ID DRRP_DEIRA Reviewed; 574 AA.
AC Q9RTJ3;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Desiccation/radiation resistance protein DR_1769;
DE Flags: Precursor;
GN OrderedLocusNames=DR_1769;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; 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 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
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).
RN [2]
RP FUNCTION IN RESISTANCE, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=23794625; DOI=10.1128/jb.00418-13;
RA Rajpurohit Y.S., Misra H.S.;
RT "DR1769, a protein with N-terminal beta propeller repeats and a low-
RT complexity hydrophilic tail, plays a role in desiccation tolerance of
RT Deinococcus radiodurans.";
RL J. Bacteriol. 195:3888-3896(2013).
CC -!- FUNCTION: Plays an important role in resistance to desiccation and
CC radiation, maybe by protecting genome integrity under extreme
CC conditions. {ECO:0000269|PubMed:23794625}.
CC -!- DOMAIN: Contains an N-terminal PQQ binding domain and a C-terminal
CC disorganized low-complexity (LC) hydrophilic region.
CC {ECO:0000269|PubMed:23794625}.
CC -!- DISRUPTION PHENOTYPE: Mutant is sensitive to gamma radiation and
CC hypersensitive to desiccation. It shows delayed DNA double-strand break
CC repair and delayed recovery of desiccated nucleoid.
CC {ECO:0000269|PubMed:23794625}.
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DR EMBL; AE000513; AAF11323.1; -; Genomic_DNA.
DR PIR; F75356; F75356.
DR RefSeq; NP_295492.1; NC_001263.1.
DR RefSeq; WP_010888404.1; NZ_JMLF01000027.1.
DR AlphaFoldDB; Q9RTJ3; -.
DR SMR; Q9RTJ3; -.
DR STRING; 243230.DR_1769; -.
DR PaxDb; 243230-DR_1769; -.
DR EnsemblBacteria; AAF11323; AAF11323; DR_1769.
DR GeneID; 69518009; -.
DR KEGG; dra:DR_1769; -.
DR PATRIC; fig|243230.17.peg.1981; -.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_473061_0_0_0; -.
DR InParanoid; Q9RTJ3; -.
DR OrthoDB; 55730at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR44394; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44394:SF1; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 7.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..574
FT /note="Desiccation/radiation resistance protein DR_1769"
FT /id="PRO_0000429794"
FT REGION 400..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 58433 MW; 6B45667FF96C7C7C CRC64;
MPDPAARRFS LPPFPLAALA LSVALLGAPA SLAQTAAPAP APAQTPAAAS RAAAPRVSWT
KPLKVSSPVS IGPRGELTYV GNDSRVHRTD ASGKELWSFA LGDIGRAQPV LTPDGGVITA
AYDDTVYALS PAGQLTWKAK LDGDVFASPA LRPDGSVVVA TAGGTVYALS SSGQTLWSYK
VGAPVFSSPA VAADGTIYFG AQNGRLHALS PEGRLTWTYA ARSSVFSSPA LDAEGNLYFG
SGDRSIYSLS PAGTLRWVQP TGLFVNASPI VTRAGLVVVG SYDGQLYALN TNGQVAWTYA
AGAAIAAPAA ELSDGSVVVG DLNGTLHAVT PTGQALWTLP GGAKIDTGAA VSDQGTLYFA
VDGGNLNAVE NLRPLATGPW PTFRASPLGW GRSATAAELT AQTQARQAAA AASTSQQPRL
PTLAQAPAPT PAPAQTTPRP QPTPAQPATP AAPVPPVASP APATARLTPQ VIGGVIYLPL
SPIAAGLGYQ VQAGSPTRAL LVAGSQRLTV PVRAVGGQSL IALRFVTGLP GVSVERQAGT
LTLRREGLSA ALPLDLAQLL PWAPQPEFPG VVRR
//
