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Conserved domains on  [gi|563351212|gb|AHB40368|]
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hypothetical protein P147_WWE3C00001G0443 [candidate division WWE3 bacterium RAAC2_WWE3_1]

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 ...
 10-402 4.75e-147

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: 423.29  E-value: 4.75e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  10 LINTFLERGVDSIYPSkDALKKKLlSGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDP-D 88
Cdd:COG0162    3 LLLELIWRGLIEQITD-EELREKL-AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPsG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  89 KDTARPLMTEEQIQKNMAGWKEQAAQLIDFEGeNPVKFMRNHEWLSKIGLADLI-KLLSNATVQQMIERDLFAKRLKRNN 167
Cdd:COG0162   81 KSEERKLLTEEQVAENAETIKEQVFKFLDFDD-NKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 168 PIGLQEFIYPLMQGFDSVAM----GVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINL 243
Cdd:COG0162  160 GISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNAIWL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 244 SDKS---EVMYGKAMSYPDELITKCLRLLTDMPMEEIWEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFER 320
Cdd:COG0162  240 DEEKtspYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 321 TVQKKEISDE--DTEVVNISGIMPVQEFLKKAlKNSESASHIKRIVEQGGVEVNGKKVATTQIEIE-----FAPGTLVKF 393
Cdd:COG0162  320 LFGKGELPDDlpEVELSAAEGGIPLVDLLVEA-GLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTagdllHGGYLVLRV 398


                 ....*....
gi 563351212 394 GKRKYFKIE 402
Cdd:COG0162  399 GKKKFALVK 407
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 10-402 4.75e-147

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: 423.29  E-value: 4.75e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  10 LINTFLERGVDSIYPSkDALKKKLlSGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDP-D 88
Cdd:COG0162    3 LLLELIWRGLIEQITD-EELREKL-AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPsG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  89 KDTARPLMTEEQIQKNMAGWKEQAAQLIDFEGeNPVKFMRNHEWLSKIGLADLI-KLLSNATVQQMIERDLFAKRLKRNN 167
Cdd:COG0162   81 KSEERKLLTEEQVAENAETIKEQVFKFLDFDD-NKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 168 PIGLQEFIYPLMQGFDSVAM----GVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINL 243
Cdd:COG0162  160 GISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNAIWL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 244 SDKS---EVMYGKAMSYPDELITKCLRLLTDMPMEEIWEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFER 320
Cdd:COG0162  240 DEEKtspYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 321 TVQKKEISDE--DTEVVNISGIMPVQEFLKKAlKNSESASHIKRIVEQGGVEVNGKKVATTQIEIE-----FAPGTLVKF 393
Cdd:COG0162  320 LFGKGELPDDlpEVELSAAEGGIPLVDLLVEA-GLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTagdllHGGYLVLRV 398


                 ....*....
gi 563351212 394 GKRKYFKIE 402
Cdd:COG0162  399 GKKKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 26-401 2.75e-115

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 342.27  E-value: 2.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  26 KDALKKKLLSGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPD-KDTARPLMTEEQIQKN 104
Cdd:PRK13354  21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSgKSKERKLLTDEQVQHN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 105 MAGWKEQAAQLIDFEgenPVKFMRNHEWLSKIGLADLI-KLLSNATVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFD 183
Cdd:PRK13354 101 AKTYTEQIFKLFDFE---KTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 184 SVAM----GVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDK---SEVMYGKAMS 256
Cdd:PRK13354 178 FVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGAIWLDPEktsPYEFYQFWMN 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 257 YPDELITKCLRLLTDMPMEEIWEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQKKEISDEDTEVVN 336
Cdd:PRK13354 258 IDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFE 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 563351212 337 ISG-IMPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKVATTQIEIEFAP-----GTLVKFGKRKYFKI 401
Cdd:PRK13354 338 VSAeTKNLVDLLVDLGLEP-SKREARRLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLV 407
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 15-376 7.30e-86

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: 265.80  E-value: 7.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   15 LERGVDSIYPSKDALKKKLLsGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPD-KDTAR 93
Cdd:TIGR00234   9 TKRGLEVQTPEEEKDLLKLL-ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTgKSEVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   94 PLMTEEQIQKNMAGWKEQAAQLIDFEgenPVKFMRNHEWLSKIGLADLIKLLSNA-TVQQMIERDLFAKRLKRNnpIGLQ 172
Cdd:TIGR00234  88 KILTREEVQENAENIKKQIARFLDFE---KAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEEN--ISLH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  173 EFIYPLMQGFDSVAMGVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDKSEVMYG 252
Cdd:TIGR00234 163 EFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGAVSLDEGKYDFYQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  253 KAMSYPDELITKCLRLLTDMPMEEIWEINKKiqDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQKKEISDEDT 332
Cdd:TIGR00234 243 KVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDEVP 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 563351212  333 EVVNISGIMPVQ--EFLKKALKNSESASHIKRIvEQGGVEVNGKKV 376
Cdd:TIGR00234 321 IFRPEKFGGPITlaDLLVLSGLFPSKSEARRDI-KNGGVYINGEKV 365
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 39-303 1.50e-80

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: 248.68  E-value: 1.50e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  39 IKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDP-DKDTARPLMTEEQIQKNMAGWKEQAAQLID 117
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPsGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 118 FEGENPVKFMRNHEWLSKIGLADLIKLLSNATVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFDSVAMGVDLEIGGTD 197
Cdd:cd00805   81 FIPPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 198 QTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDKS--EVMYGKAMSYPDELITKCLRLLTDMPME 275
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIWDPVLDspYDVYQKIRNAFDPDVLEFLKLFTFLDYE 240

                        250       260
                 ....*....|....*....|....*...
gi 563351212 276 EIWEINKKIQDGENPMIFKKQMAHEVVK 303
Cdd:cd00805  241 EIEELEEEHAEGPLPRDAKKALAEELTK 268
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
34-323 2.14e-68

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 218.30  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   34 LSGERIKAYQGFDPSGPyLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPDKDTARPLMTEEQIQknMAGWKEQAA 113
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPERKLLSRETVL--ENAIKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  114 QLIDFEgenPVKFMRNHEWLSKIGLADLIKLLSNA-TVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFDSVAMGVDLE 192
Cdd:pfam00579  78 CGLDPE---KAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  193 IGGTDQTFNMLMGRELVKRYLGKDK---YVRTNEMMEAPD-ALTMSKTKGNG-INLSDKSE---VMYGKAMSYPDELITK 264
Cdd:pfam00579 155 PGGSDQWGNIELGRDLARRFNKKIFkkpVGLTNPLLTGLDgGKKMSKSAGNSaIFLDDDPEsvyKKIQKAYTDPDREVRK 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 563351212  265 CLRLLTDMPMEEIwEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQ 323
Cdd:pfam00579 235 DLKLFTFLSNEEI-EILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
341-399 2.90e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 35.65  E-value: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 563351212   341 MPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKVatTQIEIEFAPGTLVKFGKRKYF 399
Cdd:smart00363   1 RRLDKFLARLGLAP-SRSQARRLIEQGRVKVNGKKV--TKPSYIVKPGDVISVRGKELK 56
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 10-402 4.75e-147

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: 423.29  E-value: 4.75e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  10 LINTFLERGVDSIYPSkDALKKKLlSGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDP-D 88
Cdd:COG0162    3 LLLELIWRGLIEQITD-EELREKL-AGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPsG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  89 KDTARPLMTEEQIQKNMAGWKEQAAQLIDFEGeNPVKFMRNHEWLSKIGLADLI-KLLSNATVQQMIERDLFAKRLKRNN 167
Cdd:COG0162   81 KSEERKLLTEEQVAENAETIKEQVFKFLDFDD-NKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 168 PIGLQEFIYPLMQGFDSVAM----GVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINL 243
Cdd:COG0162  160 GISFTEFSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADGTKMGKSEGNAIWL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 244 SDKS---EVMYGKAMSYPDELITKCLRLLTDMPMEEIWEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFER 320
Cdd:COG0162  240 DEEKtspYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAFEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 321 TVQKKEISDE--DTEVVNISGIMPVQEFLKKAlKNSESASHIKRIVEQGGVEVNGKKVATTQIEIE-----FAPGTLVKF 393
Cdd:COG0162  320 LFGKGELPDDlpEVELSAAEGGIPLVDLLVEA-GLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTagdllHGGYLVLRV 398


                 ....*....
gi 563351212 394 GKRKYFKIE 402
Cdd:COG0162  399 GKKKFALVK 407
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 26-401 2.75e-115

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 342.27  E-value: 2.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  26 KDALKKKLLSGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPD-KDTARPLMTEEQIQKN 104
Cdd:PRK13354  21 EEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDPSgKSKERKLLTDEQVQHN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 105 MAGWKEQAAQLIDFEgenPVKFMRNHEWLSKIGLADLI-KLLSNATVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFD 183
Cdd:PRK13354 101 AKTYTEQIFKLFDFE---KTEIVNNSDWLSKLNLIDFLrDYGKHFTVNRMLERDDVKSRLEREQGISFTEFFYPLLQAYD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 184 SVAM----GVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDK---SEVMYGKAMS 256
Cdd:PRK13354 178 FVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGTKMGKSAGGAIWLDPEktsPYEFYQFWMN 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 257 YPDELITKCLRLLTDMPMEEIWEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQKKEISDEDTEVVN 336
Cdd:PRK13354 258 IDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIFKALFSGDVKPLKDIPTFE 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 563351212 337 ISG-IMPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKVATTQIEIEFAP-----GTLVKFGKRKYFKI 401
Cdd:PRK13354 338 VSAeTKNLVDLLVDLGLEP-SKREARRLIQNGAIKINGEKVTDVDAIINPEDafdgkFVILRRGKKKFFLV 407
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 15-376 7.30e-86

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: 265.80  E-value: 7.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   15 LERGVDSIYPSKDALKKKLLsGERIKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPD-KDTAR 93
Cdd:TIGR00234   9 TKRGLEVQTPEEEKDLLKLL-ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTgKSEVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   94 PLMTEEQIQKNMAGWKEQAAQLIDFEgenPVKFMRNHEWLSKIGLADLIKLLSNA-TVQQMIERDLFAKRLKRNnpIGLQ 172
Cdd:TIGR00234  88 KILTREEVQENAENIKKQIARFLDFE---KAKFVYNSEWLLKLNYTDFIRLLGKIfTVNRMLRRDAFSSRFEEN--ISLH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  173 EFIYPLMQGFDSVAMGVDLEIGGTDQTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDKSEVMYG 252
Cdd:TIGR00234 163 EFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADGEKMGKSLGGAVSLDEGKYDFYQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  253 KAMSYPDELITKCLRLLTDMPMEEIWEINKKiqDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQKKEISDEDT 332
Cdd:TIGR00234 243 KVINTPDELVKKYLKLFTFLGLEEIEQLVEL--KGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSGGLNPDEVP 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 563351212  333 EVVNISGIMPVQ--EFLKKALKNSESASHIKRIvEQGGVEVNGKKV 376
Cdd:TIGR00234 321 IFRPEKFGGPITlaDLLVLSGLFPSKSEARRDI-KNGGVYINGEKV 365
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 39-303 1.50e-80

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: 248.68  E-value: 1.50e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  39 IKAYQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDP-DKDTARPLMTEEQIQKNMAGWKEQAAQLID 117
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPsGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 118 FEGENPVKFMRNHEWLSKIGLADLIKLLSNATVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFDSVAMGVDLEIGGTD 197
Cdd:cd00805   81 FIPPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 198 QTFNMLMGRELVKRYLGKDKYVRTNEMMEAPDALTMSKTKGNGINLSDKS--EVMYGKAMSYPDELITKCLRLLTDMPME 275
Cdd:cd00805  161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMSKSEGNAIWDPVLDspYDVYQKIRNAFDPDVLEFLKLFTFLDYE 240

                        250       260
                 ....*....|....*....|....*...
gi 563351212 276 EIWEINKKIQDGENPMIFKKQMAHEVVK 303
Cdd:cd00805  241 EIEELEEEHAEGPLPRDAKKALAEELTK 268
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
34-323 2.14e-68

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 218.30  E-value: 2.14e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212   34 LSGERIKAYQGFDPSGPyLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPDKDTARPLMTEEQIQknMAGWKEQAA 113
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPSKSPERKLLSRETVL--ENAIKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  114 QLIDFEgenPVKFMRNHEWLSKIGLADLIKLLSNA-TVQQMIERDLFAKRLKRNNPIGLQEFIYPLMQGFDSVAMGVDLE 192
Cdd:pfam00579  78 CGLDPE---KAEIVNNSDWLEHLELAWLLRDLGKHfSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  193 IGGTDQTFNMLMGRELVKRYLGKDK---YVRTNEMMEAPD-ALTMSKTKGNG-INLSDKSE---VMYGKAMSYPDELITK 264
Cdd:pfam00579 155 PGGSDQWGNIELGRDLARRFNKKIFkkpVGLTNPLLTGLDgGKKMSKSAGNSaIFLDDDPEsvyKKIQKAYTDPDREVRK 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 563351212  265 CLRLLTDMPMEEIwEINKKIQDGENPMIFKKQMAHEVVKVIKGAEEAEKAQKHFERTVQ 323
Cdd:pfam00579 235 DLKLFTFLSNEEI-EILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 42-303 9.59e-39

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: 140.13  E-value: 9.59e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  42 YQGFDPSGPYLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGDPD-KDTARPLMTEEQIQKNMAGWKEQAAQLIDFEG 120
Cdd:cd00395    3 YCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSgKKSERTLNDPEEVRQNIRRIAAQYLAVGIFED 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 121 ENPVKFMRNHEWLSKIGLADLIKLLS-NATVQQMIERDLFAKRLKRNnpIGLQEFIYPLMQGFD----SVAMGVDLEIGG 195
Cdd:cd00395   83 PTQATLFNNSDWPGPLAHIQFLRDLGkHVYVNYMERKTSFQSRSEEG--ISATEFTYPPLQAADflllNTTEGCDIQPGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 196 TDQTFNMLMGRELVKR-YLGKDKYVRTNEMMEAPDALTMSKTKGNG---INLSDKSEVMYGKAMSYPDELITKCLRLLTD 271
Cdd:cd00395  161 SDQWGNITLGRELARRfNGFTIAEGLTIPLVTKLDGPKFGKSESGPkwlDTEKTSPYEFYQFWINAVDSDVINILKYFTF 240

                        250       260       270
                 ....*....|....*....|....*....|..
gi 563351212 272 MPMEEIWEINKKIQDGENPMIFKKQMAHEVVK 303
Cdd:cd00395  241 LSKEEIERLEQEQYEAPGYRVAQKTLAEEVTK 272
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 25-253 3.31e-12

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 66.81  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  25 SKDALKKKLLSGERIKAYQGFDPSGPyLHVGHAMGIRALRILQQLGHEAIFLVGDFTTLVGdpDKDTArplmteEQIQKN 104
Cdd:PRK08560  17 TEEELRELLESKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLN--DKGDL------EEIRKV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 105 MAGWKEQaaqlIDFEGENP--VKFMRNHEW-LSKIGLADLIKLLSNATVqqmierdlfaKRLKRNNPI--------GLQE 173
Cdd:PRK08560  88 AEYNKKV----FEALGLDPdkTEFVLGSEFqLDKEYWLLVLKLAKNTTL----------ARARRSMTImgrrmeepDVSK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 174 FIYPLMQGFDSVAMGVDLEIGGTDQ-TFNMLmGRELVKRyLGKDKYVrtneMMEAP-------DALTMSKTK-GNGINLS 244
Cdd:PRK08560 154 LVYPLMQVADIFYLDVDIAVGGMDQrKIHML-AREVLPK-LGYKKPV----CIHTPlltgldgGGIKMSKSKpGSAIFVH 227


                 ....*....
gi 563351212 245 DKSEVMYGK 253
Cdd:PRK08560 228 DSPEEIRRK 236
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 42-237 2.12e-06

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: 47.09  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  42 YQGFDPSGpYLHVGHAMGIRALRILQQL------GHEAIFLVGDFTTLVGDPDkdtarplmteeqiQKNMAGWKeqaaql 115
Cdd:cd00802    3 FSGITPNG-YLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPA-------------NKKGENAK------ 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 116 idfegenpvkfmrnhewlskigladlikllsnATVQQMIErdlfakRLKRnnpiglqEFIYPLMQGFDSVAMGV---DLE 192
Cdd:cd00802   63 --------------------------------AFVERWIE------RIKE-------DVEYMFLQAADFLLLYEtecDIH 97

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 563351212 193 IGGTDQTFNMLMGRELVKR-YLGKDKYVRTNEMMEAPDALTMSKTK 237
Cdd:cd00802   98 LGGSDQLGHIELGLELLKKaGGPARPFGLTFGRVMGADGTKMSKSK 143
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 30-259 5.52e-04

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 41.76  E-value: 5.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212  30 KKKLLSGERikayqgfdPSGPyLHVGHAMGIRALRILQQLGHEAIFLVGD---FTTLVGDPDKdtarplmteeqIQKNMA 106
Cdd:PRK12282   2 KPIILTGDR--------PTGK-LHLGHYVGSLKNRVALQNEHEQFVLIADqqaLTDNAKNPEK-----------IRRNIL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 107 gwkEQAAqliDF--EGENPVK---FMRnhewlSKI-GLADLIKLLSN----ATVQQM--IERDLFAKRLKRNNPIGLqeF 174
Cdd:PRK12282  62 ---EVAL---DYlaVGIDPAKstiFIQ-----SQIpELAELTMYYMNlvtvARLERNptVKTEIAQKGFGRSIPAGF--L 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 175 IYPLMQGFDSVAMGVDLEIGGTDQTFNMLMGRELVKRY---LGKDKYVRTNEMMeaPDAL---------TMSKTKGNGIN 242
Cdd:PRK12282 129 TYPVSQAADITAFKATLVPVGDDQLPMIEQTREIVRRFnslYGTDVLVEPEALL--PEAGrlpgldgkaKMSKSLGNAIY 206

                        250
                 ....*....|....*...
gi 563351212 243 LSDKSEVMYGKAMS-YPD 259
Cdd:PRK12282 207 LSDDADTIKKKVMSmYTD 224
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 341-394 1.15e-03

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 36.70  E-value: 1.15e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 563351212  341 MPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKVATtqieiefaPGTLVKFG 394
Cdd:pfam01479   1 RRLDKVLARLGLAS-SRSQARQLIEHGRVLVNGKVVKD--------PSYRVKPG 45
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 17-79 2.66e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 39.46  E-value: 2.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 563351212  17 RGVDSIypsKDALKKkllsGERIKAYQGFDPSGPyLHVGHAMGIRALRILQQLGHEAIFLVGD 79
Cdd:PRK12285  52 RDYDKI---LEAYRN----GKPFAVYTGFMPSGP-MHIGHKMVFDELKWHQEFGANVYIPIAD 106
S4 smart00363
S4 RNA-binding domain;
341-399 2.90e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 35.65  E-value: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 563351212   341 MPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKVatTQIEIEFAPGTLVKFGKRKYF 399
Cdd:smart00363   1 RRLDKFLARLGLAP-SRSQARRLIEQGRVKVNGKKV--TKPSYIVKPGDVISVRGKELK 56
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 341-401 6.97e-03

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 34.92  E-value: 6.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 563351212 341 MPVQEFLKKALKNSeSASHIKRIVEQGGVEVNGKKV--------ATTQIEI-EFAPGTLVKFGKRKYFKI 401
Cdd:cd00165    1 MRLDKILARLGLAP-SRSEARQLIKHGHVLVNGKVVtkpsykvkPGDVIEVdGKSIEEDIVYEDKKLLVV 69
 
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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