RECF_DEIRA
ID RECF_DEIRA Reviewed; 359 AA.
AC Q9RVE0;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA replication and repair protein RecF;
GN Name=recF; OrderedLocusNames=DR_1089;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000305}.
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DR EMBL; AE000513; AAF10663.1; -; Genomic_DNA.
DR PIR; A75438; A75438.
DR RefSeq; NP_294813.1; NC_001263.1.
DR RefSeq; WP_010887732.1; NZ_CP015081.1.
DR PDB; 2O5V; X-ray; 1.61 A; A=1-359.
DR PDBsum; 2O5V; -.
DR AlphaFoldDB; Q9RVE0; -.
DR SMR; Q9RVE0; -.
DR STRING; 243230.DR_1089; -.
DR EnsemblBacteria; AAF10663; AAF10663; DR_1089.
DR KEGG; dra:DR_1089; -.
DR PATRIC; fig|243230.17.peg.1285; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_0; -.
DR InParanoid; Q9RVE0; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR EvolutionaryTrace; Q9RVE0; -.
DR Proteomes; UP000002524; Chromosome I.
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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:CACAO.
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; 2.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..359
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196413"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2O5V"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 144..165
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2O5V"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 176..207
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:2O5V"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 268..290
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2O5V"
FT HELIX 307..319
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 320..329
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:2O5V"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2O5V"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:2O5V"
SQ SEQUENCE 359 AA; 39141 MW; 9FD36A26CAFF3ECB CRC64;
MGDVRLSALS TLNYRNLAPG TLNFPEGVTG IYGENGAGKT NLLEAAYLAL TGQTDAPRIE
QLIQAGETEA YVRADLQQGG SLSIQEVGLG RGRRQLKVDG VRARTGDLPR GGAVWIRPED
SELVFGPPSG RRAYLDSLLS RLSARYGEQL SRYERTVSQR NAALRGGEEW AMHVWDDVLL
KLGTEIMLFR RRALTRLDEL AREANAQLGS RKTLALTLTE STSPETYAAD LRGRRAEELA
RGSTVTGPHR DDLLLTLGDF PASDYASRGE GRTVALALRR AELELLREKF GEDPVLLLDD
FTAELDPHRR QYLLDLAASV PQAIVTGTEL APGAALTLRA QAGRFTPVAD EEMQAEGTA
