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DIN7_YEAST
ID   DIN7_YEAST              Reviewed;         430 AA.
AC   Q12086; D6VSP7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=DNA damage-inducible protein DIN7;
DE            EC=3.1.-.-;
GN   Name=DIN7; Synonyms=DIN3; OrderedLocusNames=YDR263C; ORFNames=YD9320B.02C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OL1;
RX   PubMed=9079876; DOI=10.1007/s004380050369;
RA   Mieczkowski P.A., Fikus M., Ciesla Z.;
RT   "Characterization of a novel DNA damage-inducible gene of Saccharomyces
RT   cerevisiae, DIN7, which is a structural homolog of the RAD2 and RAD27 DNA
RT   repair genes.";
RL   Mol. Gen. Genet. 253:655-665(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
CC   -!- FUNCTION: 5'->3' double-stranded DNA exonuclease. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: By UV light, methyl methane-sulfonate (MMS) or hydroxyurea
CC       (HU), and during meiosis.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. {ECO:0000305}.
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DR   EMBL; X90707; CAA62233.1; -; Genomic_DNA.
DR   EMBL; Z70202; CAA94102.1; -; Genomic_DNA.
DR   EMBL; Z68290; CAA92581.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12107.1; -; Genomic_DNA.
DR   PIR; S61118; S61118.
DR   RefSeq; NP_010549.3; NM_001180571.3.
DR   AlphaFoldDB; Q12086; -.
DR   SMR; Q12086; -.
DR   BioGRID; 32319; 48.
DR   DIP; DIP-5214N; -.
DR   IntAct; Q12086; 2.
DR   MINT; Q12086; -.
DR   STRING; 4932.YDR263C; -.
DR   PaxDb; Q12086; -.
DR   PRIDE; Q12086; -.
DR   EnsemblFungi; YDR263C_mRNA; YDR263C; YDR263C.
DR   GeneID; 851856; -.
DR   KEGG; sce:YDR263C; -.
DR   SGD; S000002671; DIN7.
DR   VEuPathDB; FungiDB:YDR263C; -.
DR   eggNOG; KOG2518; Eukaryota.
DR   GeneTree; ENSGT00510000047676; -.
DR   HOGENOM; CLU_008978_3_0_1; -.
DR   InParanoid; Q12086; -.
DR   OMA; DVQFRAM; -.
DR   BioCyc; YEAST:G3O-29833-MON; -.
DR   PRO; PR:Q12086; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q12086; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IMP:SGD.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000729; P:DNA double-strand break processing; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IDA:SGD.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR032641; Exo1.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR044752; PIN-like_EXO1.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   PANTHER; PTHR11081; PTHR11081; 1.
DR   PANTHER; PTHR11081:SF8; PTHR11081:SF8; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..430
FT                   /note="DNA damage-inducible protein DIN7"
FT                   /id="PRO_0000154046"
FT   REGION          1..96
FT                   /note="N-domain"
FT   REGION          114..247
FT                   /note="I-domain"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   430 AA;  49034 MW;  2BC23D30832C79E9 CRC64;
     MGIPGLLPQL KRIQKQVSLK KYMYQTLAID GYAWLHRASC ACAFELVMNK PTNKYLQFFI
     KRLQLLKRLK IKPYIVFDGD SLFVKNHTET RRRKKRLENE MIAKKLWSAG NRYNAMEYFQ
     KSVDITPEMA KCIIDYCKLH SIPYIVAPFE ADPQMVYLEK MGLIQGIISE DSDLLVFGCK
     TLITKLNDQG KALEISKDDF SALPENFPLG ELSEQQFRNL VCLAGCDYTS GIWKVGVVTA
     MKIVKRYSEM KDILIQIERT EKLCFSKAFK QQVEFANYAF QYQRVFCPLS NQITTLNNIP
     KAVTNSHAEI IKIMKCIGSV VERGSGVRKD VINTKNIDHK VHEMIAKGEL HPVDMASKLI
     NRERKLKARK LFKVGLLGGE SNSFNKKVEQ PLVDTQDVLS ERENSLDNKN ASSIYMTSPA
     AISGTVPSIF
 
 
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