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Database: UniProt
Entry: A0A072NFF4_9DEIO
LinkDB: A0A072NFF4_9DEIO
Original site: A0A072NFF4_9DEIO 
ID   A0A072NFF4_9DEIO        Unreviewed;       358 AA.
AC   A0A072NFF4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578};
GN   Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN   ORFNames=RDMS_01125 {ECO:0000313|EMBL:KEF35633.1};
OS   Deinococcus sp. RL.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=1489678 {ECO:0000313|EMBL:KEF35633.1, ECO:0000313|Proteomes:UP000027898};
RN   [1] {ECO:0000313|EMBL:KEF35633.1, ECO:0000313|Proteomes:UP000027898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL {ECO:0000313|EMBL:KEF35633.1,
RC   ECO:0000313|Proteomes:UP000027898};
RA   Lal R., Mahato N.K., Tripathi C., Verma H., Kumari R., Singh N.;
RT   "Draft genome sequence of Deinococcus sp. strain RL isolated from sediments
RT   of hot springs located at Manikaran, India.";
RL   Submitted (MAY-2014) 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: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|HAMAP-
CC       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:KEF35633.1}.
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DR   EMBL; JMQF01000013; KEF35633.1; -; Genomic_DNA.
DR   RefSeq; WP_034402307.1; NZ_JMQF01000013.1.
DR   AlphaFoldDB; A0A072NFF4; -.
DR   eggNOG; COG1195; Bacteria.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000027898; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
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; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
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; PF13476; AAA_23; 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|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00365};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00365}; Reference proteome {ECO:0000313|Proteomes:UP000027898};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          10..51
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   358 AA;  38529 MW;  F0D96E46AD3437A1 CRC64;
     MQLAALSTLN YRNLAPDTLR FPAGVTGVFG ENGAGKTNLL EAAYLALTGL TDVTRLEQLV
     CAGEREAYVR ADVQQGGSLS LQEVGLGRGR RVLKVDGVRV RTGDLPRGSA VWIRPEDSEL
     VFGPPAGRRA YLDALLSRLS ARYRQQLARY ERTVSQRNAA LRAGEDWAMH VWDEALVGLG
     TDIMLFRRRA LTRLAELAAE ANAALGSRKA LSLSLQESTA PETYGADLRG KRAEELARGA
     TVTGPHRDDL VLRLGDFPAS EYASRGEGRT VALALRRAEL ELLAERFGEK PVLLIDDFSA
     ELDPGRRSFL LELAASVPQA IVTGTERVPG AALSLRAHAG RFTAEGVTVG TGALEVTA
//
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