(data stored in SCRATCH zone)

SWISSPROT: Q13F96_RHOPS

ID   Q13F96_RHOPS            Unreviewed;       378 AA.
AC   Q13F96;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930555};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=RPD_0003 {ECO:0000313|EMBL:ABE37243.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37243.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37243.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37243.1,
RC   ECO:0000313|Proteomes:UP000001818};
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-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
CC       binds preferentially to single-stranded, linear DNA. It also seems
CC       to bind ATP. {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00032557}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930558}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00365, ECO:0000256|RuleBase:RU000578,
CC       ECO:0000256|SAAS:SAAS00930556}.
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DR   EMBL; CP000283; ABE37243.1; -; Genomic_DNA.
DR   RefSeq; WP_011500436.1; NC_007958.1.
DR   STRING; 316057.RPD_0003; -.
DR   EnsemblBacteria; ABE37243; ABE37243; RPD_0003.
DR   KEGG; rpd:RPD_0003; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269558; -.
DR   KO; K03629; -.
DR   OMA; GQQKSFL; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; RPAL316057:RPD_RS00015-MONOMER; -.
DR   Proteomes; UP000001818; 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   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   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;
DR   PRODOM; Q13F96.
DR   SWISS-2DPAGE; Q13F96.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930557};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|SAAS:SAAS00930531};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354097};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354147};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930553};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930554};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00930551};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578, ECO:0000256|SAAS:SAAS00354122}.
FT   DOMAIN        6    347       SMC_N. {ECO:0000259|Pfam:PF02463}.
FT   NP_BIND      33     40       ATP. {ECO:0000256|HAMAP-Rule:MF_00365}.
SQ   SEQUENCE   378 AA;  40807 MW;  62EA32C7C2E329DD CRC64;
     MTASRITRLT LTHFRNYRAA ALHTRGERVV LVGANGAGKT NCLEAISFLS PGRGLRRATL
     DDVSDHQGDG SWAVSAEVEG ALGLATLGTG IDPPRADAAT TRRCRIDREP VGSATAFGDH
     LRMVWLTPAM DGLFMGAASE RRRFFDRLVL AIDSQHSSRV SALDRSLRSR NRLLEERNAD
     RHWLDAIERE TAELAVAVAA MRGQTAARLA AMLDARGAAS AFPSAKIMLD GWMESALLTE
     PATAVEDRYR AILRDGRLRD AAAGRTLDGP HLTDLQVIYA PKAMPARDAS TGEQKALLIG
     LVLAHAQLVS EITGITPLLL LDEVVAHLDP ARRRALFAEL ERLGAQVWMT GADPAGFAEI
     GPDAEIFTVE SGRIAPQK
//

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