ID   Y1903_DEIRA             Reviewed;         288 AA.
AC   Q9RT62;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=DegV domain-containing protein DR_1903;
GN   OrderedLocusNames=DR_1903;
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; AAF11454.1; -; Genomic_DNA.
DR   PIR; H75339; H75339.
DR   RefSeq; NP_295626.1; NC_001263.1.
DR   RefSeq; WP_010888538.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RT62; -.
DR   SMR; Q9RT62; -.
DR   STRING; 243230.DR_1903; -.
DR   EnsemblBacteria; AAF11454; AAF11454; DR_1903.
DR   KEGG; dra:DR_1903; -.
DR   PATRIC; fig|243230.17.peg.2118; -.
DR   eggNOG; COG1307; Bacteria.
DR   HOGENOM; CLU_048251_0_1_0; -.
DR   InParanoid; Q9RT62; -.
DR   OMA; DERELSC; -.
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..288
FT                   /note="DegV domain-containing protein DR_1903"
FT                   /id="PRO_0000209763"
FT   DOMAIN          2..280
FT                   /note="DegV"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00815"
FT   BINDING         59
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   288 AA;  30472 MW;  263796B0D39DF984 CRC64;
     MIAVTTESTA DILPLQLGYS GIHLLPVPLG HQGQVYSERE LPPDQLVNLI RTTGEPARTL
     AIDDEVVART FEAALQGSKS GRLVHVASGS RFTPHFEVAA RVAGQFGVRV QVIDGGTVSY
     ALGVQALHAA HLADQGADFG QIARALAELR ERTLLTFAVE SLDFLRVNGR IGNVAAFIGN
     WLGLRPLLAV EAGEVVSKAR VRGQAAAVRT LLSATHQFQH QTGETLRLYC GHTIGGEGAA
     EQLQGQLQAV YRDLPAPLHP LGSGLTANVG PGVVAVLAFP RRFGLGHA