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Conserved domains on  [gi|503441629|ref|WP_013676290|]
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MULTISPECIES: tyrosine--tRNA ligase [Pseudonocardia]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11415010)

tyrosine--tRNA ligase catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr)

CATH:  1.10.240.10|3.40.50.620
EC:  6.1.1.1
Gene Ontology:  GO:0004831|GO:0006437|GO:0005524|GO:0003723
PubMed:  12458790|10447505|8274143|1852601|2053131|11590011|10704480

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 65-462 9.69e-135

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


:

Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 394.02  E-value: 9.69e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  65 DALAARIvsaaeKGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDI 144
Cdd:COG0162   19 EELREKL-----AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLTEEQV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 145 EHNLATYREQVSPFFDFD--RAHFRRNGDWLRKITLPEIIG-ITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMA 221
Cdd:COG0162   94 AENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYPLLQG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 222 LDSVEI----NCDLEVGGIDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTA---APGEIFG 294
Cdd:COG0162  174 YDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGT--KMGKSEGNAIWLDEektSPYEFYQ 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 295 KIMSVPDRLVEPYFRALSEWLDAELAVAAERVAAGTlHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAevD 374
Cdd:COG0162  252 KWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGELP--D 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 375 DLPTV----ADLGVSVTEAVKALGFAASNGDVRRVAQQNGLRLvveaDGEQeqlsltADDARAVLAdlVKDRLDGKTgdY 450
Cdd:COG0162  329 DLPEVelsaAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSV----NGEK------VTDPDAVLT--AGDLLHGGY--L 394

                        410
                 ....*....|...
gi 503441629 451 FLKVG-RKLARIR 462
Cdd:COG0162  395 VLRVGkKKFALVK 407
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 65-462 9.69e-135

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 394.02  E-value: 9.69e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  65 DALAARIvsaaeKGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDI 144
Cdd:COG0162   19 EELREKL-----AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLTEEQV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 145 EHNLATYREQVSPFFDFD--RAHFRRNGDWLRKITLPEIIG-ITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMA 221
Cdd:COG0162   94 AENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYPLLQG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 222 LDSVEI----NCDLEVGGIDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTA---APGEIFG 294
Cdd:COG0162  174 YDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGT--KMGKSEGNAIWLDEektSPYEFYQ 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 295 KIMSVPDRLVEPYFRALSEWLDAELAVAAERVAAGTlHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAevD 374
Cdd:COG0162  252 KWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGELP--D 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 375 DLPTV----ADLGVSVTEAVKALGFAASNGDVRRVAQQNGLRLvveaDGEQeqlsltADDARAVLAdlVKDRLDGKTgdY 450
Cdd:COG0162  329 DLPEVelsaAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSV----NGEK------VTDPDAVLT--AGDLLHGGY--L 394

                        410
                 ....*....|...
gi 503441629 451 FLKVG-RKLARIR 462
Cdd:COG0162  395 VLRVGkKKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 65-457 1.15e-95

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 294.50  E-value: 1.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  65 DALAARIVSAAEKGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDI 144
Cdd:PRK13354  18 ETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 145 EHNLATYREQVSPFFDFDRAHFRRNGDWLRKITLPEII-GITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALD 223
Cdd:PRK13354  98 QHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 224 SVEIN----CDLEVGGIDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTAA---PGEIFGKI 296
Cdd:PRK13354 178 FVHLNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT--KMGKSAGGAIWLDPEktsPYEFYQFW 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 297 MSVPDRLVEPYFRALSEWLDAELAVAAERVAAGTlHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAEVDDL 376
Cdd:PRK13354 256 MNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 377 PT-VADLGVSVTEAVKALGFAASNGDVRRVAQQNGLRLvveaDGEQEqlsltaDDARAVLAdlVKDRLDGKTgdYFLKVG 455
Cdd:PRK13354 335 TFeVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKI----NGEKV------TDVDAIIN--PEDAFDGKF--VILRRG 400


                 ..
gi 503441629 456 RK 457
Cdd:PRK13354 401 KK 402
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 77-413 4.03e-80

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: 253.09  E-value: 4.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629   77 KGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDIEHNLATYREQVS 156
Cdd:TIGR00234  28 LERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTREEVQENAENIKKQIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  157 PFFDFDRAHFRRNGDWLRKITLPEIIGITAQI-PVSMSLQREDFRKRLDAgqGLSLAELMYSIVMALDSVEINCDLEVGG 235
Cdd:TIGR00234 108 RFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEE--NISLHEFIYPLLQAYDFVYLNVDLQLGG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  236 IDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTAAPGEIFGKIMSVPDRLVEPYFRALSewl 315
Cdd:TIGR00234 186 SDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE--KMGKSLGGAVSLDEGKYDFYQKVINTPDELVKKYLKLFT--- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  316 DAELAVAAERVAAGTLHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAevDDLPTV----ADLGVSVTEAVK 391
Cdd:TIGR00234 261 FLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP--DEVPIFrpekFGGPITLADLLV 338

                         330       340
                  ....*....|....*....|..
gi 503441629  392 ALGFAASNGDVRRVAQQNGLRL 413
Cdd:TIGR00234 339 LSGLFPSKSEARRDIKNGGVYI 360
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 83-346 4.55e-69

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: 220.94  E-value: 4.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  83 AKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDIEHNLATYREQVSPFFDFD 162
Cdd:cd00805    3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILDFI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 163 ---RAHFRRNGDWLRKITLPEIIGITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALDSVEINCDLEVGGIDQF 239
Cdd:cd00805   83 ppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 240 LNMQMCRKVMEISGQVPELVVATSLIEGTDgtGAKMSKSKGNYV--PLTAAPGEIFGKIMSVPDRLVEPYFRALSEWLDA 317
Cdd:cd00805  163 GNITLGRDLIRKLGYKKVVGLTTPLLTGLD--GGKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDYE 240

                        250       260
                 ....*....|....*....|....*....
gi 503441629 318 ELAVAAERVAAGTLhPMDLKKVLAGEVTA 346
Cdd:cd00805  241 EIEELEEEHAEGPL-PRDAKKALAEELTK 268
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
76-366 5.35e-56

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 187.87  E-value: 5.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629   76 EKGRPFVAKFGIDPTGAeVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSgRSDDRPALTDEDIEHNlaTYREQV 155
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  156 SPFFDFDRAHFRRNGDWLRKITLPEIIG-ITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALDSVEINCDLEVG 234
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  235 GIDQFLNMQM----CRKVMEISGQVPElVVATSLIEGTDGTGaKMSKSKGN----YVPLTAAPGEIFGKIMSVPDRLVEP 306
Cdd:pfam00579 157 GSDQWGNIELgrdlARRFNKKIFKKPV-GLTNPLLTGLDGGK-KMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRK 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503441629  307 YFRALSEWLDAELavaaERVAAGTLH--PMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFS 366
Cdd:pfam00579 235 DLKLFTFLSNEEI----EILEAELGKspYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 65-462 9.69e-135

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 394.02  E-value: 9.69e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  65 DALAARIvsaaeKGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDI 144
Cdd:COG0162   19 EELREKL-----AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEERKLLTEEQV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 145 EHNLATYREQVSPFFDFD--RAHFRRNGDWLRKITLPEIIG-ITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMA 221
Cdd:COG0162   94 AENAETIKEQVFKFLDFDdnKAEIVNNSDWLGKLSFIDFLRdLGKHFTVNRMLERDDVKKRLESGQGISFTEFSYPLLQG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 222 LDSVEI----NCDLEVGGIDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTA---APGEIFG 294
Cdd:COG0162  174 YDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGT--KMGKSEGNAIWLDEektSPYEFYQ 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 295 KIMSVPDRLVEPYFRALSEWLDAELAVAAERVAAGTlHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAevD 374
Cdd:COG0162  252 KWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGKGELP--D 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 375 DLPTV----ADLGVSVTEAVKALGFAASNGDVRRVAQQNGLRLvveaDGEQeqlsltADDARAVLAdlVKDRLDGKTgdY 450
Cdd:COG0162  329 DLPEVelsaAEGGIPLVDLLVEAGLAASKSEARRLIKQGGVSV----NGEK------VTDPDAVLT--AGDLLHGGY--L 394

                        410
                 ....*....|...
gi 503441629 451 FLKVG-RKLARIR 462
Cdd:COG0162  395 VLRVGkKKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 65-457 1.15e-95

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 294.50  E-value: 1.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  65 DALAARIVSAAEKGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDI 144
Cdd:PRK13354  18 ETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSGKSKERKLLTDEQV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 145 EHNLATYREQVSPFFDFDRAHFRRNGDWLRKITLPEII-GITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALD 223
Cdd:PRK13354  98 QHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 224 SVEIN----CDLEVGGIDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTAA---PGEIFGKI 296
Cdd:PRK13354 178 FVHLNrkedVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT--KMGKSAGGAIWLDPEktsPYEFYQFW 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 297 MSVPDRLVEPYFRALSEWLDAELAVAAERVAAGTlHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAEVDDL 376
Cdd:PRK13354 256 MNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIP 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 377 PT-VADLGVSVTEAVKALGFAASNGDVRRVAQQNGLRLvveaDGEQEqlsltaDDARAVLAdlVKDRLDGKTgdYFLKVG 455
Cdd:PRK13354 335 TFeVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKI----NGEKV------TDVDAIIN--PEDAFDGKF--VILRRG 400


                 ..
gi 503441629 456 RK 457
Cdd:PRK13354 401 KK 402
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 77-413 4.03e-80

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: 253.09  E-value: 4.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629   77 KGRPFVAKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDIEHNLATYREQVS 156
Cdd:TIGR00234  28 LERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILTREEVQENAENIKKQIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  157 PFFDFDRAHFRRNGDWLRKITLPEIIGITAQI-PVSMSLQREDFRKRLDAgqGLSLAELMYSIVMALDSVEINCDLEVGG 235
Cdd:TIGR00234 108 RFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEE--NISLHEFIYPLLQAYDFVYLNVDLQLGG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  236 IDQFLNMQMCRKVMEISGQVPELVVATSLIEGTDGTgaKMSKSKGNYVPLTAAPGEIFGKIMSVPDRLVEPYFRALSewl 315
Cdd:TIGR00234 186 SDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGE--KMGKSLGGAVSLDEGKYDFYQKVINTPDELVKKYLKLFT--- 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  316 DAELAVAAERVAAGTLHPMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFSRRTFAevDDLPTV----ADLGVSVTEAVK 391
Cdd:TIGR00234 261 FLGLEEIEQLVELKGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNP--DEVPIFrpekFGGPITLADLLV 338

                         330       340
                  ....*....|....*....|..
gi 503441629  392 ALGFAASNGDVRRVAQQNGLRL 413
Cdd:TIGR00234 339 LSGLFPSKSEARRDIKNGGVYI 360
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 83-346 4.55e-69

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: 220.94  E-value: 4.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  83 AKFGIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDIEHNLATYREQVSPFFDFD 162
Cdd:cd00805    3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILDFI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 163 ---RAHFRRNGDWLRKITLPEIIGITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALDSVEINCDLEVGGIDQF 239
Cdd:cd00805   83 ppeKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 240 LNMQMCRKVMEISGQVPELVVATSLIEGTDgtGAKMSKSKGNYV--PLTAAPGEIFGKIMSVPDRLVEPYFRALSEWLDA 317
Cdd:cd00805  163 GNITLGRDLIRKLGYKKVVGLTTPLLTGLD--GGKMSKSEGNAIwdPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDYE 240

                        250       260
                 ....*....|....*....|....*....
gi 503441629 318 ELAVAAERVAAGTLhPMDLKKVLAGEVTA 346
Cdd:cd00805  241 EIEELEEEHAEGPL-PRDAKKALAEELTK 268
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
76-366 5.35e-56

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 187.87  E-value: 5.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629   76 EKGRPFVAKFGIDPTGAeVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSgRSDDRPALTDEDIEHNlaTYREQV 155
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  156 SPFFDFDRAHFRRNGDWLRKITLPEIIG-ITAQIPVSMSLQREDFRKRLDAGQGLSLAELMYSIVMALDSVEINCDLEVG 234
Cdd:pfam00579  77 ACGLDPEKAEIVNNSDWLEHLELAWLLRdLGKHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  235 GIDQFLNMQM----CRKVMEISGQVPElVVATSLIEGTDGTGaKMSKSKGN----YVPLTAAPGEIFGKIMSVPDRLVEP 306
Cdd:pfam00579 157 GSDQWGNIELgrdlARRFNKKIFKKPV-GLTNPLLTGLDGGK-KMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRK 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503441629  307 YFRALSEWLDAELavaaERVAAGTLH--PMDLKKVLAGEVTAAIHGVDAAMKARDEFAARFS 366
Cdd:pfam00579 235 DLKLFTFLSNEEI----EILEAELGKspYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 86-345 2.20e-31

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: 121.64  E-value: 2.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  86 GIDPTGAEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSGRSDDRPALTDEDIEHNLATYREQVSPFFDFDRAH 165
Cdd:cd00395    5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGIFEDPT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 166 ---FRRNGDWLRKITLPEIIGITAQI-PVSMSLQREDFRKRLDagQGLSLAELMYSIVMALD----SVEINCDLEVGGID 237
Cdd:cd00395   85 qatLFNNSDWPGPLAHIQFLRDLGKHvYVNYMERKTSFQSRSE--EGISATEFTYPPLQAADflllNTTEGCDIQPGGSD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 238 QFLNMQMCRKVME-ISGQVPELVVATSLIEGTDGTgaKMSKSKGN---YVPLTAAPGEIFGKIMSVPDRLVEPYFRALSe 313
Cdd:cd00395  163 QWGNITLGRELARrFNGFTIAEGLTIPLVTKLDGP--KFGKSESGpkwLDTEKTSPYEFYQFWINAVDSDVINILKYFT- 239

                        250       260       270
                 ....*....|....*....|....*....|..
gi 503441629 314 WLDAELAVAAERVAAGTLHPMDLKKVLAGEVT 345
Cdd:cd00395  240 FLSKEEIERLEQEQYEAPGYRVAQKTLAEEVT 271
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 86-298 6.94e-14

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: 71.85  E-value: 6.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  86 GIDPTGAeVHLGHSVP-MQILSRFQRMGHDVVFIVGDM---TAKigdpsgrsDDRPALTDEDIEHNLATY------REQV 155
Cdd:cd00806    5 GIQPSGS-LHLGHYLGaFRFWVWLQEAGYELFFFIADLhalTVK--------QLDPEELRQNTRENAKDYlacgldPEKS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 156 SPFFDFDRAHFRRNGdWL--RKITLPEIIGITAqipvsmslqredFRKRLDAGQGLSLAELMYSIVMALDSVEINCDLEV 233
Cdd:cd00806   76 TIFFQSDVPEHYELA-WLlsCVVTFGELERMTG------------FKDKSAQGESVNIGLLTYPVLQAADILLYKACLVP 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503441629 234 GGIDQFLNMQMCRKVMEISGQ-------VPELVVA-TSLIEGTDGTGAKMSKSKG-NYVPLTAAPGEIFGKIMS 298
Cdd:cd00806  143 VGIDQDPHLELTRDIARRFNKlygeifpKPAALLSkGAFLPGLQGPSKKMSKSDPnNAIFLTDSPKEIKKKIMK 216
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 76-361 4.30e-12

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 66.81  E-value: 4.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629  76 EKGRPFVAKFGIDPTGaEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTAKIGDPSgrsddrpalTDEDIEHNLATYREQV 155
Cdd:PRK08560  26 ESKEEPKAYIGFEPSG-KIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLNDKG---------DLEEIRKVAEYNKKVF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 156 SPF-FDFDRAHFRRNGDWLRKitlPEIIGITAQIPVSMSLQR------EDFRKRLDAgqglSLAELMYSIVMALDSVEIN 228
Cdd:PRK08560  96 EALgLDPDKTEFVLGSEFQLD---KEYWLLVLKLAKNTTLARarrsmtIMGRRMEEP----DVSKLVYPLMQVADIFYLD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 229 CDLEVGGIDQflnmqmcRKVMEISGQV-PEL----VVA--TSLIEGTDGTGAKMSKSK-GNYVPLTAAPGEIFGKIMSV- 299
Cdd:PRK08560 169 VDIAVGGMDQ-------RKIHMLAREVlPKLgykkPVCihTPLLTGLDGGGIKMSKSKpGSAIFVHDSPEEIRRKIKKAy 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 300 -PDRLVE-------------PYFRA------------LSEWLDAELAVAaerVAAGTLHPMDLKKVLAGEVTAAIHGVDA 353
Cdd:PRK08560 242 cPPGEVEgnpvleiakyhifPRYDPfvierpekyggdLEYESYEELERD---YAEGKLHPMDLKNAVAEYLIEILEPVRE 318


                 ....*...
gi 503441629 354 AMKARDEF 361
Cdd:PRK08560 319 YLEEGPEL 326
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 255-341 5.59e-07

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: 51.20  E-value: 5.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 255 VPELVV--ATSLIEGTDGTgAKMSKSKGNYVPLTAAPGEIFGKIMSV---PDRLV--EP----------YFRALSEwlDA 317
Cdd:COG0180  175 EPEALIpeEGARIPGLDGR-KKMSKSYGNTINLLDDPKEIRKKIKSAvtdSERLRydDPgkpevcnlftIYSAFSG--KE 251

                         90       100
                 ....*....|....*....|....
gi 503441629 318 ELAVAAERVAAGTLHPMDLKKVLA 341
Cdd:COG0180  252 EVEELEAEYRAGGIGYGDLKKALA 275
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 70-124 6.19e-05

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 44.86  E-value: 6.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503441629  70 RIVSAAEKGRPFVAKFGIDPTGaEVHLGHSVPMQILSRFQRMGHDVVFIVGDMTA 124
Cdd:PRK12285  56 KILEAYRNGKPFAVYTGFMPSG-PMHIGHKMVFDELKWHQEFGANVYIPIADDEA 109
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 255-348 8.76e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 41.23  E-value: 8.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503441629 255 VPELVV--ATSLIEGTDGTGAKMSKSKG---NYVPLTAAPGEIFGKIMSV---PDRLVEP---------------YFRAL 311
Cdd:PRK00927 172 VPEPLIpkVGARVMGLDGPTKKMSKSDPndnNTINLLDDPKTIAKKIKKAvtdSERLREIrydlpnkpevsnlltIYSAL 251

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503441629 312 SewlDAELAVAAERVAAGTLHPMDLKKVLAGEVTAAI 348
Cdd:PRK00927 252 S---GESIEELEAEYEAGGKGYGDFKKDLAEAVVEFL 285
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
 230-283 2.67e-03

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 40.09  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 503441629  230 DLEVGGIDQ--FLNMQMCRKVMEISGQVP-ELVVATSLIegTDGTGAKMSKSKGNYV 283
Cdd:pfam00133 518 DMLLEGSDQtrGWFYRMIMLSTALTGSVPfKNVLVHGLV--RDEQGRKMSKSLGNVI 572
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 94-121 2.95e-03

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 40.14  E-value: 2.95e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 503441629  94 VHLGH---SVPMQILSRFQRM-GHDVVFIVGD 121
Cdd:PRK00133  17 IHLGHlveYIQADIWVRYQRMrGHEVLFVCAD 48
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 267-303 9.21e-03

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 37.91  E-value: 9.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 503441629 267 GTDGtGAKMSKSKGNYVPLTAAPGEIFGKIMSV---PDRL 303
Cdd:PRK12282 190 GLDG-KAKMSKSLGNAIYLSDDADTIKKKVMSMytdPNHI 228
 
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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