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FEN1_BABBO
ID   FEN1_BABBO              Reviewed;         672 AA.
AC   A7AX58;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
GN   Name=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140}; ORFNames=BBOV_I000370;
OS   Babesia bovis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Babesiidae; Babesia.
OX   NCBI_TaxID=5865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2Bo;
RX   PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
RA   Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
RA   Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
RA   Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H., Koo H.,
RA   Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q., Smith R.K. Jr.,
RA   Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr., McElwain T.F.,
RA   Nene V.M.;
RT   "Genome sequence of Babesia bovis and comparative analysis of apicomplexan
RT   hemoprotozoa.";
RL   PLoS Pathog. 3:1401-1413(2007).
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:0000255|HAMAP-Rule:MF_03140}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|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:0000255|HAMAP-
CC       Rule:MF_03140};
CC   -!- SUBUNIT: Interacts with PCNA. Three molecules of FEN1 bind to one PCNA
CC       trimer with each molecule binding to one PCNA monomer. PCNA stimulates
CC       the nuclease activity without altering cleavage specificity.
CC       {ECO:0000255|HAMAP-Rule:MF_03140}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}.
CC       Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in
CC       the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
CC       {ECO:0000255|HAMAP-Rule:MF_03140}.
CC   -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
CC       relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
CC       Rule:MF_03140}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
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DR   EMBL; AAXT01000006; EDO05131.1; -; Genomic_DNA.
DR   RefSeq; XP_001608699.1; XM_001608649.1.
DR   AlphaFoldDB; A7AX58; -.
DR   SMR; A7AX58; -.
DR   STRING; 5865.XP_001608699.1; -.
DR   EnsemblProtists; EDO05131; EDO05131; BBOV_I000370.
DR   GeneID; 5476902; -.
DR   KEGG; bbo:BBOV_I000370; -.
DR   VEuPathDB; PiroplasmaDB:BBOV_I000370; -.
DR   eggNOG; KOG2519; Eukaryota.
DR   InParanoid; A7AX58; -.
DR   Proteomes; UP000002173; Partially assembled 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   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; 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   DNA damage; DNA repair; DNA replication; Endonuclease; Exonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Mitochondrion; Nuclease; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..672
FT                   /note="Flap endonuclease 1"
FT                   /id="PRO_0000403531"
FT   REGION          1..106
FT                   /note="N-domain"
FT   REGION          124..252
FT                   /note="I-domain"
FT   REGION          327..335
FT                   /note="Interaction with PCNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   REGION          361..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         47
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         72
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         160
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         160
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         162
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         230
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         232
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03140"
SQ   SEQUENCE   672 AA;  74767 MW;  342DF882CD0ED63D CRC64;
     MGIKGLIGFL SDAAPGCISE VTLESLSGTS IAIDASTALY QFTIAIREGS YLSSLTNSKG
     ESTSHIAGLL NRCIRLLELG IRPVFVFDST PPEAKSQTLA KRKLLREEAE SSLEKAIEED
     DKEAIRKYVG RTVRITQKEN ESAKKLLRLV GVPVIEAAEE AEAQCAYLCQ RGFVTAVGSE
     DADALVFRCG VLLKNLTASN KPVVRVDLAK ALELLELTHE QFTDFCILCG CDYCGTLKGV
     GPKTAYNLIK KHGSISRILE VRSETLEGYE AAQEYFRDPK VRDITTIDRC EANIDGLREF
     LISENDFSEE RVDKLIERLQ KARSKKTQLS LKSFFGYPPR AANITRNYTV PIKGVSPPAV
     VESAVDSTSD DGKDEVPSDD KVPSVNEVPT VDKVPSVNEV PTVEEAPPAD AVPTVEDTSE
     PPSEEPDAKK RNKRVPIEVD DSLVPDNLKR FICVQHYDPR VTIKRTGASE LGSDSVDSLV
     SHICGVYGIQ SGTPDNDLSV VGEGILWPNP ILQRFRSVTK DLPNSRLHEL WRCSSSHGIS
     WDALDKLYIN FREARDSSVE EWDKYAPEIV DFASKVARDK ITQWLDGSTS CPPRLLRRWT
     HLLYSRWRER YLHVYGPRML SRYLKGEVTD RVLVREINEC LPAGVECSEL PLDTEPSEHN
     PHFVRRVPKS GS
 
 
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