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