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Conserved domains on  [gi|2541364647|ref|WP_297471305|]
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tyrosine--tRNA ligase [Acidithiobacillus sp.]

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 ...
 15-404 0e+00

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: 540.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  15 GTVDMLPEGEMLARLAaaqrdNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTR 94
Cdd:COG0162    11 GLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  95 KALSREEVVANAATYRRQVFKILDP--ERTEVMFNSEWLGALRPEELI-QIAARYTVARMLERDDFNKRYSANQPIAIHE 171
Cdd:COG0162    86 KLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FLYPLLQGYDSVAI----KADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGNFIAVED--- 244
Cdd:COG0162   166 FSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEekt 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 245 PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEAASGArNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQR 324
Cdd:COG0162   245 SPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGK 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 325 HETPEDLPLQAIKLSEAP-RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILAL-----DAVYLLQFGKRHF 398
Cdd:COG0162   324 GELPDDLPEVELSAAEGGiPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAgdllhGGYLVLRVGKKKF 403


                  ....*.
gi 2541364647 399 ARVALQ 404
Cdd:COG0162   404 ALVKLK 409
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 15-404 0e+00

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: 540.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  15 GTVDMLPEGEMLARLAaaqrdNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTR 94
Cdd:COG0162    11 GLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  95 KALSREEVVANAATYRRQVFKILDP--ERTEVMFNSEWLGALRPEELI-QIAARYTVARMLERDDFNKRYSANQPIAIHE 171
Cdd:COG0162    86 KLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FLYPLLQGYDSVAI----KADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGNFIAVED--- 244
Cdd:COG0162   166 FSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEekt 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 245 PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEAASGArNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQR 324
Cdd:COG0162   245 SPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGK 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 325 HETPEDLPLQAIKLSEAP-RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILAL-----DAVYLLQFGKRHF 398
Cdd:COG0162   324 GELPDDLPEVELSAAEGGiPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAgdllhGGYLVLRVGKKKF 403


                  ....*.
gi 2541364647 399 ARVALQ 404
Cdd:COG0162   404 ALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 6-401 1.63e-146

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 422.00  E-value: 1.63e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647   6 QDAFEQIALgtVDMLPEGEMLARLAAAQRDNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIG 85
Cdd:PRK13354    3 MNILEQLKW--RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  86 DPTGKSVTRKALSREEVVANAATYRRQVFKILDPERTEVMFNSEWLGALRPEELIQ-IAARYTVARMLERDDFNKRYSAN 164
Cdd:PRK13354   81 DPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLRdYGKHFTVNRMLERDDVKSRLERE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 165 QPIAIHEFLYPLLQGYDSVAI----KADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGVqKMSKSLGNFI 240
Cdd:PRK13354  161 QGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 241 AVED---PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEAASGArNPRDIKLDLAAELVRRFHGTAAAQEAHIA 317
Cdd:PRK13354  240 WLDPektSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEEAEKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 318 FLARFQRHETPE-DLPlqAIKLSEAPR-LSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILA-----LDAVYL 390
Cdd:PRK13354  319 FKALFSGDVKPLkDIP--TFEVSAETKnLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINpedafDGKFVI 396

                         410
                  ....*....|.
gi 2541364647 391 LQFGKRHFARV 401
Cdd:PRK13354  397 LRRGKKKFFLV 407
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 7-384 9.15e-124

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: 362.87  E-value: 9.15e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647   7 DAFEQI-ALGTVDMLPEGEMLARlaaaQRDNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIG 85
Cdd:TIGR00234   3 NILLLLtKRGLEVQTPEEEKDLL----KLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  86 DPTGKSVTRKALSREEVVANAATYRRQVFKILDPERTEVMFNSEWLGALRPEELIQIAAR-YTVARMLERDDFNKRYSAN 164
Cdd:TIGR00234  79 DPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFEEN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 165 qpIAIHEFLYPLLQGYDSVAIKADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGNFIAVED 244
Cdd:TIGR00234 159 --ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 245 PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEaasGARNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQR 324
Cdd:TIGR00234 236 GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL---KGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541364647 325 HETPEDLPLQAI-KLSEAPRLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILA 384
Cdd:TIGR00234 313 GLNPDEVPIFRPeKFGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRK 373
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 39-304 2.82e-102

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: 304.14  E-value: 2.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  39 LRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTRKALSREEVVANAATYRRQVFKILD 118
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 119 ---PERTEVMFNSEWLGALRPEELIQIAARYTVARMLERDDFNKRYSANQPIAIHEFLYPLLQGYDSVAIKADVELGGTD 195
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 196 QRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGN--FIAVEDPPAEMFGKIMSISDFLMWRYYALLSRVPA 273
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNaiWDPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2541364647 274 VEQARLQKEAASGaRNPRDIKLDLAAELVRR 304
Cdd:cd00805   240 EEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
35-323 9.90e-102

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 303.81  E-value: 9.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  35 DNSPLRIKLGMDPTAPdLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTgKSVTRKALSREEVVANAatYRRQVF 114
Cdd:pfam00579   2 KNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 115 KILDPERTEVMFNSEWLGALRPEELIQIAAR-YTVARMLERDDFNKRYSANQPIAIHEFLYPLLQGYDSVAIKADVELGG 193
Cdd:pfam00579  78 CGLDPEKAEIVNNSDWLEHLELAWLLRDLGKhFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 194 TDQRFNLLVGRELQREYGQK---PQLVLTMPILEGLDGVQKMSKSLGN----FIAVEDPPAEMFGKIMSISDFLMWRYYA 266
Cdd:pfam00579 158 SDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2541364647 267 LLSRVPAVEQARLQKEaaSGARNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQ 323
Cdd:pfam00579 238 LFTFLSNEEIEILEAE--LGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
343-400 2.82e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 44.12  E-value: 2.82e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2541364647  343 RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILALDAVYLLQFGKRHFAR 400
Cdd:smart00363   2 RLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLK 59
 
Name Accession Description Interval E-value
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 15-404 0e+00

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: 540.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  15 GTVDMLPEGEMLARLAaaqrdNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTR 94
Cdd:COG0162    11 GLIEQITDEELREKLA-----GGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALIGGFTGMIGDPSGKSEER 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  95 KALSREEVVANAATYRRQVFKILDP--ERTEVMFNSEWLGALRPEELI-QIAARYTVARMLERDDFNKRYSANQPIAIHE 171
Cdd:COG0162    86 KLLTEEQVAENAETIKEQVFKFLDFddNKAEIVNNSDWLGKLSFIDFLrDLGKHFTVNRMLERDDVKKRLESGQGISFTE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FLYPLLQGYDSVAI----KADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGNFIAVED--- 244
Cdd:COG0162   166 FSYPLLQGYDFVELyrryGCDLQLGGSDQWGNILAGRELQRRYGGEPQFGLTMPLLTGADG-TKMGKSEGNAIWLDEekt 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 245 PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEAASGArNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQR 324
Cdd:COG0162   245 SPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGP-NPREAKKRLAEEITALVHGEEAAEAAEEAFEALFGK 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 325 HETPEDLPLQAIKLSEAP-RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILAL-----DAVYLLQFGKRHF 398
Cdd:COG0162   324 GELPDDLPEVELSAAEGGiPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAgdllhGGYLVLRVGKKKF 403


                  ....*.
gi 2541364647 399 ARVALQ 404
Cdd:COG0162   404 ALVKLK 409
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 6-401 1.63e-146

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 422.00  E-value: 1.63e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647   6 QDAFEQIALgtVDMLPEGEMLARLAAAQRDNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIG 85
Cdd:PRK13354    3 MNILEQLKW--RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  86 DPTGKSVTRKALSREEVVANAATYRRQVFKILDPERTEVMFNSEWLGALRPEELIQ-IAARYTVARMLERDDFNKRYSAN 164
Cdd:PRK13354   81 DPSGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFEKTEIVNNSDWLSKLNLIDFLRdYGKHFTVNRMLERDDVKSRLERE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 165 QPIAIHEFLYPLLQGYDSVAI----KADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGVqKMSKSLGNFI 240
Cdd:PRK13354  161 QGISFTEFFYPLLQAYDFVHLnrkeDVDLQIGGTDQWGNILMGRDLQRKLEGEEQFGLTMPLLEGADGT-KMGKSAGGAI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 241 AVED---PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEAASGArNPRDIKLDLAAELVRRFHGTAAAQEAHIA 317
Cdd:PRK13354  240 WLDPektSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEP-NPRDAKKVLAEEITKFVHGEEAAEEAEKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 318 FLARFQRHETPE-DLPlqAIKLSEAPR-LSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILA-----LDAVYL 390
Cdd:PRK13354  319 FKALFSGDVKPLkDIP--TFEVSAETKnLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINpedafDGKFVI 396

                         410
                  ....*....|.
gi 2541364647 391 LQFGKRHFARV 401
Cdd:PRK13354  397 LRRGKKKFFLV 407
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 7-384 9.15e-124

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: 362.87  E-value: 9.15e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647   7 DAFEQI-ALGTVDMLPEGEMLARlaaaQRDNSPLRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIG 85
Cdd:TIGR00234   3 NILLLLtKRGLEVQTPEEEKDLL----KLLERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  86 DPTGKSVTRKALSREEVVANAATYRRQVFKILDPERTEVMFNSEWLGALRPEELIQIAAR-YTVARMLERDDFNKRYSAN 164
Cdd:TIGR00234  79 DPTGKSEVRKILTREEVQENAENIKKQIARFLDFEKAKFVYNSEWLLKLNYTDFIRLLGKiFTVNRMLRRDAFSSRFEEN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 165 qpIAIHEFLYPLLQGYDSVAIKADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGNFIAVED 244
Cdd:TIGR00234 159 --ISLHEFIYPLLQAYDFVYLNVDLQLGGSDQWFNIRKGRDLARENLPSLQFGLTVPLLTPADG-EKMGKSLGGAVSLDE 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 245 PPAEMFGKIMSISDFLMWRYYALLSRVPAVEQARLQKEaasGARNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQR 324
Cdd:TIGR00234 236 GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVEL---KGPNPREVKENLALEITKYVHGPEAALAAEEISEAIFSG 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541364647 325 HETPEDLPLQAI-KLSEAPRLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILA 384
Cdd:TIGR00234 313 GLNPDEVPIFRPeKFGGPITLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDLEPIRK 373
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 39-304 2.82e-102

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: 304.14  E-value: 2.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  39 LRIKLGMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTRKALSREEVVANAATYRRQVFKILD 118
Cdd:cd00805     1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 119 ---PERTEVMFNSEWLGALRPEELIQIAARYTVARMLERDDFNKRYSANQPIAIHEFLYPLLQGYDSVAIKADVELGGTD 195
Cdd:cd00805    81 fipPEKAKFVNNSDWLLSLYTLDFLRLGKHFTVNRMLRRDAVKVRLEEEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 196 QRFNLLVGRELQREYGQKPQLVLTMPILEGLDGvQKMSKSLGN--FIAVEDPPAEMFGKIMSISDFLMWRYYALLSRVPA 273
Cdd:cd00805   161 QRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDG-GKMSKSEGNaiWDPVLDSPYDVYQKIRNAFDPDVLEFLKLFTFLDY 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2541364647 274 VEQARLQKEAASGaRNPRDIKLDLAAELVRR 304
Cdd:cd00805   240 EEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
35-323 9.90e-102

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 303.81  E-value: 9.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  35 DNSPLRIKLGMDPTAPdLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTgKSVTRKALSREEVVANAatYRRQVF 114
Cdd:pfam00579   2 KNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLENA--IKAQLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 115 KILDPERTEVMFNSEWLGALRPEELIQIAAR-YTVARMLERDDFNKRYSANQPIAIHEFLYPLLQGYDSVAIKADVELGG 193
Cdd:pfam00579  78 CGLDPEKAEIVNNSDWLEHLELAWLLRDLGKhFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAYDILLLKADLQPGG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 194 TDQRFNLLVGRELQREYGQK---PQLVLTMPILEGLDGVQKMSKSLGN----FIAVEDPPAEMFGKIMSISDFLMWRYYA 266
Cdd:pfam00579 158 SDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGGKKMSKSAGNsaifLDDDPESVYKKIQKAYTDPDREVRKDLK 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2541364647 267 LLSRVPAVEQARLQKEaaSGARNPRDIKLDLAAELVRRFHGTAAAQEAHIAFLARFQ 323
Cdd:pfam00579 238 LFTFLSNEEIEILEAE--LGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 44-303 4.79e-34

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: 127.80  E-value: 4.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  44 GMDPTAPDLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGDPTGKSVTRKALSREEVVANAATYRRQVFKIL---DPE 120
Cdd:cd00395     5 GIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVGifeDPT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 121 RTEVMFNSEWLGalrPEELIQIAARY----TVARMLERDDFNKRysANQPIAIHEFLYPLLQGYD----SVAIKADVELG 192
Cdd:cd00395    85 QATLFNNSDWPG---PLAHIQFLRDLgkhvYVNYMERKTSFQSR--SEEGISATEFTYPPLQAADflllNTTEGCDIQPG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 193 GTDQRFNLLVGREL-QREYGQKPQLVLTMPILEGLDGvQKMSKSLGN---FIAVEDPPAEMFGKIMSISDFLMWRYYALL 268
Cdd:cd00395   160 GSDQWGNITLGRELaRRFNGFTIAEGLTIPLVTKLDG-PKFGKSESGpkwLDTEKTSPYEFYQFWINAVDSDVINILKYF 238

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2541364647 269 SRVPAVEQARLQKEAASGaRNPRDIKLDLAAELVR 303
Cdd:cd00395   239 TFLSKEEIERLEQEQYEA-PGYRVAQKTLAEEVTK 272
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 7-254 1.09e-21

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 94.93  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647   7 DAFEQIALGTVDMLPEGEMLARLAaaqrDNSPLRIKLGMDPTAPdLHLGHTVLLHKARQFQDLGHRLLFVIGDFTAMIGD 86
Cdd:PRK08560    3 ERLELITRNTEEVVTEEELRELLE----SKEEPKAYIGFEPSGK-IHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  87 ptgKSVTrkalsreEVVANAATYRRQVFKI--LDPERTEVMFNSEWlgALRPE---ELIQIAARYTVARMLERDDFNKRY 161
Cdd:PRK08560   78 ---KGDL-------EEIRKVAEYNKKVFEAlgLDPDKTEFVLGSEF--QLDKEywlLVLKLAKNTTLARARRSMTIMGRR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 162 SANQPIAihEFLYPLLQGYDSVAIKADVELGGTDQRFNLLVGRELQREYGQKPQLVLTMPILEGLDGVQ-KMSKS-LGNF 239
Cdd:PRK08560  146 MEEPDVS--KLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGiKMSKSkPGSA 223

                         250
                  ....*....|....*
gi 2541364647 240 IAVEDPPAEMFGKIM 254
Cdd:PRK08560  224 IFVHDSPEEIRRKIK 238
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 44-303 2.33e-12

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: 66.84  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  44 GMDPTAPdLHLGHTV-LLHKARQFQDLGHRLLFVIGD---FTAMIGDPTgksvTRKALSREevvaNAATYrrqvfkI--- 116
Cdd:cd00806     5 GIQPSGS-LHLGHYLgAFRFWVWLQEAGYELFFFIADlhaLTVKQLDPE----ELRQNTRE----NAKDY------Lacg 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 117 LDPERTEVMFNSEwlgalRPE--ELIQIAARYTVARMLER-----DDFNKRYSANqpiaIHEFLYPLLQGYDSVAIKADV 189
Cdd:cd00806    70 LDPEKSTIFFQSD-----VPEhyELAWLLSCVVTFGELERmtgfkDKSAQGESVN----IGLLTYPVLQAADILLYKACL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 190 ELGGTDQRFNLlvgrELQRE--------YGQ---KPQLVLTMP--ILEGLDGVQKMSKSLG-NFIAVEDPPAEMFGKIMS 255
Cdd:cd00806   141 VPVGIDQDPHL----ELTRDiarrfnklYGEifpKPAALLSKGafLPGLQGPSKKMSKSDPnNAIFLTDSPKEIKKKIMK 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541364647 256 I-SDFL---------------MWRYYALLSRVPAVEQARLQkEAASGARNPRDIKLDLAAELVR 303
Cdd:cd00806   217 AaTDGGrtehrrdgggpgvsnLVEIYSAFFNDDDEELEEID-EYRSGGLGYGECKKLLAEAIQE 279
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 40-255 2.98e-11

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 64.11  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  40 RIKLGMDPTAPdLHLGHTVLLHKAR-QFQDlGHRLLFVIGDFTAMigdptgksvTRKALSREEVvanaatyRRQVFKI-- 116
Cdd:PRK12282    4 IILTGDRPTGK-LHLGHYVGSLKNRvALQN-EHEQFVLIADQQAL---------TDNAKNPEKI-------RRNILEVal 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 117 ------LDPERTEVMFNSEWlgalrpEELIQIAARY----TVARmLERddfNKRYSANqpIAIHEF---------LYPLL 177
Cdd:PRK12282   66 dylavgIDPAKSTIFIQSQI------PELAELTMYYmnlvTVAR-LER---NPTVKTE--IAQKGFgrsipagflTYPVS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 178 QGYDSVAIKADVELGGTDQ------------RFNLLVGRELQREygqkPQLVLT-MPILEGLDGVQKMSKSLGNFIAVED 244
Cdd:PRK12282  134 QAADITAFKATLVPVGDDQlpmieqtreivrRFNSLYGTDVLVE----PEALLPeAGRLPGLDGKAKMSKSLGNAIYLSD 209

                         250
                  ....*....|.
gi 2541364647 245 PPAEMFGKIMS 255
Cdd:PRK12282  210 DADTIKKKVMS 220
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 44-256 2.12e-08

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: 55.44  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647  44 GMDPTAPdLHLGHTV-LLHKARQFQDlGHRLLFVIGDFTAMIGDPTGKSVtrkalsREEVVANAATYrrqvfkI---LDP 119
Cdd:COG0180     9 GIQPTGR-LHLGNYLgALKNWVELQD-EYECFFFIADLHALTTPQDPEEL------RENTREVAADY------LaagLDP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 120 ERTeVMFN-SEwlgalRPE--ELIQIAAryTVARM--LER-----DDFNKRYSANQPIAIheFLYPLLQGYDSVAIKADV 189
Cdd:COG0180    75 EKS-TIFVqSD-----VPEhaELAWLLS--CLTPLgeLERmpqfkDKSAKNGKENVNAGL--LTYPVLMAADILLYKADL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 190 ELGGTDQ------------RFNLLVGrelqrEYGQKPQLVLT--MPILEGLDGVQKMSKSLGNFIAVEDPPAEMFGKIMS 255
Cdd:COG0180   145 VPVGEDQkqhleltrdiarRFNHRYG-----EVFPEPEALIPeeGARIPGLDGRKKMSKSYGNTINLLDDPKEIRKKIKS 219


                  .
gi 2541364647 256 I 256
Cdd:COG0180   220 A 220
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 140-255 7.54e-08

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 53.93  E-value: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 140 IQIAARYTVARMlerddfnKRYSA--------NQPIAihEFLYPLLQGYDSVAIKADVELGGTDQR-FNLLVgrelqREY 210
Cdd:PTZ00126  165 MDIARSFNITRI-------KRCSQimgrsegdEQPCA--QILYPCMQCADIFYLKADICQLGMDQRkVNMLA-----REY 230

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2541364647 211 GQKPQ-----LVLTMPILEGL-DGVQKMSKSLGN-FIAVEDPPAEMFGKIMS 255
Cdd:PTZ00126  231 CDKKKikkkpIILSHHMLPGLlEGQEKMSKSDPNsAIFMEDSEEDVNRKIKK 282
S4 smart00363
S4 RNA-binding domain;
343-400 2.82e-06

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 44.12  E-value: 2.82e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2541364647  343 RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILALDAVYLLQFGKRHFAR 400
Cdd:smart00363   2 RLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISVRGKELKRLK 59
PRK12283 PRK12283
tryptophanyl-tRNA synthetase; Reviewed
 172-253 8.17e-06

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 183401 [Multi-domain]  Cd Length: 398  Bit Score: 47.64  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FL-YPLLQGYDSVAIKADVELGGTDQ------------RFNLLVGRE------------------------LQREYGQK- 213
Cdd:PRK12283  127 FLgYPLLQSADILIYRAGLVPVGEDQvphvemtreiarRFNHLYGREpgfeekaeaaikklgkkraklyheLRNAYQEEg 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 214 ----------------------------------------PQLVLT----MPileGLDGvQKMSKSLGNFIAVEDPPAEM 249
Cdd:PRK12283  207 ddealeqarallqeqqnlsmgdrerlfgylegagkiilpePQALLTeaskMP---GLDG-QKMSKSYGNTIGLREDPESV 282


                  ....
gi 2541364647 250 FGKI 253
Cdd:PRK12283  283 TKKI 286
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 343-401 1.48e-05

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: 42.62  E-value: 1.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541364647 343 RLSQLLVQVHLAASTSEAMRKMKEGAVRVDGERVVDTATILALDAV---------YLLQFGKRHFARV 401
Cdd:cd00165     2 RLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVievdgksieEDIVYEDKKLLVV 69
PRK12284 PRK12284
tryptophanyl-tRNA synthetase; Reviewed
 172-256 1.37e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237036 [Multi-domain]  Cd Length: 431  Bit Score: 43.84  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FLYPLLQGYDSVAIKADVELGGTDQ------------RFNLLVGRELqreygqkpqlvLTMP---------ILEGLDGvQ 230
Cdd:PRK12284  134 FMYPVLMAADILMFNAHKVPVGRDQiqhiemardiaqRFNHLYGGEF-----------FVLPeavieesvaTLPGLDG-R 201

                          90       100
                  ....*....|....*....|....*.
gi 2541364647 231 KMSKSLGNFIAVEDPPAEMFGKIMSI 256
Cdd:PRK12284  202 KMSKSYDNTIPLFAPREELKKAIFSI 227
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 172-256 5.29e-04

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 41.61  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 172 FLYPLLQGYDSVAIKAD---VelgGTDQRFNLlvgrELQRE--------YGQkpqlVLTMP---ILE------GLDG-VQ 230
Cdd:PRK00927  124 FTYPVLMAADILLYKADlvpV---GEDQKQHL----ELTRDiarrfnnlYGE----VFPVPeplIPKvgarvmGLDGpTK 192

                          90       100
                  ....*....|....*....|....*....
gi 2541364647 231 KMSKSLG---NFIAVEDPPAEMFGKIMSI 256
Cdd:PRK00927  193 KMSKSDPndnNTINLLDDPKTIAKKIKKA 221
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 171-250 6.43e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 38.73  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541364647 171 EFLYPLLQGYDSVAIKADVELGGTDQRFNLLVGRELQREYGQKPQ-LVLTMPILEGL-DGVQKMSKSlgnfiaveDPPAE 248
Cdd:PTZ00348  160 QVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKLKpVILSHHMLAGLkQGQAKMSKS--------DPDSA 231


                  ..
gi 2541364647 249 MF 250
Cdd:PTZ00348  232 IF 233
 
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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