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Database: UniProt
Entry: FEN1_THAPS
LinkDB: FEN1_THAPS
Original site: FEN1_THAPS 
ID   FEN1_THAPS              Reviewed;         390 AA.
AC   B8C6S5;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   23-MAY-2018, entry version 48.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
GN   Name=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140};
GN   ORFNames=THAPSDRAFT_269347;
OS   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OC   Eukaryota; Stramenopiles; Bacillariophyta; Coscinodiscophyceae;
OC   Thalassiosirophycidae; Thalassiosirales; Thalassiosiraceae;
OC   Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335;
RX   PubMed=15459382; DOI=10.1126/science.1101156;
RA   Armbrust E.V., Berges J.A., Bowler C., Green B.R., Martinez D.,
RA   Putnam N.H., Zhou S., Allen A.E., Apt K.E., Bechner M.,
RA   Brzezinski M.A., Chaal B.K., Chiovitti A., Davis A.K., Demarest M.S.,
RA   Detter J.C., Glavina T., Goodstein D., Hadi M.Z., Hellsten U.,
RA   Hildebrand M., Jenkins B.D., Jurka J., Kapitonov V.V., Kroger N.,
RA   Lau W.W., Lane T.W., Larimer F.W., Lippmeier J.C., Lucas S.,
RA   Medina M., Montsant A., Obornik M., Parker M.S., Palenik B.,
RA   Pazour G.J., Richardson P.M., Rynearson T.A., Saito M.A.,
RA   Schwartz D.C., Thamatrakoln K., Valentin K., Vardi A., Wilkerson F.P.,
RA   Rokhsar D.S.;
RT   "The genome of the diatom Thalassiosira pseudonana: ecology,
RT   evolution, and metabolism.";
RL   Science 306:79-86(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CCMP1335;
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A.,
RA   Detter J.C., Schmutz J., Lindquist E., Shapiro H., Lucas S.,
RA   Glavina del Rio T., Bruce D., Pitluck S., Rokhsar D., Armbrust V.;
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_03140}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-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:0000255|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:0000255|HAMAP-Rule:MF_03140}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}.
CC       Note=Resides mostly in the nucleoli and relocalizes to the
CC       nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
CC   -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
CC       relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
CC       Rule:MF_03140}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
DR   EMBL; CM000644; EED90855.1; -; Genomic_DNA.
DR   RefSeq; XP_002292004.1; XM_002291968.1.
DR   SMR; B8C6S5; -.
DR   STRING; 35128.Thaps269347; -.
DR   PRIDE; B8C6S5; -.
DR   EnsemblProtists; EED90855; EED90855; THAPSDRAFT_269347.
DR   GeneID; 7445577; -.
DR   KEGG; tps:THAPSDRAFT_269347; -.
DR   eggNOG; KOG2519; Eukaryota.
DR   eggNOG; COG0258; LUCA.
DR   HOGENOM; HOG000193853; -.
DR   InParanoid; B8C6S5; -.
DR   KO; K04799; -.
DR   OMA; GSQDYDS; -.
DR   Proteomes; UP000001449; Chromosome 8.
DR   Proteomes; UP000001449; Unassembled WGS sequence.
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:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA replication;
KW   Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN         1    390       Flap endonuclease 1.
FT                                /FTId=PRO_0000403554.
FT   REGION        1    111       N-domain.
FT   REGION      129    260       I-domain.
FT   REGION      343    351       Interaction with PCNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_03140}.
FT   METAL        34     34       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL        93     93       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       165    165       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       167    167       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       186    186       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       188    188       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   METAL       240    240       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING      47     47       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING      77     77       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     165    165       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     238    238       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
FT   BINDING     240    240       DNA substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03140}.
SQ   SEQUENCE   390 AA;  43324 MW;  49AE865116D470F1 CRC64;
     MGIKGLAKLL SDEAPLSLKE VPLSHLHGRK LAIDASMAIY QFLIAVRSGG PGGQNAAMML
     TNADGETTSH IQGIFNRTIR FISEGIRPVY VFDGKPPQFK SGELLKRREK RLKAEQALKA
     AEESGNIEEQ DKQSKRLVRA GTKENEDCIK LLTLMGVPVI RAPCEAEAQA AALARSGKVY
     AAATEDMDAL TFRSPVMVRK MTFANASKSD VQQIFYDKAI EGLEITHDQF VDLCILLGCD
     YCDTIKGIGP KTALKLIREH KNIETILKHL NREKYVVPDI YVEARRLFNH HEVLPDNEIE
     LKWTECQPEP LKSFLVDEMG FNPDRVQASI EKLQKAFKAS AKPQSRMDSF FKVKANPEGD
     KKKAEKRKAE LAASRGKGKK GKGGGGFKKK
//
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