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Database: UniProt
Entry: W4K8P3_9HOMO
LinkDB: W4K8P3_9HOMO
Original site: W4K8P3_9HOMO 
ID   W4K8P3_9HOMO            Unreviewed;       405 AA.
AC   W4K8P3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   28-MAR-2018, entry version 33.
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=FEN1 {ECO:0000256|HAMAP-Rule:MF_03140};
GN   ORFNames=HETIRDRAFT_458854 {ECO:0000313|EMBL:ETW81431.1};
OS   Heterobasidion irregulare TC 32-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Bondarzewiaceae; Heterobasidion;
OC   Heterobasidion annosum species complex.
OX   NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW81431.1, ECO:0000313|Proteomes:UP000030671};
RN   [1] {ECO:0000313|EMBL:ETW81431.1, ECO:0000313|Proteomes:UP000030671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW81431.1,
RC   ECO:0000313|Proteomes:UP000030671};
RX   PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA   Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA   Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA   van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA   Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA   Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA   Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E.,
RA   Lombard V., Lucas S., Lunden K., Morin E., Murat C., Park J.,
RA   Raffaello T., Rouze P., Salamov A., Schmutz J., Solheim H.,
RA   Stahlberg J., Velez H., de Vries R.P., Wiebenga A., Woodward S.,
RA   Yakovlev I., Garbelotto M., Martin F., Grigoriev I.V., Stenlid J.;
RT   "Insight into trade-off between wood decay and parasitism from the
RT   genome of a fungal forest pathogen.";
RL   New Phytol. 194:1001-1013(2012).
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 FEN1 bind to one
CC       PCNA trimer with each molecule binding to one PCNA monomer. PCNA
CC       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; KI925458; ETW81431.1; -; Genomic_DNA.
DR   RefSeq; XP_009546078.1; XM_009547783.1.
DR   EnsemblFungi; ETW81431; ETW81431; HETIRDRAFT_458854.
DR   GeneID; 20676960; -.
DR   KEGG; hir:HETIRDRAFT_458854; -.
DR   KO; K04799; -.
DR   Proteomes; UP000030671; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000030671};
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:UP000030671}.
FT   DOMAIN        1    108       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      147    219       XPGI. {ECO:0000259|SMART:SM00484}.
FT   REGION      123    254       I-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   REGION      353    361       Interaction with PCNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_03140}.
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       159    159       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       161    161       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       180    180       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       182    182       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       234    234       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     159    159       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     232    232       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     234    234       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
SQ   SEQUENCE   405 AA;  44858 MW;  0F7D43CD8A957B60 CRC64;
     MGIKGLTGLL SEHAPQSISS HEIKTLFGRK VAIDASMSIY QFLIAVRQKD GEMLQNDAGE
     TTSHLMGFFY RTIRIVENGI KPAYVFDGKP PELKAGVLAK RFEKREEAKE DGEEAKETGT
     TEDVDRFSRR TVKVTREHNE ECRKLLGLMG IPVVIAPSEA EAQCAELARG GKVYAAGSED
     MDTLTFNAPT LYRHLTFSEA KKQPISEINL EKALQGLDMN MSQFIDLCIL LGCDYLEPIR
     GVGPKSALKL IREHGGLAGV VEHLREKQAV KDEAAEDGKK KKGGVQIPDE WPWEEAKRVF
     EKPDVTPADE IELEWKHPDV DGLVEFLVRQ KGFNEERVRK GAEKLSKFLN AKQQGRLDGF
     FTVQPKAPSA KNVKGKKADA KGATGSKRKN KEGDAGPSKK AKAKK
//
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