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RECF_TRIEI
ID   RECF_TRIEI              Reviewed;         390 AA.
AC   Q114T6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Tery_1725;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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; CP000393; ABG50988.1; -; Genomic_DNA.
DR   RefSeq; WP_011611363.1; NC_008312.1.
DR   AlphaFoldDB; Q114T6; -.
DR   SMR; Q114T6; -.
DR   STRING; 203124.Tery_1725; -.
DR   PRIDE; Q114T6; -.
DR   EnsemblBacteria; ABG50988; ABG50988; Tery_1725.
DR   KEGG; ter:Tery_1725; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_3; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
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..390
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000048595"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   390 AA;  44299 MW;  D79E9E751CDEA3F0 CRC64;
     MYLKHLHLRQ FRNYRDQQVK FDGAKTILLG DNAQGKSNLL ESVELLSTLK SHRAIRDRDL
     ILDSKQASKI QASLERQLGN IDLALTLRSQ GKRTVAVNGE TISRHLDFLS ILNVVHFSSL
     DLDLVRGGPE VRRYWLDRLL VQLEPVYAHI LLQYNQVLRQ RNALLKKIRQ QKMAAETTGS
     SPSILTQELA LWDAQLATTG SRVIRRRQRL LQKLAPLAGE WHCAISGSME VFKMEYLANV
     IVDSNELIIQ DSLEGVRQAF LEKIKVRAIA EQYQGTTVVG PHRDDVIFTI NDTPARQYGS
     QGQQRTLVLA LKLAELQLIE EVVQEPPLLL LDDVLAELDL HRQNQLLEAI SNRFQTLITT
     THLGCFDGQW LQDTQILSVK SGNISSFLDF
 
 
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