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Database: UniProt
Entry: A0A109FDN5_9BASI
LinkDB: A0A109FDN5_9BASI
Original site: A0A109FDN5_9BASI 
ID   A0A109FDN5_9BASI        Unreviewed;       569 AA.
AC   A0A109FDN5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=CSD domain-containing protein {ECO:0000259|PROSITE:PS51857};
GN   ORFNames=RHOSPDRAFT_35851 {ECO:0000313|EMBL:KWU42592.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU42592.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU42592.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU42592.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; KQ954504; KWU42592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FDN5; -.
DR   STRING; 1305733.A0A109FDN5; -.
DR   OrthoDB; 1425506at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
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; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR46109; PROTEIN LIN-28; 1.
DR   PANTHER; PTHR46109:SF1; PROTEIN LIN-28 HOMOLOG; 1.
DR   Pfam; PF00313; CSD; 1.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS51857; CSD_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          409..479
FT                   /note="CSD"
FT                   /evidence="ECO:0000259|PROSITE:PS51857"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..569
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  59335 MW;  3D6F2A0CCC461F61 CRC64;
     MHLRAASSPS TALKPTPARS ESAKPTSKAT AAASAGRRTS SLTSSSELPR PPRRHSAQVA
     AYTRQADKEN APVDDKPALD NSKAGGGGLE KPQELANVKI EMSTSSNATK TKISTAAAAT
     ALKPKSSNVK AFQSTVSPLM HFDEPAPLPT ALFSGLAISG GVSPSQDVSS SATRSFSGPA
     ALQQQQYALL ANYAAQESGY LSVPTSPLPF YNPGFGVSPA AVSNPAAAAY YYPTDFSAFF
     YPQSYAASSP PGTPLSTSTG AVPPSSSGTT TGTTTGNNNH QHQQQLQLYP PSLGLGRPYW
     YGPATTTPSS ANTSLSLSSV AASSLGLSPG NSRSTSATSV ASAGEFDGAN KVANTAAAAP
     ATSAAIVYPI PYAYSTPFVA ATAVPAAPPP RGEETTTIRE RLEGGAVLSS KGACKFFDVE
     KGFGFIIDDH AEELGADVFI HYTGIEQTRG FRCLAQHERV EYALVKHSSG RFQALKLRGE
     NGAPLKGLDD ARQAAAFDRM NSKAAAIWSE DEENVCPPGS AKGRNRRGFA PAYYKGNMRV
     PPPPRIRRTP VEEDQEDGEG DSCVEVDDE
//
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