GenomeNet

Database: UniProt
Entry: A0A0G1N234_9BACT
LinkDB: A0A0G1N234_9BACT
Original site: A0A0G1N234_9BACT 
ID   A0A0G1N234_9BACT        Unreviewed;       357 AA.
AC   A0A0G1N234;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|ARBA:ARBA00020170, ECO:0000256|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   ORFNames=UW86_C0009G0015 {ECO:0000313|EMBL:KKT87112.1};
OS   Microgenomates group bacterium GW2011_GWA1_Microgenomates_45_10.
OC   Bacteria.
OX   NCBI_TaxID=1618493 {ECO:0000313|EMBL:KKT87112.1, ECO:0000313|Proteomes:UP000034781};
RN   [1] {ECO:0000313|EMBL:KKT87112.1, ECO:0000313|Proteomes:UP000034781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC       ECO:0000256|RuleBase:RU000578}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|ARBA:ARBA00008016,
CC       ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKT87112.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LCJY01000009; KKT87112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1N234; -.
DR   PATRIC; fig|1618493.3.peg.293; -.
DR   Proteomes; UP000034781; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.1050.90; RecF/RecN/SMC, N-terminal domain; 1.
DR   HAMAP; MF_00365; RecF; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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   NCBIfam; TIGR00611; recf; 1.
DR   PANTHER; PTHR32182; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   PANTHER; PTHR32182:SF0; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00617; RECF_1; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00365};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          22..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   357 AA;  41255 MW;  BECA6884E46F48D5 CRC64;
     MLLNSISLTH FRSFPKSHFD FDGQTIAISG LNGSGKTNLL EAIYLLASAK SFRADVEEEM
     IQETQEVGHV KGKLYSHDHE KKEIEIVLTR GQVGGEKVSR KKFYVNGVSK QVTNFVGNLK
     AVIFGPWDLD LITGSPGLRR RYLDSVLIQT DREYHRALIS YEKGLRQRNK LLEDIREKGA
     SRHQLIFWNK LLIKNGNYLT NKREEFLSFL NLFKPFLNWQ LSFLSRYDRS SISETRLQQY
     SQEEVAAGVT LVGPHRDNVE FFLERDDHNI DLSKFSSRGE QRLGVLWLKL SELEFLASSQ
     ESRPDRPVLL LDDIFSELDH RHRELVITTI GKQQTFITGA DDHLFPNFNS KIQLIRL
//
DBGET integrated database retrieval system