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RECF_KINRD
ID   RECF_KINRD              Reviewed;         391 AA.
AC   A6W3V7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; OrderedLocusNames=Krad_0004;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
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; CP000750; ABS01496.1; -; Genomic_DNA.
DR   RefSeq; WP_012085688.1; NC_009664.2.
DR   AlphaFoldDB; A6W3V7; -.
DR   SMR; A6W3V7; -.
DR   STRING; 266940.Krad_0004; -.
DR   PRIDE; A6W3V7; -.
DR   EnsemblBacteria; ABS01496; ABS01496; Krad_0004.
DR   KEGG; kra:Krad_0004; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_1_1_11; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000001116; Chromosome.
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; Reference proteome; SOS response.
FT   CHAIN           1..391
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000079590"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   391 AA;  42063 MW;  6E4C8DD52B88C492 CRC64;
     MHVAHLSLVD YRSYPTLELD LRPGTTTFVG LNGQGKTNLV EAIGYVATLG SHRVSGDAPL
     VRQGAERAVV RAQLERGGRR ALVELEITPG KANRARLNGN PVRRTRDVLG VLRTVLFAPE
     DLALVKGDPG ERRRYLDELL VTRWPRIAGV RADYDRILRQ RTALLKSAGS AMRSGRADTH
     TLDVWDEHLA TTGAELLSAR LALLADLRSP TDSAYRAVSG GQGDLELGYR SSLPLLAEGV
     ATTPGGEAPT RDALREALLA SMLEQRKSEL DRGVCLVGPH RDDLVLTLGG MPAKGYASHG
     ESWSVALGLR LASYRLLLAD DEVDDPGGPV LVLDDVFAEL DAGRRERLSE VVADAEQVLV
     TAAVPEDVPA ALRGEHTDRV HVTSGAAVRG D
 
 
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