKKKIMKALT 279
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
102-278 |
1.64e-09 |
|
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: 57.62 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 102 LER*TqFKEKSAGKEAVSAGLLTYPPL*AADILLYNTDIVPVGEDQKQHIELTRDLAERFN--KRYGelFTIPearipkv 179
Cdd:cd00805 117 LRRDA-VKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLGykKVVG--LTTP------- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 180 gari*SLVDPT-KK*SKSDPNpKAYITLLDDAKTIEKKIKSAvtdsegtirYDkeakPGISNLLNIYSTLSGQSIEELER 258
Cdd:cd00805 187 -----LLTGLDgGKMSKSEGN-AIWDPVLDSPYDVYQKIRNA---------FD----PDVLEFLKLFTFLDYEEIEELEE 247
|
170 180
....*....|....*....|.
3FI0_A 259 QY-EGKGYGVFKADLAQVVIE 278
Cdd:cd00805 248 EHaEGPLPRDAKKALAEELTK 268
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
99-302 |
3.31e-09 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 57.39 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 99 IGELER*TQFKEKSAGKEAVSAGLLtYPPL*AADILLYNTDIVPVGEDQKQHIELTRDlaerfnkrYGELFTIPEARIPK 178
Cdd:PTZ00126 173 ITRIKRCSQIMGRSEGDEQPCAQIL-YPCMQCADIFYLKADICQLGMDQRKVNMLARE--------YCDKKKIKKKPIIL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 179 VGARI*SLVDPTKK*SKSDPNpkAYITLLDDAKTIEKKIKSA-----VTDSEGTIRYDKEAKPGISNLLNI--YSTLSG- 250
Cdd:PTZ00126 244 SHHMLPGLLEGQEKMSKSDPN--SAIFMEDSEEDVNRKIKKAycppgVIEGNPILAYFKSIVFPAFNSFTVlrKEKNGGd 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3FI0_A 251 ---QSIEELERQY-EGKGY-GVFKADLAQVVIETLRPIQeryHHW*ESEELDRVLDE 302
Cdd:PTZ00126 322 vtyTTYEELEKDYlSGALHpGDLKPALAKYLNLMLQPVR---DHFQNNPEAKSLLSE 375
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
4-223 |
2.77e-04 |
|
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: 42.38 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 4 IFSGIQPSGV-ITIGNY--IGALRQFVELQHEynCYFCIVDQHAITvwQDP---HELRQ-----NIRRLAALY---LAVG 69
Cdd:TIGR00234 34 LYLGFDPTAPsLHLGHLvpLLKLRDFQQAGHE--VIVLLGDFTALI--GDPtgkSEVRKiltreEVQENAENIkkqIARF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 70 IDPTQATLFIQSEvpahaqaaW*LQcIVYIGELER*T------QFKEKSAGKEAVSAGL----LTYPPL*AADILLYNTD 139
Cdd:TIGR00234 110 LDFEKAKFVYNSE--------WLLK-LNYTDFIRLLGkiftvnRMLRRDAFSSRFEENIslheFIYPLLQAYDFVYLNVD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 140 IVPVGEDQKQHIELTRDLAERFNKRYGELFTIPearipkvgari*sLVDPT--KK*SKS-------DPNPKA-YITLLDD 209
Cdd:TIGR00234 181 LQLGGSDQWFNIRKGRDLARENLPSLQFGLTVP-------------LLTPAdgEKMGKSlggavslDEGKYDfYQKVINT 247
|
250
....*....|....
3FI0_A 210 AKTIEKKIKSAVTD 223
Cdd:TIGR00234 248 PDELVKKYLKLFTF 261
|
|
| PLN02486 |
PLN02486 |
aminoacyl-tRNA ligase |
121-302 |
3.11e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 178104 Cd Length: 383 Bit Score: 42.04 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 121 GLLTYPPL*AADIL------LYNTDI-----VPVGEDQKQHIELTRDLAERFNKRYGELFtipEARIpkvgarI*SLVDP 189
Cdd:PLN02486 192 GKISFPAVQAAPSFpssfphLFGGKDklrclIPCAIDQDPYFRMTRDVAPRLGYYKPALI---ESRF------FPALQGE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3FI0_A 190 TKK*SKSDPNPKAYITllDDAKTIEKKIKSAVTdSEGTIRYDKEAKPGISNLLNI---YSTLSGQSIEELERQYEGKGYG 266
Cdd:PLN02486 263 SGKMSASDPNSAIYVT--DTPKEIKNKINKYAF-SGGQDTVEEHRELGANLEVDIpwkYLNFFLEDDAELERIKKEYGSG 339
|
170 180 190
....*....|....*....|....*....|....*..
3FI0_A 267 -VFKADLAQVVIETLRPIQERyHHW*ESEELDRVLDE 302
Cdd:PLN02486 340 rMLTGEVKKRLIEVLTEIVER-HQRARAAVTDEMVDA 375
|
|
| |
