ID Q2S0T4_SALRD Unreviewed; 110 AA.
AC Q2S0T4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Conserved domain protein {ECO:0000313|EMBL:ABC44050.1};
GN Name=cspa {ECO:0000313|EMBL:ABC44050.1};
GN OrderedLocusNames=SRU_2091 {ECO:0000313|EMBL:ABC44050.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44050.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44050.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000408}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000159; ABC44050.1; -; Genomic_DNA.
DR RefSeq; YP_446197.1; NC_007677.1.
DR AlphaFoldDB; Q2S0T4; -.
DR STRING; 309807.SRU_2091; -.
DR EnsemblBacteria; ABC44050; ABC44050; SRU_2091.
DR KEGG; sru:SRU_2091; -.
DR eggNOG; COG1278; Bacteria.
DR HOGENOM; CLU_117621_0_0_10; -.
DR OrthoDB; 9805039at2; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR11544; COLD SHOCK DOMAIN CONTAINING PROTEINS; 1.
DR PANTHER; PTHR11544:SF60; LD37574P; 1.
DR Pfam; PF00313; CSD; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT DOMAIN 1..67
FT /note="CSD"
FT /evidence="ECO:0000259|PROSITE:PS51857"
FT REGION 66..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 110 AA; 12138 MW; 705C958E09CF045B CRC64;
MRTSTVKWFD AKKGYGFIHH PDDGEDVFVH YSNIQSDDDF KTLKSDQHVR FEMNDGPKGL
HALEVAPLDD EEAPSADDDN EPELTPADVD PTATVDPSPS GDDSSSDSSW
//
