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Conserved domains on  [gi|575446676|gb|AHG78826|]
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Tryptophanyl-tRNA synthetase [Mannheimia varigena USDA-ARS-USMARC-1388]

Protein Classification

tryptophan--tRNA ligase( domain architecture ID 11479345)

tryptophan--tRNA ligase is a class I tRNA synthetase and aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA

EC:  6.1.1.2
Gene Ontology:  GO:0006436|GO:0004830|GO:0005524

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
11-351 0e+00

tryptophanyl-tRNA synthetase; Reviewed


:

Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 600.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  11 KPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIFIQ 90
Cdd:PRK00927   1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  91 SHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:PRK00927  81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGkkdaegnviePVFAVPEVFIAKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKAVAKKIKRAMTDGDEPPV 250
Cdd:PRK00927 161 RFNNLYG----------EVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLRE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 251 VRYDVQNKAGVSNLLDILSAITGKTIAELEAEFE--GKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIYREGA 328
Cdd:PRK00927 231 IRYDLPNKPEVSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGA 310
                        330       340
                 ....*....|....*....|...
gi 575446676 329 DKARARARATLDKVYELVGFVRY 351
Cdd:PRK00927 311 EKARAVASKTLKEVREAMGLLRK 333
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
11-351 0e+00

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 600.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  11 KPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIFIQ 90
Cdd:PRK00927   1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  91 SHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:PRK00927  81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGkkdaegnviePVFAVPEVFIAKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKAVAKKIKRAMTDGDEPPV 250
Cdd:PRK00927 161 RFNNLYG----------EVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLRE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 251 VRYDVQNKAGVSNLLDILSAITGKTIAELEAEFE--GKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIYREGA 328
Cdd:PRK00927 231 IRYDLPNKPEVSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGA 310
                        330       340
                 ....*....|....*....|...
gi 575446676 329 DKARARARATLDKVYELVGFVRY 351
Cdd:PRK00927 311 EKARAVASKTLKEVREAMGLLRK 333
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
9-351 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: 550.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   9 MTKPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIF 88
Cdd:COG0180    1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  89 IQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARY-EENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRD 167
Cdd:COG0180   81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 168 IANRFNVLYGkkdaegnviePVFAVPEVFIAKSGARVMSlLEPTKKMSKSDdnrNNVIGLLEDPKAVAKKIKRAMTDGDE 247
Cdd:COG0180  161 IARRFNHRYG----------EVFPEPEALIPEEGARIPG-LDGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSER 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 248 ppvVRYDVQNKAGVSNLLDILSAITGK-TIAELEAEFE--GKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIY 324
Cdd:COG0180  227 ---LRYDDPGKPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEIL 303
                        330       340
                 ....*....|....*....|....*..
gi 575446676 325 REGADKARARARATLDKVYELVGFVRY 351
Cdd:COG0180  304 AEGAEKARAIAAKTLAEVREAMGLLYF 330
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
13-302 4.08e-141

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: 401.19  E-value: 4.08e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  13 IVFSGVQPSGELTIGNYLGALRNWVKMQD-DYDCVYCIVDQHAITVRQ-DPEALRKSTLDVLALYLACGIDPNKSTIFIQ 90
Cdd:cd00806    1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  91 SHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSArYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:cd00806   81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGkkdaegnviePVFAVPEVFIAKsGARVMSLLEPTKKMSKSDDnrNNVIGLLEDPKAVAKKIKRAMTDGDepPV 250
Cdd:cd00806  160 RFNKLYG----------EIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGG--RT 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 575446676 251 VRYDVQNKAGVSNLLDILSAITGKTIAELEA----EFEGKMYGHLKTEVADKVSEL 302
Cdd:cd00806  225 EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQEF 280
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
11-348 1.64e-138

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: 396.32  E-value: 1.64e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   11 KPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQ-DPEALRKSTLDVLALYLACGIDPNKSTIFI 89
Cdd:TIGR00233   2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   90 QSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSarYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIA 169
Cdd:TIGR00233  82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  170 NRFNVLYGKKdaegnviepvFAVPEVFIAKSGARVMSLlePTKKMSKSDDnrNNVIGLLEDPKAVAKKIKRAMTDGDEPp 249
Cdd:TIGR00233 160 ERFNKKFKNF----------FPKPESLISKFFPRLMGL--SGKKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  250 vVRYDVQNKAGVSNLLDILSAITGKTI------AELEAEFEGK-MYGHLKTEVADKVSELLTNLQERYHHYrqDEALLEK 322
Cdd:TIGR00233 225 -TLFEHREKPGVPNLLVIYQYLSFFLIdddklkEIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEI--AEEILDK 301
                         330       340
                  ....*....|....*....|....*.
gi 575446676  323 IYREGADKARARARATLDKVYELVGF 348
Cdd:TIGR00233 302 ILEPGAKKARETANKTLADVYKAMGL 327
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
11-304 1.66e-92

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 278.01  E-value: 1.66e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   11 KPIVFSGVQPSGELTIGnYLGALRNWVKMQDD-YDCVYCIVDQHAITVRQD---PEALRKSTLDVLAL---YLACGIDPN 83
Cdd:pfam00579   5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   84 KSTIFIQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEEN--VNVGLFTYPVLMAADILLYQANQVPVGDDQKQH 161
Cdd:pfam00579  84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGpgISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  162 LEITRDIANRFNvlygkkdaegnviEPVFAVPEVFIAKsgarVMSLLEPTKKMSKSDDNRnnVIGLLEDPKAVAKKIKRA 241
Cdd:pfam00579 164 IELGRDLARRFN-------------KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKA 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  242 MTDGDEppVVRYDVQNKAGVSN-LLDILSAITGKTI----AELEAEFEGKM--YGHLKTEVADKVSELLT 304
Cdd:pfam00579 225 YTDPDR--EVRKDLKLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
11-351 0e+00

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 600.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  11 KPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIFIQ 90
Cdd:PRK00927   1 KKRVLSGIQPTGKLHLGNYLGAIKNWVELQDEYECFFCIADLHALTVPQDPEELRENTRELAADYLACGIDPEKSTIFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  91 SHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:PRK00927  81 SHVPEHAELAWILNCITPLGELERMTQFKDKSAKQKENVSAGLFTYPVLMAADILLYKADLVPVGEDQKQHLELTRDIAR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGkkdaegnviePVFAVPEVFIAKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKAVAKKIKRAMTDGDEPPV 250
Cdd:PRK00927 161 RFNNLYG----------EVFPVPEPLIPKVGARVMGLDGPTKKMSKSDPNDNNTINLLDDPKTIAKKIKKAVTDSERLRE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 251 VRYDVQNKAGVSNLLDILSAITGKTIAELEAEFE--GKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIYREGA 328
Cdd:PRK00927 231 IRYDLPNKPEVSNLLTIYSALSGESIEELEAEYEagGKGYGDFKKDLAEAVVEFLAPIRERYEELLADPAYLDEILAEGA 310
                        330       340
                 ....*....|....*....|...
gi 575446676 329 DKARARARATLDKVYELVGFVRY 351
Cdd:PRK00927 311 EKARAVASKTLKEVREAMGLLRK 333
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
9-351 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: 550.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   9 MTKPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIF 88
Cdd:COG0180    1 MSKKRVLSGIQPTGRLHLGNYLGALKNWVELQDEYECFFFIADLHALTTPQDPEELRENTREVAADYLAAGLDPEKSTIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  89 IQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARY-EENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRD 167
Cdd:COG0180   81 VQSDVPEHAELAWLLSCLTPLGELERMPQFKDKSAKNgKENVNAGLLTYPVLMAADILLYKADLVPVGEDQKQHLELTRD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 168 IANRFNVLYGkkdaegnviePVFAVPEVFIAKSGARVMSlLEPTKKMSKSDdnrNNVIGLLEDPKAVAKKIKRAMTDGDE 247
Cdd:COG0180  161 IARRFNHRYG----------EVFPEPEALIPEEGARIPG-LDGRKKMSKSY---GNTINLLDDPKEIRKKIKSAVTDSER 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 248 ppvVRYDVQNKAGVSNLLDILSAITGK-TIAELEAEFE--GKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIY 324
Cdd:COG0180  227 ---LRYDDPGKPEVCNLFTIYSAFSGKeEVEELEAEYRagGIGYGDLKKALAEAVVEFLAPIRERRAELLADPAELDEIL 303
                        330       340
                 ....*....|....*....|....*..
gi 575446676 325 REGADKARARARATLDKVYELVGFVRY 351
Cdd:COG0180  304 AEGAEKARAIAAKTLAEVREAMGLLYF 330
PLN02886 PLN02886
aminoacyl-tRNA ligase
9-351 8.39e-145

aminoacyl-tRNA ligase


Pssm-ID: 215478 [Multi-domain]  Cd Length: 389  Bit Score: 414.60  E-value: 8.39e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   9 MTKPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIF 88
Cdd:PLN02886  44 ARKKRVVSGVQPTGSIHLGNYLGAIKNWVALQETYDTFFCVVDLHAITLPHDPRELGKATRSTAAIYLACGIDPSKASVF 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  89 IQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARY-EENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRD 167
Cdd:PLN02886 124 VQSHVPAHAELMWLLSCSTPIGWLNKMIQFKEKSRKAgDENVGVGLLTYPVLMASDILLYQADLVPVGEDQKQHLELTRD 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 168 IANRFNVLYG--KKDAEGNVIEPVFAVPEVFIAKSGARVMSLLEPTKKMSKSDDNRNNVIGLLEDPKAVAKKIKRAMTDG 245
Cdd:PLN02886 204 IAERVNNLYGgrKWKKLGGRGGSVFKVPEALIPPAGARVMSLTDGTSKMSKSAPSDQSRINLLDPPDVIANKIKRCKTDS 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 246 dePPVVRYDVQNKAGVSNLLDILSAITGKTIAELEAEFEGKMYGHLKTEVADKVSELLTNLQERYHHYRQDEALLEKIYR 325
Cdd:PLN02886 284 --FPGLEFDNPERPECNNLLSIYQLVTGKTKEEVLAECGDMRWGDFKPLLTDALIEHLSPIQVRYEEIMSDPSYLDSVLK 361
                        330       340
                 ....*....|....*....|....*.
gi 575446676 326 EGADKARARARATLDKVYELVGFVRY 351
Cdd:PLN02886 362 EGADAAAEIADRTLANVYQAMGFVQR 387
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
13-302 4.08e-141

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: 401.19  E-value: 4.08e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  13 IVFSGVQPSGELTIGNYLGALRNWVKMQD-DYDCVYCIVDQHAITVRQ-DPEALRKSTLDVLALYLACGIDPNKSTIFIQ 90
Cdd:cd00806    1 RVLSGIQPSGSLHLGHYLGAFRFWVWLQEaGYELFFFIADLHALTVKQlDPEELRQNTRENAKDYLACGLDPEKSTIFFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  91 SHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSArYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:cd00806   81 SDVPEHYELAWLLSCVVTFGELERMTGFKDKSA-QGESVNIGLLTYPVLQAADILLYKACLVPVGIDQDPHLELTRDIAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGkkdaegnviePVFAVPEVFIAKsGARVMSLLEPTKKMSKSDDnrNNVIGLLEDPKAVAKKIKRAMTDGDepPV 250
Cdd:cd00806  160 RFNKLYG----------EIFPKPAALLSK-GAFLPGLQGPSKKMSKSDP--NNAIFLTDSPKEIKKKIMKAATDGG--RT 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 575446676 251 VRYDVQNKAGVSNLLDILSAITGKTIAELEA----EFEGKMYGHLKTEVADKVSEL 302
Cdd:cd00806  225 EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEideyRSGGLGYGECKKLLAEAIQEF 280
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
11-348 1.64e-138

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: 396.32  E-value: 1.64e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   11 KPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVRQ-DPEALRKSTLDVLALYLACGIDPNKSTIFI 89
Cdd:TIGR00233   2 KFRVLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAITVKQtDPDALRKAREELAADYLAVGLDPEKTFIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   90 QSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSarYEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIA 169
Cdd:TIGR00233  82 QSDYPEHYELAWLLSCQVTFGELKRMTQFKDKS--QAENVPIGLLSYPVLQAADILLYQADLVPVGIDQDQHLELTRDLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  170 NRFNVLYGKKdaegnviepvFAVPEVFIAKSGARVMSLlePTKKMSKSDDnrNNVIGLLEDPKAVAKKIKRAMTDGDEPp 249
Cdd:TIGR00233 160 ERFNKKFKNF----------FPKPESLISKFFPRLMGL--SGKKMSKSDP--NSAIFLTDTPKQIKKKIRKAATDGGRV- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  250 vVRYDVQNKAGVSNLLDILSAITGKTI------AELEAEFEGK-MYGHLKTEVADKVSELLTNLQERYHHYrqDEALLEK 322
Cdd:TIGR00233 225 -TLFEHREKPGVPNLLVIYQYLSFFLIdddklkEIYEAYKSGKlGYGECKKALIEVLQEFLKEIQERRAEI--AEEILDK 301
                         330       340
                  ....*....|....*....|....*.
gi 575446676  323 IYREGADKARARARATLDKVYELVGF 348
Cdd:TIGR00233 302 ILEPGAKKARETANKTLADVYKAMGL 327
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
10-347 5.48e-97

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 290.99  E-value: 5.48e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  10 TKPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAIT-VRQDPEALRKSTLDVLALYLACGIDPNKSTIF 88
Cdd:PRK12282   1 TKPIILTGDRPTGKLHLGHYVGSLKNRVALQNEHEQFVLIADQQALTdNAKNPEKIRRNILEVALDYLAVGIDPAKSTIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  89 IQSHVPEHAQLAWV-LNCYTyFGEMSRMTQFKDKSAR--YEENVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEIT 165
Cdd:PRK12282  81 IQSQIPELAELTMYyMNLVT-VARLERNPTVKTEIAQkgFGRSIPAGFLTYPVSQAADITAFKATLVPVGDDQLPMIEQT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 166 RDIANRFNVLYGkkdaegnviEPVFAVPEVFIAKSGaRVMSlLEPTKKMSKSDdnrNNVIGLLEDPKAVAKKIKRAMTDg 245
Cdd:PRK12282 160 REIVRRFNSLYG---------TDVLVEPEALLPEAG-RLPG-LDGKAKMSKSL---GNAIYLSDDADTIKKKVMSMYTD- 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 246 dePPVVRYDVQNKAGVSNLLDILSAI--TGKTIAELEAEFEGKMYG--HLKTEVADKVSELLTNLQERYHHYRQDEALLE 321
Cdd:PRK12282 225 --PNHIRVEDPGKVEGNVVFTYLDAFdpDKAEVAELKAHYQRGGLGdvKCKRYLEEVLQELLAPIRERRAEFAKDPGYVL 302
                        330       340
                 ....*....|....*....|....*.
gi 575446676 322 KIYREGADKARARARATLDKVYELVG 347
Cdd:PRK12282 303 EILKAGSEKAREVAAQTLSEVKDAMG 328
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
11-304 1.66e-92

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 278.01  E-value: 1.66e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   11 KPIVFSGVQPSGELTIGnYLGALRNWVKMQDD-YDCVYCIVDQHAITVRQD---PEALRKSTLDVLAL---YLACGIDPN 83
Cdd:pfam00579   5 PLRVYSGIDPTGPLHLG-YLVPLMKLRQFQQAgHEVFFLIGDLHAIIGDPSkspERKLLSRETVLENAikaQLACGLDPE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   84 KSTIFIQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEEN--VNVGLFTYPVLMAADILLYQANQVPVGDDQKQH 161
Cdd:pfam00579  84 KAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQGpgISLGEFTYPLLQAYDILLLKADLQPGGSDQWGN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  162 LEITRDIANRFNvlygkkdaegnviEPVFAVPEVFIAKsgarVMSLLEPTKKMSKSDDNRnnVIGLLEDPKAVAKKIKRA 241
Cdd:pfam00579 164 IELGRDLARRFN-------------KKIFKKPVGLTNP----LLTGLDGGKKMSKSAGNS--AIFLDDDPESVYKKIQKA 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  242 MTDGDEppVVRYDVQNKAGVSN-LLDILSAITGKTI----AELEAEFEGKM--YGHLKTEVADKVSELLT 304
Cdd:pfam00579 225 YTDPDR--EVRKDLKLFTFLSNeEIEILEAELGKSPyreaEELLAREVTGLvhGGDLKKAAAEAVNKLLQ 292
PRK12556 PRK12556
tryptophanyl-tRNA synthetase; Provisional
9-348 9.43e-80

tryptophanyl-tRNA synthetase; Provisional


Pssm-ID: 183592 [Multi-domain]  Cd Length: 332  Bit Score: 246.94  E-value: 9.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676   9 MTKPIVFSGVQPSGELTIGNYLGALRNWVKMQDDYDC--VYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKST 86
Cdd:PRK12556   1 MSEKIMLTGIKPTGYPHLGNYIGAIKPALQMAKNYEGkaLYFIADYHALNAVHDPEQFRSYTREVAATWLSLGLDPEDVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  87 IFIQSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEE-------NVNVGLFTYPVLMAADILLYQANQVPVGDDQK 159
Cdd:PRK12556  81 FYRQSDVPEIFELAWILSCLTPKGLMNRAHAYKAKVDQNKEagldldaGVNMGLYTYPILMAADILLFQATHVPVGKDQI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 160 QHLEITRDIANRFNVLYGKkdaegnviepVFAVPEVFIAKSGArVMSLLEpTKKMSKSDDnrnNVIGLLEDPKAVAKKIK 239
Cdd:PRK12556 161 QHIEIARDIATYFNHTFGD----------TFTLPEYVIQEEGA-ILPGLD-GRKMSKSYG---NVIPLFAEQEKLRKLIF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 240 RAMTDgDEPPVVRYDVQNkagvSNLLDILSAI-TGKTIAELEAEFEGKM-YGHLKTEVADKVSELLTNLQERYHHYRQDE 317
Cdd:PRK12556 226 KIKTD-SSLPNEPKDPET----SALFTIYKEFaTEEEVQSMREKYETGIgWGDVKKELFRVVDRELAGPREKYAMYMNEP 300
                        330       340       350
                 ....*....|....*....|....*....|.
gi 575446676 318 ALLEKIYREGADKARARARATLDKVYELVGF 348
Cdd:PRK12556 301 SLLDEALEKGAERAREIAKPNLAEIKKAIGF 331
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
14-347 1.62e-70

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 225.22  E-value: 1.62e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  14 VFSGVQPSGELTIGNYLGALRNWVKMQDDYDCVYCIVDQHAITVR-QDPEALRKSTLDVLALYLACGIDPNKSTIFIQSH 92
Cdd:PRK12283   5 VLSGMRPTGRLHLGHYHGVLKNWVKLQHEYECFFFVADWHALTTHyETPEVIEKNVWDMVIDWLAAGVDPAQATLFIQSK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  93 VPEHAQLAWVLNCYTYFGEMSRMTQFKDKSARYEEN--VNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEITRDIAN 170
Cdd:PRK12283  85 VPEHAELHLLLSMITPLGWLERVPTYKDQQEKLKEKdlSTYGFLGYPLLQSADILIYRAGLVPVGEDQVPHVEMTREIAR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 171 RFNVLYGK-KDAEGNVIEPV--------------------------FAVPEVFIAKS----------------GARVMSL 207
Cdd:PRK12283 165 RFNHLYGRePGFEEKAEAAIkklgkkraklyhelrnayqeegddeaLEQARALLQEQqnlsmgdrerlfgyleGAGKIIL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 208 LEP----TK----------KMSKSddnRNNVIGLLEDPKAVAKKIKRAMTD---------GDeP---PV-----VRYDVQ 256
Cdd:PRK12283 245 PEPqallTEaskmpgldgqKMSKS---YGNTIGLREDPESVTKKIRTMPTDparvrrtdpGD-PekcPVwqlhqVYSDEE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 257 NKAGVSNlldilsAITGKTIAELEAefegkmyghlKTEVADKVSELLTNLQERYHHYRQDEALLEKIYREGADKARARAR 336
Cdd:PRK12283 321 TKEWVQK------GCRSAGIGCLEC----------KQPVIDAILREQQPMRERAQKYEDDPSLVRAIVADGCEKARKVAR 384
                        410
                 ....*....|.
gi 575446676 337 ATLDKVYELVG 347
Cdd:PRK12283 385 ETMRDVREAMG 395
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
14-347 4.85e-63

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 206.78  E-value: 4.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  14 VFSGVQPSGELTIGNYLGALRNWVKM--QDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGIDPNKSTIFIQS 91
Cdd:PRK12284   5 VLTGITTTGTPHLGNYAGAIRPAIAAsrQPGVESFYFLADYHALIKCDDPARIQRSTLEIAATWLAAGLDPERVTFYRQS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  92 HVPEHAQLAWVLNCYTYFGEMSRMTQFK---DK-SARYEE---NVNVGLFTYPVLMAADILLYQANQVPVGDDQKQHLEI 164
Cdd:PRK12284  85 DIPEIPELTWLLTCVAGKGLLNRAHAYKaavDKnVAAGEDpdaGVTAGLFMYPVLMAADILMFNAHKVPVGRDQIQHIEM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 165 TRDIANRFNVLYGKKdaegnviepVFAVPEVFIAKSGARVMSLlePTKKMSKSDDnrnNVIGLLEDPKAVAKKIKRAMTD 244
Cdd:PRK12284 165 ARDIAQRFNHLYGGE---------FFVLPEAVIEESVATLPGL--DGRKMSKSYD---NTIPLFAPREELKKAIFSIVTD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 245 GDEPPVVRyDVQNkagvSNLLDILSAI-TGKTIAELEAEFEGKM-YGHLKTEVADKVSELLTNLQERYHHYRQDEALLEK 322
Cdd:PRK12284 231 SRAPGEPK-DTEG----SALFQLYQAFaTPEETAAFRQALADGIgWGDAKQRLFERIDRELAPMRERYEALIARPADIED 305
                        330       340
                 ....*....|....*....|....*
gi 575446676 323 IYREGADKARARARATLDKVYELVG 347
Cdd:PRK12284 306 ILLAGAAKARRIATPFLAELREAVG 330
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
14-302 1.85e-55

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: 182.50  E-value: 1.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  14 VFSGVQPSGE-LTIGNYLGaLRNWVKMQD-DYDCVYCIVDQHAITV----------RQDPEALRKSTLDVLALYLACGID 81
Cdd:cd00395    2 LYCGIDPTADsLHIGHLIG-LLTFRRFQHaGHRPIFLIGGQTGIIGdpsgkksertLNDPEEVRQNIRRIAAQYLAVGIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  82 --PNKSTIFIQSHVP---EHAQLAWVLNCYTYFGEMSRMTQFKDKSaryEENVNVGLFTYPVLMAADILLYQANQ----V 152
Cdd:cd00395   81 edPTQATLFNNSDWPgplAHIQFLRDLGKHVYVNYMERKTSFQSRS---EEGISATEFTYPPLQAADFLLLNTTEgcdiQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 153 PVGDDQKQHLEITRDIANRFNvlyGKKDAEGNVIepvfavpevfiaksgARVMSLLEPtkKMSKSDDNRNNVIGLLEDPK 232
Cdd:cd00395  158 PGGSDQWGNITLGRELARRFN---GFTIAEGLTI---------------PLVTKLDGP--KFGKSESGPKWLDTEKTSPY 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575446676 233 AVAKKIKRAMtdgdeppvvrydvqnkagVSNLLDILSAITGKTIAELEA----EFEGKMYGHLKTEVADKVSEL 302
Cdd:cd00395  218 EFYQFWINAV------------------DSDVINILKYFTFLSKEEIERleqeQYEAPGYRVAQKTLAEEVTKT 273
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
14-310 1.29e-24

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 102.64  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  14 VFSGVQPSGELTIGNYL--GALRNWVKMQDDydcVY-CIVDQHAITVR-QDPEALRKSTLDVLALYLACGIDPNKSTIFI 89
Cdd:PRK12285  69 VYTGFMPSGPMHIGHKMvfDELKWHQEFGAN---VYiPIADDEAYAARgLSWEETREWAYEYILDLIALGFDPDKTEIYF 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  90 QSHVPEHAQLAWVLNCYTYFGEMSRMTQFKDKSaryeenvNVGLFTYPVLMAADILLYQANQ------VPVGDDQKQHLE 163
Cdd:PRK12285 146 QSENIKVYDLAFELAKKVNFSELKAIYGFTGET-------NIGHIFYPATQAADILHPQLEEgpkptlVPVGIDQDPHIR 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 164 ITRDIANRFNVLYGkkdaegnviepvfavpevFIAKSG--ARVMSLLEPTkKMSKSDDnrNNVIGLLEDPKAVAKKIKRA 241
Cdd:PRK12285 219 LTRDIAERLHGGYG------------------FIKPSStyHKFMPGLTGG-KMSSSKP--ESAIYLTDDPETVKKKIMKA 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 242 MTDG--------------DEPPVvrYDvqnkagvsnLLDILSAITGKTIAELEAEF-EGK-MYGHLKTEVADKVSELLTN 305
Cdd:PRK12285 278 LTGGratleeqrklggepDECVV--YE---------LLLYHLEEDDKELKEIYEECrSGElLCGECKKEAAEKIAEFLKE 346

                 ....*
gi 575446676 306 LQERY 310
Cdd:PRK12285 347 HQEKR 351
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
13-218 4.50e-09

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: 54.41  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  13 IVFSGVQPSGELTIGNYLGALRNWVKMQD------DYDCVYCIVDQHAITVRQDPEALRkstldvlalylacgidpnkst 86
Cdd:cd00802    1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPANKKGE--------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  87 ifiqshVPEHAQLAWvlncytyfgemsrmtqfkdkSARYEEnvnvgLFTYPVLMAADILLYQANQ---VPVGDDQKQHLE 163
Cdd:cd00802   60 ------NAKAFVERW--------------------IERIKE-----DVEYMFLQAADFLLLYETEcdiHLGGSDQLGHIE 108
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 575446676 164 ITRDIANRFnvlYGKKDAEGNVIEpvfavpevfiaksgaRVMSllEPTKKMSKSD 218
Cdd:cd00802  109 LGLELLKKA---GGPARPFGLTFG---------------RVMG--ADGTKMSKSK 143
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
112-302 4.50e-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: 56.46  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 112 MSRMTQFKDKSARYEENVNVGL--FTYPVLMAADIL-LYQANQVPvGDDQKQHLEITRDIANRfnvlYGKKdaegnvieP 188
Cdd:cd00805  113 VNRMLRRDAVKVRLEEEEGISFseFIYPLLQAYDFVyLDVDLQLG-GSDQRGNITLGRDLIRK----LGYK--------K 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 189 VFAVpevfiaksgarVMSLLEPT--KKMSKSDDNrNNVIGLLEDPKAVAKKIKRAmtdgdeppvvrYDvqnkAGVSNLLD 266
Cdd:cd00805  180 VVGL-----------TTPLLTGLdgGKMSKSEGN-AIWDPVLDSPYDVYQKIRNA-----------FD----PDVLEFLK 232
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 575446676 267 ILSAITGKTIAELEAEF-EGKMYGHLKTEVADKVSEL 302
Cdd:cd00805  233 LFTFLDYEEIEELEEEHaEGPLPRDAKKALAEELTKL 269
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
11-241 1.97e-05

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 46.01  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  11 KPIVFSGVQPSGELTIGNYLgalrnWV-KMQD----DYDCVYCIVDQHA-ITVRQDPEALRKSTLDVLALYLACGIDPNK 84
Cdd:PRK08560  30 EPKAYIGFEPSGKIHLGHLL-----TMnKLADlqkaGFKVTVLLADWHAyLNDKGDLEEIRKVAEYNKKVFEALGLDPDK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676  85 STIF----IQSHvPEHAQLAWVLNCYTyfgEMSRMTQFKDKSARYEENVNVGLFTYPVLMAADIlLYQANQVPVG--DDQ 158
Cdd:PRK08560 105 TEFVlgseFQLD-KEYWLLVLKLAKNT---TLARARRSMTIMGRRMEEPDVSKLVYPLMQVADI-FYLDVDIAVGgmDQR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 159 KQHLeITRDIANRFNVlygKKdaegnviePVfAVPEVFIAksgarvmSLLEPTKKMSKSDDnrNNVIGLLEDPKAVAKKI 238
Cdd:PRK08560 180 KIHM-LAREVLPKLGY---KK--------PV-CIHTPLLT-------GLDGGGIKMSKSKP--GSAIFVHDSPEEIRRKI 237

                 ...
gi 575446676 239 KRA 241
Cdd:PRK08560 238 KKA 240
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
14-81 2.06e-04

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: 40.21  E-value: 2.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575446676  14 VFSGVQPsGELTIGNYLGALRNwvkMQDDYDCVYCIVDQHAITVRQDPEALRKSTLDVLALYLACGID 81
Cdd:cd02156    2 ARFPGEP-GYLHIGHAKLICRA---KGIADQCVVRIDDNPPVKVWQDPHELEERKESIEEDISVCGED 65
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
136-323 3.21e-04

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 42.37  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 136 YPVLMAADILLYQANQVPVGDDQKQHLEITRDIANRfnvlygKKDAEGNVIepvfavpevfiaKSGARVMSLLEPTKKMS 215
Cdd:PTZ00126 198 YPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDK------KKIKKKPII------------LSHHMLPGLLEGQEKMS 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575446676 216 KSDDnrNNVIGLLEDPKAVAKKIKRA-----MTDGDepPVVRYDVQNKAGVSNLLDILSA------ITGKTIAELEAEF- 283
Cdd:PTZ00126 260 KSDP--NSAIFMEDSEEDVNRKIKKAycppgVIEGN--PILAYFKSIVFPAFNSFTVLRKeknggdVTYTTYEELEKDYl 335
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 575446676 284 EGKMY-GHLKTEVADKVSELltnLQERYHHYRQDE---ALLEKI 323
Cdd:PTZ00126 336 SGALHpGDLKPALAKYLNLM---LQPVRDHFQNNPeakSLLSEV 376
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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