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Database: UniProt
Entry: A0A165NMA5_EXIGL
LinkDB: A0A165NMA5_EXIGL
Original site: A0A165NMA5_EXIGL 
ID   A0A165NMA5_EXIGL        Unreviewed;       414 AA.
AC   A0A165NMA5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 32.
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   ORFNames=EXIGLDRAFT_710702 {ECO:0000313|EMBL:KZW00945.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW00945.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW00945.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW00945.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'-
CC       3' exonuclease activities involved in DNA replication and repair.
CC       During DNA replication, cleaves the 5'-overhanging flap structure that
CC       is generated by displacement synthesis when DNA polymerase encounters
CC       the 5'-end of a downstream Okazaki fragment. It enters the flap from
CC       the 5'-end and then tracks to cleave the flap base, leaving a nick for
CC       ligation. Also involved in the long patch base excision repair (LP-BER)
CC       pathway, by cleaving within the apurinic/apyrimidinic (AP) site-
CC       terminated flap. Acts as a genome stabilization factor that prevents
CC       flaps from equilibrating into structures that lead to duplications and
CC       deletions. Also possesses 5'-3' exonuclease activity on nicked or
CC       gapped double-stranded DNA, and exhibits RNase H activity. Also
CC       involved in replication and repair of rDNA and in repairing
CC       mitochondrial DNA. {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03140};
CC       Note=Binds 2 magnesium ions per subunit. They probably participate in
CC       the reaction catalyzed by the enzyme. May bind an additional third
CC       magnesium ion after substrate binding. {ECO:0000256|HAMAP-
CC       Rule:MF_03140};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03140}.
CC       Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in
CC       the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
CC       {ECO:0000256|HAMAP-Rule:MF_03140}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}.
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DR   EMBL; KV425897; KZW00945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165NMA5; -.
DR   STRING; 1314781.A0A165NMA5; -.
DR   InParanoid; A0A165NMA5; -.
DR   OrthoDB; 5479162at2759; -.
DR   Proteomes; UP000077266; 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; cd09907; H3TH_FEN1-Euk; 1.
DR   CDD; cd09867; PIN_FEN1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 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:SF9; FLAP ENDONUCLEASE 1; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 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; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_03140};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_03140};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_03140};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_03140};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_03140};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03140};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03140};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03140}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03140};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          1..108
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          147..219
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          267..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  46284 MW;  E6E78B3AD62D69A2 CRC64;
     MGIKGLTALI TEHAPKAFKE HDIKTLFGRK VAIDASMSIY QFLIAVRQQD GQLLTNEAGE
     TTSHLMGFFY RTIRIVENGI KPAYVFDGKP PELKSGVLAK RYERREEAKE EGEEAKETGT
     AEDVERFSRR TVKVTRQHNE ECQKLLRLMG IPVVIAPSEA EAQCAELARG HKVYAAGSED
     MDTLTFGTPV LYRHLTFSEA KKQPISEIDL EKTLEGLEMT MDQFIELCLL LGCDYLEPIK
     GVGPKSALKY IREMGSLEKV VEHLREKQAD RDEANANAEG EGKKKKGGVQ VPENWPWEDA
     KKLFLKPDVT PADQLELKWK NPDIDGLVDF LVTEKGFNEE RVRKGAEKLT KFLNAKQQGR
     LDGFFKAVPK KDDDKPAAKG TGKGKGKDDA KGKKRKADEK DAGGSSSSKK TRKK
//
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