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EXO1_ORYSJ
ID   EXO1_ORYSJ              Reviewed;         836 AA.
AC   Q60GC1; A0A0P0V8U2; Q5ZAZ7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Exonuclease 1;
DE            EC=3.1.-.-;
DE   AltName: Full=OsEXO-1;
GN   Name=EXO1; OrderedLocusNames=Os01g0777300, LOC_Os01g56940;
GN   ORFNames=P0413G02.29;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nipponbare;
RA   Furukawa T., Shimada H.;
RT   "Oryza sativa OsEXO-1 gene for Exonuclease-1, complete cds.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
CC   -!- FUNCTION: Putative 5'->3' double-stranded DNA exonuclease which may
CC       also contain a cryptic 3'->5' double-stranded DNA exonuclease activity.
CC       May be involved in DNA mismatch repair (MMR) (By similarity).
CC       {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:0000250}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD53243.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB179769; BAD60834.1; -; mRNA.
DR   EMBL; AP003344; BAD53243.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP008207; BAF06335.2; -; Genomic_DNA.
DR   EMBL; AP014957; BAS74613.1; -; Genomic_DNA.
DR   RefSeq; XP_015612001.1; XM_015756515.1.
DR   RefSeq; XP_015612007.1; XM_015756521.1.
DR   AlphaFoldDB; Q60GC1; -.
DR   SMR; Q60GC1; -.
DR   STRING; 4530.OS01T0777300-00; -.
DR   PaxDb; Q60GC1; -.
DR   PRIDE; Q60GC1; -.
DR   EnsemblPlants; Os01t0777300-00; Os01t0777300-00; Os01g0777300.
DR   GeneID; 4327899; -.
DR   Gramene; Os01t0777300-00; Os01t0777300-00; Os01g0777300.
DR   KEGG; osa:4327899; -.
DR   eggNOG; KOG2518; Eukaryota.
DR   HOGENOM; CLU_008978_4_0_1; -.
DR   InParanoid; Q60GC1; -.
DR   OMA; RKAIWAF; -.
DR   OrthoDB; 796591at2759; -.
DR   BRENDA; 3.1.11.1; 4460.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q60GC1; OS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032183; F:SUMO binding; IEA:EnsemblPlants.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProt.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd09908; H3TH_EXO1; 1.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR032641; Exo1.
DR   InterPro; IPR037315; EXO1_H3TH.
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.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease;
KW   Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..836
FT                   /note="Exonuclease 1"
FT                   /id="PRO_0000315621"
FT   REGION          1..99
FT                   /note="N-domain"
FT   REGION          82..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..230
FT                   /note="I-domain"
FT   REGION          464..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          744..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   836 AA;  92248 MW;  F555F7F041951754 CRC64;
     MGIQGLLPQL KSIMAPIGVE ALKGQTVAVD TYSWLHKGAL SCGDRLCKGL PTTRHIEYCM
     HRVNMLRHHG VKPILVFDGG HLPMKGDQET KRERSRKENL ERAKEHESAG NSRAAFECYQ
     KAVDITPRIA FELIQVLKQE KVDYIVAPYE ADAQMTFLSV NKLVDAVITE DSDLIPFGCS
     RIIFKMDKFG QGVEFHITRL QRCRELDLNG FTMQMLLEMC ILSGCDYLPS LPGMGVKRAH
     ALIQKLKGHE KVIKHLRYSA VSVPPQYEEN FRKAIWAFQF QRVYDPVTED IVHLSGIPHG
     SSEDLDFLGP WLPQTVAKGI AQGNIDPITK EPFEGKTESS ALAFDKVHLN RESSAPSNGK
     KKLDLPVQRN VLTNYFCLAS LEAKRKFRAP KVTPKQQVLN GSLPSPRIED SGTPDLIEDT
     SLPSNNIQVY QCSSEHFSSG TPLDDSINTA SQCSSERVRC DIPRDDSASV SPQCSHDIGS
     DPAEDPDIEG NKVKVNFCNR STIPTGSFLE GTLPGISDPF LDSHNTEPSR AAPRYAEKSN
     VVSANRNITV RSSYFKTVNK RVCTNQGEDE CHDEDNCETG NYTLPGDQQR SSGGILKRRK
     FSDPQNFEDG MFQPTSPHES PPVADKGCDS DSHDGINTNS EGKFGCNVAH VNKYSGIAEK
     SMDKFAALIS SFRYAGSRAS GLRAPLKDVK NTLPVRSVLR PPEQRFGCTA KKTTRVPLQS
     RFSSDATNST DVPDLSTFAY RPTTASAHSD QGKITSKATD AAAGPPDLRT FAYAPTRSTT
     SRFDQSENTR KAMCTADSPP DISTFEYKPM KSAVRRSDGS KFSGAALKAA RRTSRS
 
 
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