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GEN_DROPS
ID   GEN_DROPS               Reviewed;         754 AA.
AC   Q29FC1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Flap endonuclease GEN;
DE            EC=3.1.-.-;
DE   AltName: Full=Flap structure-specific endonuclease GEN;
DE   AltName: Full=Xpg-like endonuclease;
GN   Name=Gen; ORFNames=GA10481;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Endonuclease which cleaves flap structures at the junction
CC       between single-stranded DNA and double-stranded DNA. Specific for 5'-
CC       overhanging flap structures in which the 5'-upstream of the flap is
CC       completely double-stranded. Prefers the blocked-flap structures similar
CC       to those occurring at replication forks, in which the 5' single-strand
CC       overhang of the flap is double-stranded. Also possesses weak 5'- to 3'-
CC       exonuclease activity on nicked but not gapped double-stranded DNA. Does
CC       not cleave bubble-like or Holliday junction substrates (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CH379067; EAL31334.1; -; Genomic_DNA.
DR   RefSeq; XP_001354281.1; XM_001354245.3.
DR   AlphaFoldDB; Q29FC1; -.
DR   SMR; Q29FC1; -.
DR   STRING; 7237.FBpp0276620; -.
DR   EnsemblMetazoa; FBtr0278182; FBpp0276620; FBgn0070538.
DR   GeneID; 4814122; -.
DR   KEGG; dpo:Dpse_GA10481; -.
DR   eggNOG; KOG2519; Eukaryota.
DR   HOGENOM; CLU_013777_2_0_1; -.
DR   InParanoid; Q29FC1; -.
DR   OMA; MCAYLNE; -.
DR   PhylomeDB; Q29FC1; -.
DR   Proteomes; UP000001819; Chromosome X.
DR   Bgee; FBgn0070538; Expressed in female reproductive system and 2 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IEA:EnsemblMetazoa.
DR   GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:EnsemblMetazoa.
DR   GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:EnsemblMetazoa.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; ISS:UniProtKB.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblMetazoa.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR041012; GEN_chromo.
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; PF18704; Chromo_2; 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; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..754
FT                   /note="Flap endonuclease GEN"
FT                   /id="PRO_0000314149"
FT   REGION          1..90
FT                   /note="N-domain"
FT   REGION          130..226
FT                   /note="I-domain"
FT   REGION          479..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..754
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   754 AA;  85187 MW;  A0D064A37CD3FAB9 CRC64;
     MGVKELWTVL TPHAERKPIN ELRGKKVAID LAGWVCESLN VVDYFVHPRH HLKNLFFRTC
     YLIWEQVTPV FVLEGVAPKL KGQVIAKRNE LQFRGVRPKD AATGTQTAAK VDKGRTRFNH
     VLKQCETLLL SMGIQCVQGP GEAEAYAAFL NKHGLVDGVI SQDSDCFAYG AIRVYRNFSV
     STQGAQAAAG GAVDIYDMRE ITSRMDFGQH KIIVMALLCG CDYCPDGIGG IGKDGVLKLF
     NKYKESEILD RLRNWRAETD KYNALEMRVD DKSICSNCGH IGRTQSHTKS GCSVCRTKRG
     CDKTLWKEQR LSIKAELILR RKALLAPEFP NEEIISEFLS EPPTIPNLNL GWRQPNLVKF
     IKQIGHLLQW PEIYCFQKFF PILTRWQVQQ AARTNAIGRV ELVQPVDIIK KRTVKGVASL
     ELRWQDPSGS FQGLIPDKQI SEFELEHPKG IEELYYTVEP LDMLEAAYPD LVASFLKSKE
     KPPKKATRKK KTDPLSAIEN IPETLDKQKA NPAKPKRVVK KKKAPTEQAQ PSLQQFLRRE
     KIGGTPVKDS LPQMAQLPQQ CSTPITKFLP SDLESDCDAV EFDMSDVVNG IISNPNARPT
     VTRHEGRQLH YEALSDDLSM RLAQLSLRKD ELQEEPLPPV AEHKRDLSLV EHLPQSKRLS
     LDDSFDLLVK GDLKKVPHLI QPIRTPVDRF KHQHRISEHL PQPAVEPAAN VSYFFNQSSD
     NADAFEQLMN SSLGIQEQAE EDEEEEDDLV VISD
 
 
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