位置:首页 > 蛋白库 > SYYC_DANRE
SYYC_DANRE
ID   SYYC_DANRE              Reviewed;         529 AA.
AC   Q6TGS6; Q6DFZ7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Tyrosine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.1;
DE   AltName: Full=Tyrosyl-tRNA synthetase;
DE            Short=TyrRS;
GN   Name=yars1; Synonyms=yars;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC       step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC       then transferred to the acceptor end of tRNA(Tyr). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC         tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC         Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY398430; AAQ97863.1; -; mRNA.
DR   EMBL; BX547927; CAK04282.1; -; Genomic_DNA.
DR   EMBL; BX000986; CAK04465.1; -; Genomic_DNA.
DR   EMBL; BC076558; AAH76558.1; -; mRNA.
DR   RefSeq; NP_958473.1; NM_201316.1.
DR   RefSeq; XP_005159655.1; XM_005159598.3.
DR   AlphaFoldDB; Q6TGS6; -.
DR   SMR; Q6TGS6; -.
DR   STRING; 7955.ENSDARP00000108800; -.
DR   PaxDb; Q6TGS6; -.
DR   PRIDE; Q6TGS6; -.
DR   GeneID; 368235; -.
DR   KEGG; dre:368235; -.
DR   CTD; 8565; -.
DR   ZFIN; ZDB-GENE-030425-2; yars1.
DR   eggNOG; KOG2144; Eukaryota.
DR   eggNOG; KOG2241; Eukaryota.
DR   InParanoid; Q6TGS6; -.
DR   OrthoDB; 852081at2759; -.
DR   PhylomeDB; Q6TGS6; -.
DR   TreeFam; TF300898; -.
DR   PRO; PR:Q6TGS6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:ZFIN.
DR   GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00805; TyrRS_core; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002305; aa-tRNA-synth_Ic.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR002307; Tyr-tRNA-ligase.
DR   Pfam; PF00579; tRNA-synt_1b; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01040; TRNASYNTHTYR.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00234; tyrS; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..529
FT                   /note="Tyrosine--tRNA ligase, cytoplasmic"
FT                   /id="PRO_0000239693"
FT   DOMAIN          365..469
FT                   /note="tRNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00209"
FT   REGION          335..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           44..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000250"
FT   MOTIF           222..226
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="L-tyrosine"
FT                   /ligand_id="ChEBI:CHEBI:58315"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        351
FT                   /note="V -> A (in Ref. 1; AAQ97863/CAK04282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   529 AA;  59534 MW;  A3264E3E39D362F4 CRC64;
     MGEQLSPDEK FQLITRNLQE VLGEERLKEI LKERELKVYW GTATTGKPHV AYFVPMSKIA
     DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVKYYEQV IKAMLESIGV PLDKLKFVKG
     TDYQLSREYT LDVYRLSSMV TEHDAKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD
     AQFGGVDQRK IFTLAEKYLP SLGYTKRSHL MNPMVPGLTG SKMSSSEEES KIDLLDKNQD
     VKKKLKKAFC EPGNVENNGV LSFVKHVLFP LHSEFVIKRD PKFGGDKVYT DFEEVEKDFA
     AEQIHPGDLK ASVELALNKL LDPIRKKFES PELKKLTSSA YPEPSKNKGG VKGNPKQTTD
     DDEVIPSRLD IRVGKVISVE KHPDADSLYL EKIDVGEEQP RTVVSGLVAY ITEEQLQDRL
     VVLLCNLKPQ KMRGIESQAM VLCASIEGEP RKVEPLDPPE GSAAGDRVYV EGYESGKPDD
     ELKPKKKVFE KLQVDLKISG EFVAQWKEQN LMTKLGRITC KTLKGGNIS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024