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Database: UniProt
Entry: R1CDV0_EMIHU
LinkDB: R1CDV0_EMIHU
Original site: R1CDV0_EMIHU 
ID   R1CDV0_EMIHU            Unreviewed;       416 AA.
AC   R1CDV0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   07-NOV-2018, entry version 48.
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=EMIHUDRAFT_101628 {ECO:0000313|EMBL:EOD20908.1};
OS   Emiliania huxleyi (Pontosphaera huxleyi).
OC   Eukaryota; Haptophyceae; Isochrysidales; Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD20908.1};
RN   [1] {ECO:0000313|EMBL:EOD20908.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD20908.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Allen A., Bidle K., Borodovsky M., Bowler C.,
RA   Brownlee C., Claverie J.-M., Cock M., De Vargas C., Elias M.,
RA   Frickenhaus S., Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A.,
RA   Herman E., Iglesias-Rodriguez D., Jones B., Lawson T., Leese F.,
RA   Lin Y.-C., Lindquist E., Lobanov A., Lucas S., Malik S.-H.B.,
RA   Marsh M.E., Mock T., Monier A., Moreau H., Mueller-Roeber B.,
RA   Napier J., Ogata H., Parker M., Probert I., Quesneville H., Raines C.,
RA   Rensing S., Riano-Pachon D.M., Richier S., Rokitta S., Salamov A.,
RA   Sarno A.F., Schmutz J., Schroeder D., Shiraiwa Y., Soanes D.M.,
RA   Valentin K., Van Der Giezen M., Van Der Peer Y., Vardi A., Verret F.,
RA   Von Dassow P., Wheeler G., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X.,
RA   Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblProtists:EOD20908, ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EnsemblProtists:EOD20908,
RC   ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D.,
RA   de Vargas C., Verret F., von Dassow P., Valentin K., Van de Peer Y.,
RA   Wheeler G., Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G.,
RA   John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.,
RA   Allen A.E., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Cock J.M., Elias M., Gladyshev V.N., Groth M., Guda C., Hadaegh A.,
RA   Iglesias-Rodriguez M.D., Jenkins J., Jones B.M., Lawson T., Leese F.,
RA   Lindquist E., Lobanov A., Lomsadze A., Malik S.B., Marsh M.E.,
RA   Mackinder L., Mock T., Mueller-Roeber B., Pagarete A., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD20908}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (APR-2018) to UniProtKB.
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:SAAS00882638}.
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:SAAS00882753}. 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; KB865995; EOD20908.1; -; Genomic_DNA.
DR   RefSeq; XP_005773337.1; XM_005773280.1.
DR   EnsemblProtists; EOD20908; EOD20908; EMIHUDRAFT_101628.
DR   GeneID; 17266454; -.
DR   KEGG; ehx:EMIHUDRAFT_101628; -.
DR   KO; K04799; -.
DR   Proteomes; UP000013827; 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:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013827};
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:SAAS00882738};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03140,
KW   ECO:0000256|SAAS:SAAS00022948};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013827}.
FT   DOMAIN        1    109       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      149    226       XPGI. {ECO:0000259|SMART:SM00484}.
FT   REGION      374    382       Interaction with PCNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_03140}.
FT   COILED       99    119       {ECO:0000256|SAM:Coils}.
FT   METAL        34     34       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL        88     88       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       161    161       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       163    163       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       182    182       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       184    184       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       243    243       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      47     47       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      72     72       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     161    161       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     241    241       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     243    243       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
SQ   SEQUENCE   416 AA;  46125 MW;  8112014069F2DB45 CRC64;
     MGIHGLSKLL NDNAPRCVRE HKMEYFAGRK IAIDASMQIY QFLIAVRQQG GEGQLTNEAG
     EVTSHLTGML YRTIRMMEAG IKPVFVFDGK PPTLKSGELA KRKERQQAAE TELTRLQEQG
     GSAEDVERQQ KRTVRASREQ SEEVKKLLGL MGVPVVDAPC EAEATCAALA KAGLVYATAT
     EDMDALTFAT PLLIRNLNSP EARERAARKL PIREFNLELA LGTEGLDMSI EQFTDLCILW
     GWDYTNSIKG IGPEMIPDPF PFEEARRMFR EPEVADTSAT PAFKWSDPDV EGLKRRPLPP
     APPHYHHHPL PLPLPLPHPH PLPLVAARRP GGLTSCARCT SCARCSYLID EKQFGEERVL
     KAIERLKKCK GKSGQNRMED FFGKATIIPN KRKEAEAAKG KGKGKAGKGP LKKAKK
//
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