ID   Y1986_DEIRA             Reviewed;         281 AA.
AC   Q9RSY3;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=DegV domain-containing protein DR_1986;
GN   OrderedLocusNames=DR_1986;
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: May bind long-chain fatty acids, such as palmitate, and may
CC       play a role in lipid transport or fatty acid metabolism. {ECO:0000250}.
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DR   EMBL; AE000513; AAF11538.1; -; Genomic_DNA.
DR   PIR; E75330; E75330.
DR   RefSeq; NP_295709.1; NC_001263.1.
DR   RefSeq; WP_010888619.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RSY3; -.
DR   SMR; Q9RSY3; -.
DR   STRING; 243230.DR_1986; -.
DR   EnsemblBacteria; AAF11538; AAF11538; DR_1986.
DR   KEGG; dra:DR_1986; -.
DR   PATRIC; fig|243230.17.peg.2209; -.
DR   eggNOG; COG1307; Bacteria.
DR   HOGENOM; CLU_048251_0_1_0; -.
DR   InParanoid; Q9RSY3; -.
DR   OMA; MALGFCA; -.
DR   OrthoDB; 1288126at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1180.10; -; 1.
DR   InterPro; IPR003797; DegV.
DR   InterPro; IPR043168; DegV_C.
DR   Pfam; PF02645; DegV; 1.
DR   TIGRFAMs; TIGR00762; DegV; 1.
DR   PROSITE; PS51482; DEGV; 1.
PE   3: Inferred from homology;
KW   Lipid-binding; Reference proteome.
FT   CHAIN           1..281
FT                   /note="DegV domain-containing protein DR_1986"
FT                   /id="PRO_0000209764"
FT   DOMAIN          3..278
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         61
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
FT   BINDING         93
FT                   /ligand="hexadecanoate"
FT                   /ligand_id="ChEBI:CHEBI:7896"
FT                   /evidence="ECO:0000250|UniProtKB:Q9X1H9"
SQ   SEQUENCE   281 AA;  29367 MW;  9E307C00DFBE3945 CRC64;
     MSIAIVTDST SDLTPEHLAA LGVTGVPLYV LFEGQLYQDG VQLSARQLVE GVRAGKAIPS
     TSQPSPAEFA QAYAQALEHA DEVLSLHISG QLSGTVGSAR LAAQEFGGRV TVVDTHTVTL
     GLGLQVLRAA ELVRAGQSVP QIVQTLERVY PQADLRFTVD TLDFLRLNGR IGGASALLGG
     LLNIKPLLVV RGGRVDAGGR VRGQKKALAD LAEHVRRYVS QHGGARVAFL ATVGGEEDRA
     AVRAQLSDLH FQDMGDHEIG AVVTVHAGPG AVGVALEPLS A