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EXO5_DANRE
ID   EXO5_DANRE              Reviewed;         394 AA.
AC   F1Q514;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Exonuclease V;
DE            Short=Exo V;
DE            EC=3.1.-.-;
GN   Name=exo5; ORFNames=zgc:123272;
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 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).
CC   -!- FUNCTION: Single-stranded DNA (ssDNA) bidirectional exonuclease
CC       involved in DNA repair. Probably involved in DNA repair following
CC       ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage.
CC       Has both 5'-3' and 3'-5' exonuclease activities with a strong
CC       preference for 5'-ends (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q9H790};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9H790};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P38289};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EXO5 family. {ECO:0000305}.
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DR   EMBL; BX908796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1Q514; -.
DR   SMR; F1Q514; -.
DR   STRING; 7955.ENSDARP00000105428; -.
DR   PaxDb; F1Q514; -.
DR   Ensembl; ENSDART00000129154; ENSDARP00000105428; ENSDARG00000042727.
DR   ZFIN; ZDB-GENE-051113-108; exo5.
DR   eggNOG; KOG4760; Eukaryota.
DR   GeneTree; ENSGT00390000015205; -.
DR   HOGENOM; CLU_013225_0_2_1; -.
DR   InParanoid; F1Q514; -.
DR   OMA; STQNWCE; -.
DR   PhylomeDB; F1Q514; -.
DR   TreeFam; TF332529; -.
DR   PRO; PR:F1Q514; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 15.
DR   Bgee; ENSDARG00000042727; Expressed in mature ovarian follicle and 19 other tissues.
DR   ExpressionAtlas; F1Q514; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR   Gene3D; 3.90.320.10; -; 1.
DR   InterPro; IPR019190; EXOV.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   PANTHER; PTHR14464; PTHR14464; 1.
DR   Pfam; PF09810; Exo5; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; DNA damage; DNA repair; DNA-binding; Exonuclease;
KW   Hydrolase; Iron; Iron-sulfur; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..394
FT                   /note="Exonuclease V"
FT                   /id="PRO_0000421759"
FT   REGION          42..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         373
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  44989 MW;  4DD27E44246F9CB5 CRC64;
     MMDASRSQQP LDAWDDISDS EFLNIPSDEE SIESQLPLIG ETKGKHSVNL DKPSSSSSFH
     KCSEEAPKQE AVKTDDVRGL KRKSLHENSF SPMQRFRKQH LSVTLLCDQT WCEMKSVYNL
     LKPHIKRKEM QRTEVQIGQE IHLSRELEIQ DVVPVDIRTR EDGEAVKLLN MLHMIPLLEA
     GQRVREFPVF GVQEGVFIMG VIDELMYNQK GELVLNELKT RRQNSLPSSA QDKVNCFQVG
     LYKLLFDGLV RGEMKKNHIF DHLKLRSAQI LGAGVQAHAK NLGVHARTFE ELVETLLITV
     SCSDLPCIDL LQIEYFHQGS NGPIGTRVAP FDEAQIRGEL QAYLSYWTGQ REPKGVDIEE
     AWKCRSCLYE EICEWRKNRF TVSDQQAAHS SSHL
 
 
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