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Database: UniProt
Entry: A0A0M8ZV55_9HYME
LinkDB: A0A0M8ZV55_9HYME
Original site: A0A0M8ZV55_9HYME 
ID   A0A0M8ZV55_9HYME        Unreviewed;       408 AA.
AC   A0A0M8ZV55;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   28-MAR-2018, entry version 18.
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=WN51_04919 {ECO:0000313|EMBL:KOX70179.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Apoidea; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX70179.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX70179.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX70179.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX70179.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) 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}. 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; KQ435876; KOX70179.1; -; Genomic_DNA.
DR   Proteomes; UP000053105; 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; 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; 2.
DR   PROSITE; PS00841; XPG_1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053105};
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:KOX70179.1};
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:SAAS00636222};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105}.
FT   DOMAIN        1    107       XPGN. {ECO:0000259|SMART:SM00485}.
FT   DOMAIN      146    227       XPGI. {ECO:0000259|SMART:SM00484}.
FT   REGION        1    104       N-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   REGION      363    371       Interaction with PCNA.
FT                                {ECO:0000256|HAMAP-Rule:MF_03140}.
FT   COILED       97    117       {ECO:0000256|SAM:Coils}.
FT   METAL        34     34       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL        86     86       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       167    167       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       169    169       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       188    188       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       190    190       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   METAL       260    260       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      47     47       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING      70     70       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     167    167       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     258    258       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
FT   BINDING     260    260       DNA substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03140}.
SQ   SEQUENCE   408 AA;  46224 MW;  BCDEA41089B68482 CRC64;
     MGILGLAKLI ADISPGAIRE QELKHYFGRK VAIDASMCLY QFLIAVRSEG AQLTSVDGET
     TSHLMGTFYR TIRLVEQGIK PVYVFDGKPP DLKGGELAKR DERRDEAQKL LQAAEEAGNA
     EDVEKFNRRL VKVTKAHAEE AKQLLQLMGI PFIDVGKYSR MRHAPCEAEA QCAALVKAGK
     VYATATEDMD ALTFGCNVLL RRLTFSEARK MPIQEFHFDK VLEGLELNHN EVRKNCIRGI
     NRVVFAYLQF IDLCIMLGCD YTNSIKGVGP KRAIELIKTH RSLEKIIENL DTKKFPIPED
     WNYKQARLLF QEPEITDPET NDLKWTEPDE EGLIKYLCGD KQFNEERVRN GAKKLHKARN
     TSTQGRLDTF FKVLSSPNPL KRKVEDSKTT NKKNKKGATG KPRGRPPK
//
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