|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
82-406 |
2.38e-150 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 438.37 E-value: 2.38e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNaRDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSA 161
Cdd:PRK00927 4 VLSGIQPTGKLHLGNYLGAIKNWVELQD-EYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 162 VAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKD-VPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:PRK00927 83 VPEHAELAWILNCITPLGELERMTQFKDKSAKQKEnVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIeDGDASRVLSLRDPSKKMSKSEANPKATINLCDSPDLITQKIKKAVTDftSD----ITYNPGKRA 316
Cdd:PRK00927 163 NNLYGEVFPVPEPLI-PKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTD--SErlreIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 317 GVSNLVNIHAQVTGQSIKTVVNE--AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQ 394
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAEyeAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 24666151 395 TLNDVKQRLGLG 406
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
82-406 |
3.88e-144 |
|
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: 422.53 E-value: 3.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNaRDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSA 161
Cdd:COG0180 6 VLSGIQPTGRLHLGNYLGALKNWVELQD-EYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 162 VAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKD--VPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARI 239
Cdd:COG0180 85 VPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKenVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 240 YNGRYGETFPVCTAIIEDgDASRVLSLrDPSKKMSKSEANpkaTINLCDSPDLITQKIKKAVTDftSD-ITYNPGKRAGV 318
Cdd:COG0180 165 FNHRYGEVFPEPEALIPE-EGARIPGL-DGRKKMSKSYGN---TINLLDDPKEIRKKIKSAVTD--SErLRYDDPGKPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 319 SNLVNIHAQVTGQ-SIKTVVNE--AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQT 395
Cdd:COG0180 238 CNLFTIYSAFSGKeEVEELEAEyrAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKT 317
|
330
....*....|.
gi 24666151 396 LNDVKQRLGLG 406
Cdd:COG0180 318 LAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
82-359 |
1.36e-126 |
|
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: 375.77 E-value: 1.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNARDDVTVCIVDLHSITMPH-NPPLLRENIFTMAATLLACGIDPTKSTLFVQS 160
Cdd:cd00806 2 VLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 161 AVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:cd00806 82 DVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARRF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIEDGdaSRVLSLRDPSKKMSKSeaNPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSN 320
Cdd:cd00806 162 NKLYGEIFPKPAALLSKG--AFLPGLQGPSKKMSKS--DPNNAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24666151 321 LVNIHAQVTGQSIKTVV----NEAATLDTAKYKDRVAEAVVEH 359
Cdd:cd00806 238 LVEIYSAFFNDDDEELEeideYRSGGLGYGECKKLLAEAIQEF 280
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
82-405 |
1.29e-88 |
|
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: 279.60 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNArDDVTVCIVDLHSITMPHNPPL-LRENIFTMAATLLACGIDPTKSTLFVQS 160
Cdd:TIGR00233 5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFG-VELFICIADLHAITVKQTDPDaLRKAREELAADYLAVGLDPEKTFIFLQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 161 AVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLlKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:TIGR00233 84 DYPEHYELAWLLSCQVTFGELKRMTQFKDKSQA-ENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAERF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIEDgDASRVLSLRDpsKKMSKSeaNPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSN 320
Cdd:TIGR00233 163 NKKFKNFFPKPESLISK-FFPRLMGLSG--KKMSKS--DPNSAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 321 LVNIHAQVTGQSIKTVVNEAA-------TLDTAKYKDRVAEAVVEHLRPIREQIHHhmtKRNEMIY-LLEVGAEKARQQA 392
Cdd:TIGR00233 238 LLVIYQYLSFFLIDDDKLKEIyeayksgKLGYGECKKALIEVLQEFLKEIQERRAE---IAEEILDkILEPGAKKARETA 314
|
330
....*....|...
gi 24666151 393 RQTLNDVKQRLGL 405
Cdd:TIGR00233 315 NKTLADVYKAMGL 327
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
79-360 |
1.70e-69 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 227.93 E-value: 1.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTGSLHLGnYLGAVRKWVQLQNARDDVTVCIVDLHSITMPHN---PPLLRENIFTMAAT---LLACGIDPT 152
Cdd:pfam00579 5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 153 KSTLFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFRE-KSRL--LKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQH 229
Cdd:pfam00579 84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDvKKRLeqGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 230 IQLAQHLARIYNGRygeTFPVCTAIIedgdaSRVLSLRDPSKKMSKSEANPKatINLCDSPDLITQKIKKAVTDFTSDIT 309
Cdd:pfam00579 164 IELGRDLARRFNKK---IFKKPVGLT-----NPLLTGLDGGKKMSKSAGNSA--IFLDDDPESVYKKIQKAYTDPDREVR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666151 310 YNPGKRAGVSN-LVNIHAQVTGQSIKTVVNE------AATLDTAKYKDRVAEAVVEHL 360
Cdd:pfam00579 234 KDLKLFTFLSNeEIEILEAELGKSPYREAEEllarevTGLVHGGDLKKAAAEAVNKLL 291
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00927 |
PRK00927 |
tryptophanyl-tRNA synthetase; Reviewed |
82-406 |
2.38e-150 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 234866 [Multi-domain] Cd Length: 333 Bit Score: 438.37 E-value: 2.38e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNaRDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSA 161
Cdd:PRK00927 4 VLSGIQPTGKLHLGNYLGAIKNWVELQD-EYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 162 VAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKD-VPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:PRK00927 83 VPEHAELAWILNCITPLGELERMTQFKDKSAKQKEnVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIeDGDASRVLSLRDPSKKMSKSEANPKATINLCDSPDLITQKIKKAVTDftSD----ITYNPGKRA 316
Cdd:PRK00927 163 NNLYGEVFPVPEPLI-PKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTD--SErlreIRYDLPNKP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 317 GVSNLVNIHAQVTGQSIKTVVNE--AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQ 394
Cdd:PRK00927 240 EVSNLLTIYSALSGESIEELEAEyeAGGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGAEKARAVASK 319
|
330
....*....|..
gi 24666151 395 TLNDVKQRLGLG 406
Cdd:PRK00927 320 TLKEVREAMGLL 331
|
|
| TrpS |
COG0180 |
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
82-406 |
3.88e-144 |
|
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: 422.53 E-value: 3.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNaRDDVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSA 161
Cdd:COG0180 6 VLSGIQPTGRLHLGNYLGALKNWVELQD-EYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIFVQSD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 162 VAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKD--VPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARI 239
Cdd:COG0180 85 VPEHAELAWLLSCLTPLGELERMPQFKDKSAKNGKenVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIARR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 240 YNGRYGETFPVCTAIIEDgDASRVLSLrDPSKKMSKSEANpkaTINLCDSPDLITQKIKKAVTDftSD-ITYNPGKRAGV 318
Cdd:COG0180 165 FNHRYGEVFPEPEALIPE-EGARIPGL-DGRKKMSKSYGN---TINLLDDPKEIRKKIKSAVTD--SErLRYDDPGKPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 319 SNLVNIHAQVTGQ-SIKTVVNE--AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQT 395
Cdd:COG0180 238 CNLFTIYSAFSGKeEVEELEAEyrAGGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEILAEGAEKARAIAAKT 317
|
330
....*....|.
gi 24666151 396 LNDVKQRLGLG 406
Cdd:COG0180 318 LAEVREAMGLL 328
|
|
| TrpRS_core |
cd00806 |
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ... |
82-359 |
1.36e-126 |
|
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: 375.77 E-value: 1.36e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNARDDVTVCIVDLHSITMPH-NPPLLRENIFTMAATLLACGIDPTKSTLFVQS 160
Cdd:cd00806 2 VLSGIQPSGSLHLGHYLGAFRFWVWLQEAGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 161 AVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:cd00806 82 DVPEHYELAWLLSCVVTFGELERMTGFKDKSAQGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIARRF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIEDGdaSRVLSLRDPSKKMSKSeaNPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSN 320
Cdd:cd00806 162 NKLYGEIFPKPAALLSKG--AFLPGLQGPSKKMSKS--DPNNAIFLTDSPKEIKKKIMKAATDGGRTEHRRDGGGPGVSN 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24666151 321 LVNIHAQVTGQSIKTVV----NEAATLDTAKYKDRVAEAVVEH 359
Cdd:cd00806 238 LVEIYSAFFNDDDEELEeideYRSGGLGYGECKKLLAEAIQEF 280
|
|
| PLN02886 |
PLN02886 |
aminoacyl-tRNA ligase |
34-404 |
4.15e-108 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215478 [Multi-domain] Cd Length: 389 Bit Score: 332.16 E-value: 4.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 34 FLPGLASRTAGTPSATAQVTGGNKQHVHPHGNSVNSGHEEHNTRWPRKVFSGIQPTGSLHLGNYLGAVRKWVQLQNARDD 113
Cdd:PLN02886 1 SSLGSLGRLLSKPGPLSGSASSASCCSAATAATAPEKEAPPKVARKKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 114 VtVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFREKSRL 193
Cdd:PLN02886 81 F-FCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVFVQSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 194 --LKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIYN------------GRYGETFPVCTAIIEDGD 259
Cdd:PLN02886 160 agDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRDIAERVNnlyggrkwkklgGRGGSVFKVPEALIPPAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 260 AsRVLSLRDPSKKMSKSEANPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSNLVNIHAQVTGQSIKTVVNE 339
Cdd:PLN02886 240 A-RVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDSFPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24666151 340 AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQTLNDVKQRLG 404
Cdd:PLN02886 319 CGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLKEGADAAAEIADRTLANVYQAMG 383
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
82-405 |
1.29e-88 |
|
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: 279.60 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNArDDVTVCIVDLHSITMPHNPPL-LRENIFTMAATLLACGIDPTKSTLFVQS 160
Cdd:TIGR00233 5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFG-VELFICIADLHAITVKQTDPDaLRKAREELAADYLAVGLDPEKTFIFLQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 161 AVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLlKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLARIY 240
Cdd:TIGR00233 84 DYPEHYELAWLLSCQVTFGELKRMTQFKDKSQA-ENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLAERF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 241 NGRYGETFPVCTAIIEDgDASRVLSLRDpsKKMSKSeaNPKATINLCDSPDLITQKIKKAVTDFTSDITYNPGKRAGVSN 320
Cdd:TIGR00233 163 NKKFKNFFPKPESLISK-FFPRLMGLSG--KKMSKS--DPNSAIFLTDTPKQIKKKIRKAATDGGRVTLFEHREKPGVPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 321 LVNIHAQVTGQSIKTVVNEAA-------TLDTAKYKDRVAEAVVEHLRPIREQIHHhmtKRNEMIY-LLEVGAEKARQQA 392
Cdd:TIGR00233 238 LLVIYQYLSFFLIDDDKLKEIyeayksgKLGYGECKKALIEVLQEFLKEIQERRAE---IAEEILDkILEPGAKKARETA 314
|
330
....*....|...
gi 24666151 393 RQTLNDVKQRLGL 405
Cdd:TIGR00233 315 NKTLADVYKAMGL 327
|
|
| PRK12282 |
PRK12282 |
tryptophanyl-tRNA synthetase II; Reviewed |
82-405 |
1.20e-78 |
|
tryptophanyl-tRNA synthetase II; Reviewed
Pssm-ID: 183400 [Multi-domain] Cd Length: 333 Bit Score: 253.62 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVRKWVQLQNaRDDVTVCIVDLHSIT-MPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQS 160
Cdd:PRK12282 5 ILTGDRPTGKLHLGHYVGSLKNRVALQN-EHEQFVLIADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTIFIQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 161 AVAEHAEFNWILSSLTTMPRLAQLPQFREKSRL---LKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQLAQHLA 237
Cdd:PRK12282 84 QIPELAELTMYYMNLVTVARLERNPTVKTEIAQkgfGRSIPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQTREIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 238 RIYNGRYGETFPV-CTAIIedGDASRVLSLrDPSKKMSKSEANpkaTINLCDSPDLITQKIKKAVTDfTSDITYN-PGKR 315
Cdd:PRK12282 164 RRFNSLYGTDVLVePEALL--PEAGRLPGL-DGKAKMSKSLGN---AIYLSDDADTIKKKVMSMYTD-PNHIRVEdPGKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 316 AGvsNLVNIHAQVTGQSiKTVVNE------AATLDTAKYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKAR 389
Cdd:PRK12282 237 EG--NVVFTYLDAFDPD-KAEVAElkahyqRGGLGDVKCKRYLEEVLQELLAPIRERRAEFAKDPGYVLEILKAGSEKAR 313
|
330
....*....|....*.
gi 24666151 390 QQARQTLNDVKQRLGL 405
Cdd:PRK12282 314 EVAAQTLSEVKDAMGL 329
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
79-360 |
1.70e-69 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 227.93 E-value: 1.70e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTGSLHLGnYLGAVRKWVQLQNARDDVTVCIVDLHSITMPHN---PPLLRENIFTMAAT---LLACGIDPT 152
Cdd:pfam00579 5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 153 KSTLFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFRE-KSRL--LKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQH 229
Cdd:pfam00579 84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDvKKRLeqGPGISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 230 IQLAQHLARIYNGRygeTFPVCTAIIedgdaSRVLSLRDPSKKMSKSEANPKatINLCDSPDLITQKIKKAVTDFTSDIT 309
Cdd:pfam00579 164 IELGRDLARRFNKK---IFKKPVGLT-----NPLLTGLDGGKKMSKSAGNSA--IFLDDDPESVYKKIQKAYTDPDREVR 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24666151 310 YNPGKRAGVSN-LVNIHAQVTGQSIKTVVNE------AATLDTAKYKDRVAEAVVEHL 360
Cdd:pfam00579 234 KDLKLFTFLSNeEIEILEAELGKSPYREAEEllarevTGLVHGGDLKKAAAEAVNKLL 291
|
|
| PRK12556 |
PRK12556 |
tryptophanyl-tRNA synthetase; Provisional |
79-406 |
6.59e-60 |
|
tryptophanyl-tRNA synthetase; Provisional
Pssm-ID: 183592 [Multi-domain] Cd Length: 332 Bit Score: 204.19 E-value: 6.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTGSLHLGNYLGAVRKWVQLQNARDDVTV-CIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLF 157
Cdd:PRK12556 3 EKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGKALyFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVIFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 158 VQSAVAEHAEFNWILSSLTT---MPRLAQLPQFREKSR-----LLKDVPLGLYVYPVLQAADIMLYKSTHVPVGADQIQH 229
Cdd:PRK12556 83 RQSDVPEIFELAWILSCLTPkglMNRAHAYKAKVDQNKeagldLDAGVNMGLYTYPILMAADILLFQATHVPVGKDQIQH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 230 IQLAQHLARIYNGRYGETFPVCTAIIEDgdASRVLSLRDpSKKMSKSEANpkaTINLCDSPDlitqKIKKAVTDFTSDIT 309
Cdd:PRK12556 163 IEIARDIATYFNHTFGDTFTLPEYVIQE--EGAILPGLD-GRKMSKSYGN---VIPLFAEQE----KLRKLIFKIKTDSS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 310 -YNPGKRAGVSNLVNIHAQVTGQSikTVVNEAATLDTA----KYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVG 384
Cdd:PRK12556 233 lPNEPKDPETSALFTIYKEFATEE--EVQSMREKYETGigwgDVKKELFRVVDRELAGPREKYAMYMNEPSLLDEALEKG 310
|
330 340
....*....|....*....|..
gi 24666151 385 AEKARQQARQTLNDVKQRLGLG 406
Cdd:PRK12556 311 AERAREIAKPNLAEIKKAIGFE 332
|
|
| PRK12283 |
PRK12283 |
tryptophanyl-tRNA synthetase; Reviewed |
79-406 |
2.11e-58 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 183401 [Multi-domain] Cd Length: 398 Bit Score: 202.10 E-value: 2.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTGSLHLGNYLGAVRKWVQLQNARDdVTVCIVDLHSITMPH-NPPLLRENIFTMAATLLACGIDPTKSTLF 157
Cdd:PRK12283 2 PDRVLSGMRPTGRLHLGHYHGVLKNWVKLQHEYE-CFFFVADWHALTTHYeTPEVIEKNVWDMVIDWLAAGVDPAQATLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 158 VQSAVAEHAEFNWILSSLTTMPRLAQLPQFREKSRLLKDVPLGLYV---YPVLQAADIMLYKSTHVPVGADQIQHIQLAQ 234
Cdd:PRK12283 81 IQSKVPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKDLSTYGflgYPLLQSADILIYRAGLVPVGEDQVPHVEMTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 235 HLARIYNGRYG-------------------------------------ETFPVCTAIIED------GDASRVLS------ 265
Cdd:PRK12283 161 EIARRFNHLYGrepgfeekaeaaikklgkkraklyhelrnayqeegddEALEQARALLQEqqnlsmGDRERLFGylegag 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 266 ---LRDP-------SK-------KMSKSEANpkaTINLCDSPDLITQKIKKAVTDFTSDITYNPG--KRAGVSNLvniHA 326
Cdd:PRK12283 241 kiiLPEPqallteaSKmpgldgqKMSKSYGN---TIGLREDPESVTKKIRTMPTDPARVRRTDPGdpEKCPVWQL---HQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 327 QVTGQSIKTVVNEAATldTAKY-----KDRVAEAVVEHLRPIREQIHHHMTKRNEMIYLLEVGAEKARQQARQTLNDVKQ 401
Cdd:PRK12283 315 VYSDEETKEWVQKGCR--SAGIgclecKQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVARETMRDVRE 392
|
....*
gi 24666151 402 RLGLG 406
Cdd:PRK12283 393 AMGLS 397
|
|
| PRK12284 |
PRK12284 |
tryptophanyl-tRNA synthetase; Reviewed |
81-419 |
3.97e-40 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237036 [Multi-domain] Cd Length: 431 Bit Score: 152.47 E-value: 3.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 81 KVFSGIQPTGSLHLGNYLGAVRKWVQLQNARD-DVTVCIVDLHSITMPHNPPLLRENIFTMAATLLACGIDPTKSTLFVQ 159
Cdd:PRK12284 4 RVLTGITTTGTPHLGNYAGAIRPAIAASRQPGvESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 160 SAVAEHAEFNWILSSLTTMPRL-------AQLPQFREKSRLLKD-VPLGLYVYPVLQAADIMLYKSTHVPVGADQIQHIQ 231
Cdd:PRK12284 84 SDIPEIPELTWLLTCVAGKGLLnrahaykAAVDKNVAAGEDPDAgVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 232 LAQHLARIYNGRYG-ETFPVCTAIIEDGDASrvLSLRDpSKKMSKSEANpkaTINLCDSPDLITQKIKKAVTDftsdiTY 310
Cdd:PRK12284 164 MARDIAQRFNHLYGgEFFVLPEAVIEESVAT--LPGLD-GRKMSKSYDN---TIPLFAPREELKKAIFSIVTD-----SR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 311 NPG--KRAGVSNLVNIHaqvtgQSIKTVvNEAATLDTA--------KYKDRVAEAVVEHLRPIREQIHHHMTKRNEMIYL 380
Cdd:PRK12284 233 APGepKDTEGSALFQLY-----QAFATP-EETAAFRQAladgigwgDAKQRLFERIDRELAPMRERYEALIARPADIEDI 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 24666151 381 LEVGAEKARQQARQTLNDVKQRLGLGtsaNIPAAVHVAP 419
Cdd:PRK12284 307 LLAGAAKARRIATPFLAELREAVGLR---SLSSAAQAAA 342
|
|
| Tyr_Trp_RS_core |
cd00395 |
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ... |
82-358 |
3.36e-35 |
|
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: 134.35 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTG-SLHLGNYLGaVRKWVQLQNARDDVTVCIVDLHSIT----------MPHNPPLLRENIFTMAATLLACGID 150
Cdd:cd00395 2 LYCGIDPTAdSLHIGHLIG-LLTFRRFQHAGHRPIFLIGGQTGIIgdpsgkkserTLNDPEEVRQNIRRIAAQYLAVGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 151 --PTKSTLFVQSAV---AEHAEFNWILSSLTTMPRLAQLPQFREKSRllKDVPLGLYVYPVLQAADIMLYKSTH----VP 221
Cdd:cd00395 81 edPTQATLFNNSDWpgpLAHIQFLRDLGKHVYVNYMERKTSFQSRSE--EGISATEFTYPPLQAADFLLLNTTEgcdiQP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 222 VGADQIQHIQLAQHLARIYNGR---YGETFPvctaiiedgdasRVLSLRDPskKMSKSEANPKATINLCDSPDLITQKIK 298
Cdd:cd00395 159 GGSDQWGNITLGRELARRFNGFtiaEGLTIP------------LVTKLDGP--KFGKSESGPKWLDTEKTSPYEFYQFWI 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666151 299 KAVtdftsditynpgkragVSNLVNIHAQVTGQSIKTVVNEAATLDTAK----YKDRVAEAVVE 358
Cdd:cd00395 225 NAV----------------DSDVINILKYFTFLSKEEIERLEQEQYEAPgyrvAQKTLAEEVTK 272
|
|
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
79-300 |
7.37e-20 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 91.08 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTGSLHLGNYLgAVRKWVQLQNARDDVTVCIVDLHSI-----TMPhnppLLRENIFTMAATLLACGIDPTK 153
Cdd:PRK08560 30 EPKAYIGFEPSGKIHLGHLL-TMNKLADLQKAGFKVTVLLADWHAYlndkgDLE----EIRKVAEYNKKVFEALGLDPDK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 154 STLFVQSAVAEHAEFnWI----LSSLTTMPR----LAQLpqfrekSRLLKDVPLGLYVYPVLQAADImLYKSTHVPVGA- 224
Cdd:PRK08560 105 TEFVLGSEFQLDKEY-WLlvlkLAKNTTLARarrsMTIM------GRRMEEPDVSKLVYPLMQVADI-FYLDVDIAVGGm 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24666151 225 DQiQHIQLaqhLARIYNGRYGETFPVC--TAIIedgdasrvLSLRDPSKKMSKSEanPKATINLCDSPDLITQKIKKA 300
Cdd:PRK08560 177 DQ-RKIHM---LAREVLPKLGYKKPVCihTPLL--------TGLDGGGIKMSKSK--PGSAIFVHDSPEEIRRKIKKA 240
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
82-302 |
5.97e-18 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 86.07 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 82 VFSGIQPTGSLHLGNYLGAVR-KWVQLQNArdDVTVCIVDLHS-----ITMPHNPPLLRENIftmaATLLACGIDPTKST 155
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKMVFDElKWHQEFGA--NVYIPIADDEAyaargLSWEETREWAYEYI----LDLIALGFDPDKTE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 156 LFVQSAVAEHAEFNWILSSLTTMPRLAQLPQFREKSrllkdvPLGLYVYPVLQAADIML------YKSTHVPVGADQIQH 229
Cdd:PRK12285 143 IYFQSENIKVYDLAFELAKKVNFSELKAIYGFTGET------NIGHIFYPATQAADILHpqleegPKPTLVPVGIDQDPH 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24666151 230 IQLAQHLARIYNGRYGetFPVCTAIIedgdaSRVL-SLRdpSKKMSKSeaNPKATINLCDSPDLITQKIKKAVT 302
Cdd:PRK12285 217 IRLTRDIAERLHGGYG--FIKPSSTY-----HKFMpGLT--GGKMSSS--KPESAIYLTDDPETVKKKIMKALT 279
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
81-300 |
2.24e-13 |
|
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: 70.71 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 81 KVFSGIQPTG-SLHLGNYLgAVRKWVQLQNARDDVTVCIVDLH---------SITMPHNPP-LLRENIFTMAATLLAcgi 149
Cdd:cd00805 2 KVYIGFDPTApSLHLGHLV-PLMKLRDFQQAGHEVIVLIGDATamigdpsgkSEERKLLDLeLIRENAKYYKKQLKA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 150 dptkstlFVQSAVAEHAEF----NWiLSSLTTMPRLAQLPQFR---------EKSRLLKDVPLGL--YVYPVLQAADI-M 213
Cdd:cd00805 78 -------ILDFIPPEKAKFvnnsDW-LLSLYTLDFLRLGKHFTvnrmlrrdaVKVRLEEEEGISFseFIYPLLQAYDFvY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 214 LYKSTHVPvGADQIQHIQLAQHLARIYNgrYGETFPVCTAIIEDGDasrvlslrdpSKKMSKSEANpKATINLCDSPDLI 293
Cdd:cd00805 150 LDVDLQLG-GSDQRGNITLGRDLIRKLG--YKKVVGLTTPLLTGLD----------GGKMSKSEGN-AIWDPVLDSPYDV 215
|
....*..
gi 24666151 294 TQKIKKA 300
Cdd:cd00805 216 YQKIRNA 222
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
79-303 |
5.60e-10 |
|
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: 61.64 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 79 PRKVFSGIQPTG-SLHLGNYLgAVRKWVQLQNARDDVTVCIVDLHS-ITMPHNP-----PLLRENIFTMAATL---LACG 148
Cdd:TIGR00234 31 PLKLYLGFDPTApSLHLGHLV-PLLKLRDFQQAGHEVIVLLGDFTAlIGDPTGKsevrkILTREEVQENAENIkkqIARF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 149 IDPTKsTLFVQSavaehaeFNWILS-SLTTMPRLA----QLPQFREK----SRLLKDVPLGLYVYPVLQAADI-MLYKST 218
Cdd:TIGR00234 110 LDFEK-AKFVYN-------SEWLLKlNYTDFIRLLgkifTVNRMLRRdafsSRFEENISLHEFIYPLLQAYDFvYLNVDL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 219 HVPvGADQIQHIQLAQHLARIYNGR--YGETFPvctaiiedgdasrvLSLRDPSKKMSKSEAN-----PKAT---INLCD 288
Cdd:TIGR00234 182 QLG-GSDQWFNIRKGRDLARENLPSlqFGLTVP--------------LLTPADGEKMGKSLGGavsldEGKYdfyQKVIN 246
|
250
....*....|....*
gi 24666151 289 SPDLITQKIKKAVTD 303
Cdd:TIGR00234 247 TPDELVKKYLKLFTF 261
|
|
| PRK13354 |
PRK13354 |
tyrosyl-tRNA synthetase; Provisional |
190-279 |
2.49e-04 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 237360 [Multi-domain] Cd Length: 410 Bit Score: 44.12 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 190 KSRLLKDVPLGL--YVYPVLQAAD-IMLYKSTHVPV---GADQIQHIQLAQHLARIYNG--RYGETFPvctaIIEDGDAs 261
Cdd:PRK13354 154 KSRLEREQGISFteFFYPLLQAYDfVHLNRKEDVDLqigGTDQWGNILMGRDLQRKLEGeeQFGLTMP----LLEGADG- 228
|
90
....*....|....*...
gi 24666151 262 rvlslrdpsKKMSKSEAN 279
Cdd:PRK13354 229 ---------TKMGKSAGG 237
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
204-300 |
4.69e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 39.67 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24666151 204 YPVLQAADIMLYKSTHVPVGADQiQHIQLaqhLARIYngrygetfpvcTAIIEDGDASRVLS------LRDPSKKMSKSe 277
Cdd:PTZ00126 198 YPCMQCADIFYLKADICQLGMDQ-RKVNM---LAREY-----------CDKKKIKKKPIILShhmlpgLLEGQEKMSKS- 261
|
90 100
....*....|....*....|...
gi 24666151 278 aNPKATINLCDSPDLITQKIKKA 300
Cdd:PTZ00126 262 -DPNSAIFMEDSEEDVNRKIKKA 283
|
|
|