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FEN_HALMA
ID   FEN_HALMA               Reviewed;         326 AA.
AC   Q5V5T7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614};
DE            Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_00614};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00614};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614};
GN   Name=fen {ECO:0000255|HAMAP-Rule:MF_00614}; OrderedLocusNames=rrnAC0032;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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. Binds the unpaired 3'-DNA
CC       end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves
CC       one nucleotide into the double-stranded DNA from the junction in flap
CC       DNA, leaving a nick for ligation. Also involved in the base excision
CC       repair (BER) pathway. Acts as a genome stabilization factor that
CC       prevents flaps from equilibrating into structures that lead to
CC       duplications and deletions. Also possesses 5'-3' exonuclease activity
CC       on nicked or gapped double-stranded DNA (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00614};
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:0000255|HAMAP-
CC       Rule:MF_00614};
CC   -!- SUBUNIT: Interacts with PCNA. PCNA stimulates the nuclease activity
CC       without altering cleavage specificity. {ECO:0000255|HAMAP-
CC       Rule:MF_00614}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00614}.
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DR   EMBL; AY596297; AAV45115.1; -; Genomic_DNA.
DR   RefSeq; WP_011222786.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V5T7; -.
DR   SMR; Q5V5T7; -.
DR   STRING; 272569.rrnAC0032; -.
DR   EnsemblBacteria; AAV45115; AAV45115; rrnAC0032.
DR   GeneID; 40154350; -.
DR   KEGG; hma:rrnAC0032; -.
DR   PATRIC; fig|272569.17.peg.844; -.
DR   eggNOG; arCOG04050; Archaea.
DR   HOGENOM; CLU_032444_0_0_2; -.
DR   OMA; GSQDYDS; -.
DR   Proteomes; UP000001169; Chromosome I.
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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR019973; Flap_structure-sp_endonuc_arc.
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.
DR   TIGRFAMs; TIGR03674; fen_arch; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; Endonuclease; Exonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..326
FT                   /note="Flap endonuclease 1"
FT                   /id="PRO_1000200235"
FT   REGION          1..100
FT                   /note="N-domain"
FT   REGION          118..246
FT                   /note="I-domain"
FT   REGION          318..326
FT                   /note="Interaction with PCNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         28
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         82
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         154
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
SQ   SEQUENCE   326 AA;  36132 MW;  6A6DCC5D1426B738 CRC64;
     MGNADLRSLA ALSDVSFDDL GGSVVAVDAH NWLYRYLTTT VKFTSESKYT TSNGEEVANL
     IGVVQGLPKF FEHDMTPVFV FDGAVTDLKD DEVEKRREQR QKYESELEAA REAGDSTRVA
     KLDSRTQRLT DTIVDTTRDL LELLDVPIVD APAEGEGQAS VMARRGDVDY VGTEDYDALL
     FGAPMTLRQI TSKGDPELMD FAATLEHHDL TWEQLVDAAI LMGTDFNEGI SGIGPKTAVK
     DLHEHGDLYT VLAARGEHID HADRIRDLFL DPAATDDYEI PDSIEPDIDA ARTFVTDQWE
     VDADEVARGF ERIDDSVVQT GLDRWA
 
 
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