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RECF_SYNE7
ID   RECF_SYNE7              Reviewed;         387 AA.
AC   Q31KY9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=Synpcc7942_2250;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC       required for DNA replication and normal SOS inducibility. RecF binds
CC       preferentially to single-stranded, linear DNA. It also seems to bind
CC       ATP. {ECO:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00365}.
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DR   EMBL; CP000100; ABB58280.1; -; Genomic_DNA.
DR   RefSeq; WP_011378373.1; NC_007604.1.
DR   AlphaFoldDB; Q31KY9; -.
DR   SMR; Q31KY9; -.
DR   STRING; 1140.Synpcc7942_2250; -.
DR   PRIDE; Q31KY9; -.
DR   EnsemblBacteria; ABB58280; ABB58280; Synpcc7942_2250.
DR   KEGG; syf:Synpcc7942_2250; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_3; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_2250-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.1050.90; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00365; RecF; 1.
DR   InterPro; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00611; recf; 1.
DR   PROSITE; PS00617; RECF_1; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; Nucleotide-binding; SOS response.
FT   CHAIN           1..387
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000236158"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   387 AA;  43910 MW;  53D46BD57E6C5426 CRC64;
     MFLHSLHLQH FRNYRDQTVQ FQAPKTILLG ENAQGKTNLL EAVELFSTLR SHRVSRDRDL
     VQTGAESALL TAVVERDSGE QQLQIQLQQQ GRRRVQRDGE VLRRQLDLLG SLCSVQFSSL
     DLDLVRGGPQ QRRDWLDRLL IQLQPIYAHL QQQYGRVLRQ RNALLRRAES LDLALLAPLN
     WQLAQLGVHI MRRRSRAIQR LVPLAAHWHR EISGQREQLI VAYQPSVLAP DDTDEAIAWQ
     ERMLAQIEAR RAAELGQRTS LVGPHRDDLN LSINGTEARL QASQGQQRTL VLSLKLAELE
     LIEAVLGEPP LLLLDDVLAE LDLRRQQQLL EAIANRFQTL ITTTHLSAFD QSWVETAQIL
     TVQSGHLQSE AVPMAPSSAS LHKSLDS
 
 
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