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Database: UniProt
Entry: C1CVX9_DEIDV
LinkDB: C1CVX9_DEIDV
Original site: C1CVX9_DEIDV 
ID   C1CVX9_DEIDV            Unreviewed;       404 AA.
AC   C1CVX9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative Sporulation related domain-containing protein {ECO:0000313|EMBL:ACO46346.1};
GN   OrderedLocusNames=Deide_14021 {ECO:0000313|EMBL:ACO46346.1};
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414 {ECO:0000313|EMBL:ACO46346.1, ECO:0000313|Proteomes:UP000002208};
RN   [1] {ECO:0000313|EMBL:ACO46346.1, ECO:0000313|Proteomes:UP000002208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115
RC   {ECO:0000313|Proteomes:UP000002208};
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
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DR   EMBL; CP001114; ACO46346.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1CVX9; -.
DR   STRING; 546414.Deide_14021; -.
DR   PaxDb; 546414-Deide_14021; -.
DR   KEGG; ddr:Deide_14021; -.
DR   HOGENOM; CLU_697792_0_0_0; -.
DR   OrthoDB; 71320at2; -.
DR   Proteomes; UP000002208; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 2.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   Pfam; PF05036; SPOR; 2.
DR   SUPFAM; SSF110997; Sporulation related repeat; 2.
DR   PROSITE; PS51724; SPOR; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002208};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          192..270
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   DOMAIN          331..404
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   REGION          66..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..331
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  40436 MW;  E2F5055637B6D263 CRC64;
     MSRPNVAGSR PSPGMARRWP DLMISVLVVL LLGGFGALLM RGNNSAATIT AETESSTAAV
     EADIPAAPGT DNVSATPPSE PAEAVTPPTS PASAAPEPEP TTTTEVPAPA TTAPVTTEAT
     PGTDPVAAAP LQPAPTAAGT EKSEVPSAAT LPETPAAPVT PPTSLTTGNA AAETITISPP
     PAAAVPAAEQ RVPLRSDYRI SLGSFGTEQT VRTQTAGVSG LGYTVHPIDL GGQYVAQVGP
     FADEATARRA LADIRRAFPS AVLYPPRGVS LTGETAPAPQ TPQTPAAQEP AAQTQTPAVQ
     TPAPATGTNT AAATPAPPLP VPAPAEPAAP PSASSPAYLQ VGAFDRVESA QTLVEQLRAA
     GFTPSVNAPE GRKVTVLVGP FSGTALTDAE SKLSAAGHDS FRVR
//
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