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Database: UniProt
Entry: A0A023B9S8_GRENI
LinkDB: A0A023B9S8_GRENI
Original site: A0A023B9S8_GRENI 
ID   A0A023B9S8_GRENI        Unreviewed;       415 AA.
AC   A0A023B9S8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   28-MAR-2018, entry version 30.
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=GNI_046820 {ECO:0000313|EMBL:EZG74926.1};
OS   Gregarina niphandrodes (Septate eugregarine).
OC   Eukaryota; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC   Eugregarinorida; Gregarinidae; Gregarina.
OX   NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG74926.1, ECO:0000313|Proteomes:UP000019763};
RN   [1] {ECO:0000313|EMBL:EZG74926.1, ECO:0000313|Proteomes:UP000019763}
RP   NUCLEOTIDE SEQUENCE.
RA   Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (DEC-2013) 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: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, ECO:0000256|SAAS:SAAS00725726}.
CC       Note=Resides mostly in the nucleoli and relocalizes to the
CC       nucleoplasm upon DNA damage. {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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EZG74926.1}.
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DR   EMBL; AFNH02000360; EZG74926.1; -; Genomic_DNA.
DR   RefSeq; XP_011129616.1; XM_011131314.1.
DR   EnsemblProtists; EZG74926; EZG74926; GNI_046820.
DR   GeneID; 22911738; -.
DR   Proteomes; UP000019763; 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; IPR002421; 5-3_exonuclease_N.
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; 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; SM00475; 53EXOc; 1.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019763};
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   ECO:0000313|EMBL:EZG74926.1};
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:SAAS00725748};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019763}.
FT   DOMAIN        1    109       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN       28    415       53EXOc. {ECO:0000259|SMART:SM00475}.
FT   DOMAIN      148    219       XPGI. {ECO:0000259|SMART:SM00484}.
FT   COILED       99    126       {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       160    160       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       162    162       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       181    181       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       183    183       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      72     72       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     160    160       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   415 AA;  45769 MW;  6B4039297DA10028 CRC64;
     MGIHGLNKFV AEKAPGAVEH AAPQSFMGRT VAVDASTCLY AFMIAIRDSE NYGNLTNEAG
     EATSHIAGML SRAIRMLELG MKPVYVFDGK PPLLKSGELA RRKDRKAQAE AEMKEAKELG
     DDVRVKQLAG RMVRVTKKHN DDVKKLLKLM GIPIIEAPGE AESQCAMLCR AGKADATVSE
     DSDSLCFGTP LLLRSMNFTD KKQPVMVYHL DKLLQTLNFN QEQFIEFCIL CGCDYCDSIK
     GIGPATAYKL LKDYGSIERI IDRLCTRPQH GTATKNIYND GIYTQGVMNQ DQDHMNQEQV
     TGSNEQVTGS NEQVTGSNEQ VTGSNGSGTQ TESLPELNEI SGSGIQDVDK GDDMVDEMVG
     DGLDKKGSDQ KKKKLYELPF MYPWAEAKQL FVYPDVIPLE ELKDLDFQQK ELQGG
//
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