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Database: UniProt
Entry: G0WF42_NAUDC
LinkDB: G0WF42_NAUDC
Original site: G0WF42_NAUDC 
ID   G0WF42_NAUDC            Unreviewed;       384 AA.
AC   G0WF42;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-MAR-2018, entry version 51.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000256|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03140};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
GN   Name=NDAI0H02290 {ECO:0000313|EMBL:CCD26403.1};
GN   Synonyms=FEN1 {ECO:0000256|HAMAP-Rule:MF_03140};
GN   OrderedLocusNames=NDAI_0H02290 {ECO:0000313|EMBL:CCD26403.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 /
OS   NBRC 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26403.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26403.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease
CC       and 5'-3' exonuclease activities involved in DNA replication and
CC       repair. During DNA replication, cleaves the 5'-overhanging flap
CC       structure that is generated by displacement synthesis when DNA
CC       polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC       It enters the flap from the 5'-end and then tracks to cleave the
CC       flap base, leaving a nick for ligation. Also involved in the long
CC       patch base excision repair (LP-BER) pathway, by cleaving within
CC       the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a
CC       genome stabilization factor that prevents flaps from equilibrating
CC       into structurs that lead to duplications and deletions. Also
CC       possesses 5'-3' exonuclease activity on nicked or gapped double-
CC       stranded DNA, and exhibits RNase H activity. Also involved in
CC       replication and repair of rDNA and in repairing mitochondrial DNA.
CC       {ECO:0000256|HAMAP-Rule:MF_03140, ECO:0000256|SAAS:SAAS00725765}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03140};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate
CC       in the reaction catalyzed by the enzyme. May bind an additional
CC       third magnesium ion after substrate binding. {ECO:0000256|HAMAP-
CC       Rule:MF_03140};
CC   -!- SUBUNIT: Interacts with PCNA. Three molecules of NDAI0H02290 bind
CC       to one PCNA trimer with each molecule binding to one PCNA monomer.
CC       PCNA stimulates the nuclease activity without altering cleavage
CC       specificity. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-
CC       Rule:MF_03140, ECO:0000256|SAAS:SAAS00725720}. Nucleus, nucleolus
CC       {ECO:0000256|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm
CC       {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in the
CC       nucleoli and relocalizes to the nucleoplasm upon DNA damage.
CC       {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
CC       relocalization to the nuclear plasma. {ECO:0000256|HAMAP-
CC       Rule:MF_03140}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03140}.
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DR   EMBL; HE580274; CCD26403.1; -; Genomic_DNA.
DR   RefSeq; XP_003671646.1; XM_003671598.1.
DR   STRING; 1071378.XP_003671646.1; -.
DR   EnsemblFungi; CCD26403; CCD26403; NDAI_0H02290.
DR   GeneID; 11496127; -.
DR   KEGG; ndi:NDAI_0H02290; -.
DR   eggNOG; KOG2519; Eukaryota.
DR   eggNOG; COG0258; LUCA.
DR   KO; K04799; -.
DR   OrthoDB; EOG092C2ISI; -.
DR   Proteomes; UP000000689; Chromosome 8.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:1904162; F:5'-3' exodeoxyribonuclease activity involved in UV-damage excision repair; IEA:EnsemblFungi.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051908; F:double-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; IEA:EnsemblFungi.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0000734; P:gene conversion at mating-type locus, DNA repair synthesis; IEA:EnsemblFungi.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
DR   GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   CDD; cd09867; PIN_FEN1; 1.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
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   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.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000689};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_03140};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_03140};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000256|SAAS:SAAS00725731};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000256|SAAS:SAAS00636222};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN        1    108       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      144    216       XPGI. {ECO:0000259|SMART:SM00484}.
FT   REGION      120    251       I-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   REGION      339    347       Interaction with PCNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_03140}.
FT   COILED      105    125       {ECO:0000256|SAM:Coils}.
FT   METAL        34     34       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL        87     87       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       156    156       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       158    158       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       177    177       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       179    179       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       231    231       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      47     47       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      71     71       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     156    156       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     229    229       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     231    231       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
SQ   SEQUENCE   384 AA;  43315 MW;  9E2836C1EA55F587 CRC64;
     MGIKGLTAII SENAPLAIRK SDIKAFFGRK VAIDASMSLY QFLIAVRQQD GGQLTNDAGE
     TTSHLMGMFY RTLRMIDNGI KPCYVFDGKP PVLKSHELDK RIARRAETEK KFAEATDQAE
     KIKQERRLVK VSKEHNDEAK KLLELMGIPY VNAPGEAEAQ CAELAKKGKV YAAASEDMDT
     LCYRTPYLLR HLTFSEAKKE PIQEINTEQV LQGLELTLEQ FIDLGIMLGC DYCENIRGIG
     PVTAFKLIKE HGSLEKIIEF IESDENTNKK WKVPENWPYK EARELFVTPD IIDGNQITLK
     WEPPKEDALI EFLCKEKLFN EERVKAGIKR LQKGLKAGVQ TRLEGFFKVV PKTKEQLASA
     AAKAKAAKKA NKANKGKGRI IKKR
//
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