GenomeNet

Database: UniProt
Entry: W2TIX7_NECAM
LinkDB: W2TIX7_NECAM
Original site: W2TIX7_NECAM 
ID   W2TIX7_NECAM            Unreviewed;       389 AA.
AC   W2TIX7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
DE   Flags: Fragment;
GN   ORFNames=NECAME_17803 {ECO:0000313|EMBL:ETN82060.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN82060.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA   Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA   Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA   Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA   Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(2014).
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|RuleBase:RU910737}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000256|RuleBase:RU910737}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI658584; ETN82060.1; -; Genomic_DNA.
DR   RefSeq; XP_013304287.1; XM_013448833.1.
DR   AlphaFoldDB; W2TIX7; -.
DR   STRING; 51031.W2TIX7; -.
DR   EnsemblMetazoa; NECAME_17803; NECAME_17803; NECAME_17803.
DR   GeneID; 25357828; -.
DR   KEGG; nai:NECAME_17803; -.
DR   CTD; 25357828; -.
DR   OMA; QNTNDER; -.
DR   OrthoDB; 126305at2759; -.
DR   Proteomes; UP000053676; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
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; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 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|RuleBase:RU910737};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW   Exonuclease {ECO:0000256|RuleBase:RU910737};
KW   Hydrolase {ECO:0000256|RuleBase:RU910737};
KW   Magnesium {ECO:0000256|RuleBase:RU910737};
KW   Metal-binding {ECO:0000256|RuleBase:RU910737};
KW   Nuclease {ECO:0000256|RuleBase:RU910737};
KW   Nucleus {ECO:0000256|RuleBase:RU910737};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT   DOMAIN          55..124
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          317..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ETN82060.1"
FT   NON_TER         389
FT                   /evidence="ECO:0000313|EMBL:ETN82060.1"
SQ   SEQUENCE   389 AA;  43981 MW;  ECB8961E93D69E81 CRC64;
     CQNTNDERRQ RRADNVKAAE LLLSEGKVSE AADKFRRATS ITSEIVESTI EHFRTYKNVD
     ILVSPYESDA QLAFLVNEGF ADVVVTEDSD LIAFGCEKIA FKWSWETGEC TIYEKKELPR
     CFSGAMSSQF DFTKFRRICI LSGCDYLQAG LPGIGLNKAL SFFSKTSRTD LRTLLPRIPN
     YLNMSKLTVS KEFIEEFIRA ENTFMYQFVR PNKGKNSSDY SYAGEVLSPN LAVRLALGNQ
     IENSVIADKF FLPSPIPEWS VWCDKYESCG KQKRRLEEEH KREEKKCGSA FRFDSPSKKR
     AKLDVTIDLI DLEQEDDLKS LQSSSPGEIV QPPDLRCDAS SKEKQGNLRN LATRPKSLKN
     EADPTWTVDA MMKMYGSEEN SSNANAAAA
//
DBGET integrated database retrieval system