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Conserved domains on  [gi|488284236|ref|WP_002355444|]
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MULTISPECIES: tyrosine--tRNA ligase [Enterococcus]

Protein Classification

tyrosine--tRNA ligase( domain architecture ID 11486587)

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
EC:  6.1.1.1
Gene Ontology:  GO:0004831|GO:0006437
PubMed:  12458790|10447505
SCOP:  4003807

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-416 0e+00

tyrosyl-tRNA synthetase; Provisional


:

Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 662.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   1 MNIIDELAWRDAINQQTNEEGLRE-LTENTSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDP 79
Cdd:PRK13354   3 MNILEQLKWRGAINQETDEEKLRKsLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  80 SGRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDaEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRL--ES 157
Cdd:PRK13354  83 SGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE-KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLerEQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 158 GISFTEFTYQILQSIDFYTLHKKHNIQLQIGGADQWGNITAGLDLIRKKEGPEAkvFGLTIPLMLKADGTKFGKTAGGAI 237
Cdd:PRK13354 162 GISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQ--FGLTMPLLEGADGTKMGKSAGGAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 238 WLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKIS 317
Cdd:PRK13354 240 WLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 318 EALFSGNIKDLTieeieqgleHVPTVEITKDAKNIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPTQHF 397
Cdd:PRK13354 320 KALFSGDVKPLK---------DIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAF 390

                        410
                 ....*....|....*....
gi 488284236 398 DGKFVVVRKGKKNYFLAKV 416
Cdd:PRK13354 391 DGKFVILRRGKKKFFLVKL 409
 
Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-416 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 662.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   1 MNIIDELAWRDAINQQTNEEGLRE-LTENTSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDP 79
Cdd:PRK13354   3 MNILEQLKWRGAINQETDEEKLRKsLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  80 SGRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDaEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRL--ES 157
Cdd:PRK13354  83 SGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE-KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLerEQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 158 GISFTEFTYQILQSIDFYTLHKKHNIQLQIGGADQWGNITAGLDLIRKKEGPEAkvFGLTIPLMLKADGTKFGKTAGGAI 237
Cdd:PRK13354 162 GISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQ--FGLTMPLLEGADGTKMGKSAGGAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 238 WLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKIS 317
Cdd:PRK13354 240 WLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 318 EALFSGNIKDLTieeieqgleHVPTVEITKDAKNIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPTQHF 397
Cdd:PRK13354 320 KALFSGDVKPLK---------DIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAF 390

                        410
                 ....*....|....*....
gi 488284236 398 DGKFVVVRKGKKNYFLAKV 416
Cdd:PRK13354 391 DGKFVILRRGKKKFFLVKL 409
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 1-416 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: 583.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   1 MNIIDELAWRDAINQQTnEEGLRELTENTSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILigggtgtigDPS 80
Cdd:COG0162    1 MNLLLELIWRGLIEQIT-DEELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALiggftgmigDPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  81 GRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDAE-VTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLES-- 157
Cdd:COG0162   80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDDNkAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLESgq 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 158 GISFTEFTYQILQSIDFYTLHKKHNIQLQIGGADQWGNITAGLDLIRKKEGPEakVFGLTIPLMLKADGTKFGKTAGGAI 237
Cdd:COG0162  160 GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEP--QFGLTMPLLTGADGTKMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 238 WLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKIS 317
Cdd:COG0162  238 WLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 318 EALFS-GNIKDltieeieqgleHVPTVEITKDAK--NIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPT 394
Cdd:COG0162  318 EALFGkGELPD-----------DLPEVELSAAEGgiPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAG 386

                        410       420
                 ....*....|....*....|..
gi 488284236 395 QHFDGKFVVVRKGKKNYFLAKV 416
Cdd:COG0162  387 DLLHGGYLVLRVGKKKFALVKL 408
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 1-387 7.00e-121

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: 355.94  E-value: 7.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236    1 MNIIDELAWRDAINQQT-NEEGLRELTENtSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDP 79
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPeEEKDLLKLLER-PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   80 SGRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDaEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLESGI 159
Cdd:TIGR00234  81 TGKSEVRKILTREEVQENAENIKKQIARFLDFE-KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  160 SFTEFTYQILQSIDFYTLHKkhniQLQIGGADQWGNITAGLDLIRKKEgpEAKVFGLTIPLMLKADGTKFGKTAGGAIWL 239
Cdd:TIGR00234 160 SLHEFIYPLLQAYDFVYLNV----DLQLGGSDQWFNIRKGRDLARENL--PSLQFGLTVPLLTPADGEKMGKSLGGAVSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  240 DPkktSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEkvEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKISEA 319
Cdd:TIGR00234 234 DE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEA 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  320 LFSGNIK--DLTIEEIEQGLEHVptveitkdakNIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDL 387
Cdd:TIGR00234 309 IFSGGLNpdEVPIFRPEKFGGPI----------TLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 31-303 5.73e-110

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: 324.17  E-value: 5.73e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  31 ISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDPSGRTTERVLQTMEAVQHNVDSLSNQMKKL-- 108
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAIld 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 109 FGKDAEVTMVNNYDWLSELSLLDFLRdYGKNFNVNTMLAKDIVASRLES--GISFTEFTYQILQSIDFYTLHKkhniQLQ 186
Cdd:cd00805   81 FIPPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEeeGISFSEFIYPLLQAYDFVYLDV----DLQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 187 IGGADQWGNITAGLDLIRKKEGpeAKVFGLTIPLMLKADGTKFGKTAGGAIWlDPKKTSPFEFYQFWLNQDDRDVIKYLK 266
Cdd:cd00805  156 LGGSDQRGNITLGRDLIRKLGY--KKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488284236 267 FFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRF 303
Cdd:cd00805  233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
26-322 4.27e-80

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 248.73  E-value: 4.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   26 TENTSISLYCGVDPTGDsMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDPSgRTTERVLQTMEAVQHNvdSLSNQM 105
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  106 KKlfGKDAE-VTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLES--GISFTEFTYQILQSIDFYTLHKkhn 182
Cdd:pfam00579  77 AC--GLDPEkAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQgpGISLGEFTYPLLQAYDILLLKA--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  183 iQLQIGGADQWGNITAGLDLIRK-KEGPEAKVFGLTIPLMLKADGT-KFGKTAGG-AIWLDPKKTSPFEFYQFWLNQDDR 259
Cdd:pfam00579 152 -DLQPGGSDQWGNIELGRDLARRfNKKIFKKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTDPDR 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284236  260 DVIKYLKFFTFLDKEEIDALAEKVEKEPgKREAQRRLAEEVTRFVHDDAALEEAQKISEALFS 322
Cdd:pfam00579 231 EVRKDLKLFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
S4 smart00363
S4 RNA-binding domain;
363-415 1.02e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 37.19  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 488284236   363 PSKRQAREDVSGGAISINGDRVTDLDFAVDPTQhfdgkfVVVRKGKKNYFLAK 415
Cdd:smart00363  14 PSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGD------VISVRGKELKRLKK 60
 
Name Accession Description Interval E-value
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 1-416 0e+00

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 662.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   1 MNIIDELAWRDAINQQTNEEGLRE-LTENTSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDP 79
Cdd:PRK13354   3 MNILEQLKWRGAINQETDEEKLRKsLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQDAGHRPVILIGGFTGKIGDP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  80 SGRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDaEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRL--ES 157
Cdd:PRK13354  83 SGKSKERKLLTDEQVQHNAKTYTEQIFKLFDFE-KTEIVNNSDWLSKLNLIDFLRDYGKHFTVNRMLERDDVKSRLerEQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 158 GISFTEFTYQILQSIDFYTLHKKHNIQLQIGGADQWGNITAGLDLIRKKEGPEAkvFGLTIPLMLKADGTKFGKTAGGAI 237
Cdd:PRK13354 162 GISFTEFFYPLLQAYDFVHLNRKEDVDLQIGGTDQWGNILMGRDLQRKLEGEEQ--FGLTMPLLEGADGTKMGKSAGGAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 238 WLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKIS 317
Cdd:PRK13354 240 WLDPEKTSPYEFYQFWMNIDDRDVVKYLKLFTDLSPDEIDELEAQLETEPNPRDAKKVLAEEITKFVHGEEAAEEAEKIF 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 318 EALFSGNIKDLTieeieqgleHVPTVEITKDAKNIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPTQHF 397
Cdd:PRK13354 320 KALFSGDVKPLK---------DIPTFEVSAETKNLVDLLVDLGLEPSKREARRLIQNGAIKINGEKVTDVDAIINPEDAF 390

                        410
                 ....*....|....*....
gi 488284236 398 DGKFVVVRKGKKNYFLAKV 416
Cdd:PRK13354 391 DGKFVILRRGKKKFFLVKL 409
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 1-416 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: 583.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   1 MNIIDELAWRDAINQQTnEEGLRELTENTSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILigggtgtigDPS 80
Cdd:COG0162    1 MNLLLELIWRGLIEQIT-DEELREKLAGGPLTIYLGFDPTAPSLHLGHLVPLMKLRRFQDLGHRPIALiggftgmigDPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  81 GRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDAE-VTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLES-- 157
Cdd:COG0162   80 GKSEERKLLTEEQVAENAETIKEQVFKFLDFDDNkAEIVNNSDWLGKLSFIDFLRDLGKHFTVNRMLERDDVKKRLESgq 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 158 GISFTEFTYQILQSIDFYTLHKKHNIQLQIGGADQWGNITAGLDLIRKKEGPEakVFGLTIPLMLKADGTKFGKTAGGAI 237
Cdd:COG0162  160 GISFTEFSYPLLQGYDFVELYRRYGCDLQLGGSDQWGNILAGRELQRRYGGEP--QFGLTMPLLTGADGTKMGKSEGNAI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 238 WLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKIS 317
Cdd:COG0162  238 WLDEEKTSPYEFYQKWMNISDADVWRYLKLFTFLPLEEIEELEAEVAEGPNPREAKKRLAEEITALVHGEEAAEAAEEAF 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 318 EALFS-GNIKDltieeieqgleHVPTVEITKDAK--NIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPT 394
Cdd:COG0162  318 EALFGkGELPD-----------DLPEVELSAAEGgiPLVDLLVEAGLAASKSEARRLIKQGGVSVNGEKVTDPDAVLTAG 386

                        410       420
                 ....*....|....*....|..
gi 488284236 395 QHFDGKFVVVRKGKKNYFLAKV 416
Cdd:COG0162  387 DLLHGGYLVLRVGKKKFALVKL 408
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 1-387 7.00e-121

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: 355.94  E-value: 7.00e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236    1 MNIIDELAWRDAINQQT-NEEGLRELTENtSISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDP 79
Cdd:TIGR00234   2 NNILLLLTKRGLEVQTPeEEKDLLKLLER-PLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   80 SGRTTERVLQTMEAVQHNVDSLSNQMKKLFGKDaEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLESGI 159
Cdd:TIGR00234  81 TGKSEVRKILTREEVQENAENIKKQIARFLDFE-KAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  160 SFTEFTYQILQSIDFYTLHKkhniQLQIGGADQWGNITAGLDLIRKKEgpEAKVFGLTIPLMLKADGTKFGKTAGGAIWL 239
Cdd:TIGR00234 160 SLHEFIYPLLQAYDFVYLNV----DLQLGGSDQWFNIRKGRDLARENL--PSLQFGLTVPLLTPADGEKMGKSLGGAVSL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  240 DPkktSPFEFYQFWLNQDDRDVIKYLKFFTFLDKEEIDALAEkvEKEPGKREAQRRLAEEVTRFVHDDAALEEAQKISEA 319
Cdd:TIGR00234 234 DE---GKYDFYQKVINTPDELVKKYLKLFTFLGLEEIEQLVE--LKGPNPREVKENLALEITKYVHGPEAALAAEEISEA 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  320 LFSGNIK--DLTIEEIEQGLEHVptveitkdakNIVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDL 387
Cdd:TIGR00234 309 IFSGGLNpdEVPIFRPEKFGGPI----------TLADLLVLSGLFPSKSEARRDIKNGGVYINGEKVEDL 368
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 31-303 5.73e-110

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: 324.17  E-value: 5.73e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  31 ISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDPSGRTTERVLQTMEAVQHNVDSLSNQMKKL-- 108
Cdd:cd00805    1 LKVYIGFDPTAPSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSGKSEERKLLDLELIRENAKYYKKQLKAIld 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 109 FGKDAEVTMVNNYDWLSELSLLDFLRdYGKNFNVNTMLAKDIVASRLES--GISFTEFTYQILQSIDFYTLHKkhniQLQ 186
Cdd:cd00805   81 FIPPEKAKFVNNSDWLLSLYTLDFLR-LGKHFTVNRMLRRDAVKVRLEEeeGISFSEFIYPLLQAYDFVYLDV----DLQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 187 IGGADQWGNITAGLDLIRKKEGpeAKVFGLTIPLMLKADGTKFGKTAGGAIWlDPKKTSPFEFYQFWLNQDDRDVIKYLK 266
Cdd:cd00805  156 LGGSDQRGNITLGRDLIRKLGY--KKVVGLTTPLLTGLDGGKMSKSEGNAIW-DPVLDSPYDVYQKIRNAFDPDVLEFLK 232

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488284236 267 FFTFLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRF 303
Cdd:cd00805  233 LFTFLDYEEIEELEEEHAEGPLPRDAKKALAEELTKL 269
Tyr_Trp_RS_core cd00395
catalytic core domain of tyrosinyl-tRNA and tryptophanyl-tRNA synthetase; Tyrosinyl-tRNA ...
 32-303 7.29e-106

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: 313.86  E-value: 7.29e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  32 SLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDPSGRTTERVLQTMEAVQHNVDSLSNQMKKL--F 109
Cdd:cd00395    1 TLYCGIDPTADSLHIGHLIGLLTFRRFQHAGHRPIFLIGGQTGIIGDPSGKKSERTLNDPEEVRQNIRRIAAQYLAVgiF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 110 GKDAEVTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLESGISFTEFTYQILQSIDFYTLHKKHNIQLQIGG 189
Cdd:cd00395   81 EDPTQATLFNNSDWPGPLAHIQFLRDLGKHVYVNYMERKTSFQSRSEEGISATEFTYPPLQAADFLLLNTTEGCDIQPGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 190 ADQWGNITAGLDLIRKKEGpEAKVFGLTIPLMLKADGTKFGKTAGGAIWLDPKKTSPFEFYQFWLNQDDRDVIKYLKFFT 269
Cdd:cd00395  161 SDQWGNITLGRELARRFNG-FTIAEGLTIPLVTKLDGPKFGKSESGPKWLDTEKTSPYEFYQFWINAVDSDVINILKYFT 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 488284236 270 FLDKEEIDALAEKVEKEPGKREAQRRLAEEVTRF 303
Cdd:cd00395  240 FLSKEEIERLEQEQYEAPGYRVAQKTLAEEVTKT 273
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
26-322 4.27e-80

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 248.73  E-value: 4.27e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236   26 TENTSISLYCGVDPTGDsMHIGHLIPFMMMKRFQLAGHHPYILIGGGTGTIGDPSgRTTERVLQTMEAVQHNvdSLSNQM 105
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGP-LHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIGDPS-KSPERKLLSRETVLEN--AIKAQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  106 KKlfGKDAE-VTMVNNYDWLSELSLLDFLRDYGKNFNVNTMLAKDIVASRLES--GISFTEFTYQILQSIDFYTLHKkhn 182
Cdd:pfam00579  77 AC--GLDPEkAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFKDVKKRLEQgpGISLGEFTYPLLQAYDILLLKA--- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  183 iQLQIGGADQWGNITAGLDLIRK-KEGPEAKVFGLTIPLMLKADGT-KFGKTAGG-AIWLDPKKTSPFEFYQFWLNQDDR 259
Cdd:pfam00579 152 -DLQPGGSDQWGNIELGRDLARRfNKKIFKKPVGLTNPLLTGLDGGkKMSKSAGNsAIFLDDDPESVYKKIQKAYTDPDR 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284236  260 DVIKYLKFFTFLDKEEIDALAEKVEKEPgKREAQRRLAEEVTRFVHDDAALEEAQKISEALFS 322
Cdd:pfam00579 231 EVRKDLKLFTFLSNEEIEILEAELGKSP-YREAEELLAREVTGLVHGGDLKKAAAEAVNKLLQ 292
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
 33-232 4.44e-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: 45.93  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236  33 LYCGVDPTGdSMHIGHLIPFMMMKRFQLA------GHHPYILIGGGTGTIGDPSGRTTervlqtmEAVQHNVDSLSNQMK 106
Cdd:cd00802    2 TFSGITPNG-YLHIGHLRTIVTFDFLAQAyrklgyKVRCIALIDDAGGLIGDPANKKG-------ENAKAFVERWIERIK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284236 107 KLfgkdaevtmvnnYDWLSeLSLLDFLRDYGKNFNvntmlakdivasrlesgisfteftyqilqsidfytlhkkhniqLQ 186
Cdd:cd00802   74 ED------------VEYMF-LQAADFLLLYETECD-------------------------------------------IH 97

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 488284236 187 IGGADQWGNITAGLDLIRKKEGPEAKvFGLTIPLMLKADGTKFGKT 232
Cdd:cd00802   98 LGGSDQLGHIELGLELLKKAGGPARP-FGLTFGRVMGADGTKMSKS 142
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 352-416 5.51e-06

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: 43.78  E-value: 5.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284236 352 IVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDPTQH--FDGKFVVVRKGKKNYFLAKV 416
Cdd:cd00165    3 LDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVieVDGKSIEEDIVYEDKKLLVV 69
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 352-393 5.79e-05

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: 40.17  E-value: 5.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 488284236  352 IVDWLVDTEIEPSKRQAREDVSGGAISINGDRVTDLDFAVDP 393
Cdd:pfam01479   3 LDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVKP 44
PLN02486 PLN02486
aminoacyl-tRNA ligase
 33-61 4.70e-04

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 42.04  E-value: 4.70e-04
                         10        20
                 ....*....|....*....|....*....
gi 488284236  33 LYCGVDPTGDSMHIGHLIPFMMMKRFQLA 61
Cdd:PLN02486  76 LYTGRGPSSEALHLGHLIPFMFTKYLQDA 104
S4 smart00363
S4 RNA-binding domain;
363-415 1.02e-03

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 37.19  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 488284236   363 PSKRQAREDVSGGAISINGDRVTDLDFAVDPTQhfdgkfVVVRKGKKNYFLAK 415
Cdd:smart00363  14 PSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGD------VISVRGKELKRLKK 60
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 22-68 5.46e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 38.69  E-value: 5.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488284236  22 LRELTENTSISLYCGVDPTGDsMHIGHLIPFMMMKRFQLAGHHPYIL 68
Cdd:PRK12285  58 LEAYRNGKPFAVYTGFMPSGP-MHIGHKMVFDELKWHQEFGANVYIP 103
 
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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