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Database: UniProt
Entry: I0YU24_COCSC
LinkDB: I0YU24_COCSC
Original site: I0YU24_COCSC 
ID   I0YU24_COCSC            Unreviewed;       347 AA.
AC   I0YU24;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN   ORFNames=COCSUDRAFT_17205 {ECO:0000313|EMBL:EIE21893.1};
OS   Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC   Coccomyxa subellipsoidea.
OX   NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE21893.1, ECO:0000313|Proteomes:UP000007264};
RN   [1] {ECO:0000313|EMBL:EIE21893.1, ECO:0000313|Proteomes:UP000007264}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-169 {ECO:0000313|EMBL:EIE21893.1,
RC   ECO:0000313|Proteomes:UP000007264};
RX   PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA   Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA   Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA   Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA   Van Etten J., Lomsadze A., Borodovsky M.;
RT   "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT   reveals traits of cold adaptation.";
RL   Genome Biol. 13:R39-R39(2012).
CC   -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC       a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC       DNA mismatch repair. {ECO:0000256|RuleBase:RU910737}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU910737};
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:0000256|RuleBase:RU910737};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU910737}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000256|ARBA:ARBA00010563,
CC       ECO:0000256|RuleBase:RU910737}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIE21893.1}.
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DR   EMBL; AGSI01000011; EIE21893.1; -; Genomic_DNA.
DR   RefSeq; XP_005646437.1; XM_005646380.1.
DR   AlphaFoldDB; I0YU24; -.
DR   STRING; 574566.I0YU24; -.
DR   GeneID; 17039878; -.
DR   KEGG; csl:COCSUDRAFT_17205; -.
DR   eggNOG; KOG2518; Eukaryota.
DR   OrthoDB; 126305at2759; -.
DR   Proteomes; UP000007264; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd09908; H3TH_EXO1; 1.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR037315; EXO1_H3TH.
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:SF8; EXONUCLEASE 1; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW   DNA excision {ECO:0000256|RuleBase:RU910737};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU910737};
KW   Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW   ECO:0000256|RuleBase:RU910737};
KW   Exonuclease {ECO:0000256|RuleBase:RU910737};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU910737};
KW   Magnesium {ECO:0000256|RuleBase:RU910737};
KW   Metal-binding {ECO:0000256|RuleBase:RU910737};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU910737};
KW   Nucleus {ECO:0000256|RuleBase:RU910737};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT   DOMAIN          1..100
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          139..209
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
SQ   SEQUENCE   347 AA;  38268 MW;  0BEEEC2B407B852E CRC64;
     MGIQGLLPLL KSITKSPVHV RRYSGQKAAV DAYGWLHKAA YCCSYELCEG IYSDRFVAYC
     MQRVETLQQA GVSPIIIFDG GRLPMKSAEE GTRARSRSEN LEKARAYWQA GNTTAAYESY
     QRAVDISPAT AKQLIEALKA ANVEYIVAPY EADAQMAYLA INGIVQVVIS EDSDMLAYGC
     PRVFFKMDKN GDGQEICMAD LPECRNPSLI GFTPDMFLEM CILAGCDFLK ALSSIGIKKA
     HGHIRKYKTF IRVCKSLRFS GVKVPREYEA DFQRALWTFR HQRVYCPAAR AVVHLRPLPP
     GGLADGVLVL AALPSKEEAD LPFLGPMLPD SVAQGIATGG PLLLEVW
//
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