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Database: UniProt
Entry: A0A124SFX1_CYNCS
LinkDB: A0A124SFX1_CYNCS
Original site: A0A124SFX1_CYNCS 
ID   A0A124SFX1_CYNCS        Unreviewed;       406 AA.
AC   A0A124SFX1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 27.
DE   RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN   ORFNames=Ccrd_017120 {ECO:0000313|EMBL:KVI04562.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI04562.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVI04562.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVI04562.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
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|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:KVI04562.1}.
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DR   EMBL; LEKV01001994; KVI04562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124SFX1; -.
DR   STRING; 59895.A0A124SFX1; -.
DR   EnsemblPlants; KVI04562; KVI04562; Ccrd_017120.
DR   Gramene; KVI04562; KVI04562; Ccrd_017120.
DR   OMA; CITTEDS; -.
DR   Proteomes; UP000243975; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd09901; H3TH_FEN1-like; 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; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR044752; PIN-like_EXO1.
DR   InterPro; IPR019734; TPR_repeat.
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; PS50005; TPR; 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|RuleBase:RU910737};
KW   Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW   Exonuclease {ECO:0000256|RuleBase:RU910737, ECO:0000313|EMBL:KVI04562.1};
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:UP000243975};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          1..102
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   REPEAT          99..132
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          141..220
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
SQ   SEQUENCE   406 AA;  46195 MW;  164B1557B2FC4782 CRC64;
     MGIKDLLRFM KPYVEPIHIK KYAGKRVGID AYSWLHKGAY SCSMELCLNM EGDKKFQYLN
     YCMHRINVLR HHNINPVLVF DGGNIPCKAQ TEQDRHSKRK CNLDLAMAKL KEGNINAAAE
     IFQRAVSITP SMAHQLIQIL RSENIEFVVA PYEADAQLAY LSSLDEDKGG IAAVISEDSD
     LLAYGCSSVR ISMELVVFKM DRYGNGEEIV IDKVFDSVGL VILITYKFKM QQYTLDLLFS
     FHNKCSDFSA YGESQTNDDS ECIGMCVLAG CDFLSSVPGI GIAKAHALVS KYRNLDRVLS
     TLKHEKGNQM PEDYFKSFHK AFAVFQHARM CVTFSLLHVR PIIISYSYYP SYMSYIICSY
     DAESKRLKHL TPLPETLVHY LGEEIDFLGP YPLYLLNANQ FQPFEF
//
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