ID   SDS23_PODAS             Reviewed;         513 AA.
AC   Q874W3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Protein SDS23;
GN   Name=SDS23;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA   Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA   Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT   "Characterization of the genomic organization of the region bordering the
RT   centromere of chromosome V of Podospora anserina by direct sequencing.";
RL   Fungal Genet. Biol. 39:250-263(2003).
CC   -!- FUNCTION: Involved in DNA replication and cell separation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SDS23 family. {ECO:0000305}.
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DR   EMBL; BX088700; CAD60769.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q874W3; -.
DR   VEuPathDB; FungiDB:PODANS_5_6150; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:InterPro.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   Gene3D; 3.10.580.10; -; 2.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR016711; Ssd23.
DR   Pfam; PF00571; CBS; 2.
DR   PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 2.
DR   PROSITE; PS51371; CBS; 2.
PE   3: Inferred from homology;
KW   CBS domain; Cytoplasm; Nucleus; Repeat.
FT   CHAIN           1..513
FT                   /note="Protein SDS23"
FT                   /id="PRO_0000324959"
FT   DOMAIN          190..249
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          264..321
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  54951 MW;  FF387B10A9393EF7 CRC64;
     MDIPGAQESA ANSSNSSLGA TLSTSQTERN KSGHITAHRQ SFAEDQRRPP PSPRSHRHPS
     LTQQAVQELM NHPPINRHAN PQYAGRNWQE IAVGELAVAD DVKWTDLDES VQDATLTLLK
     NHPTNAVLVR ETPTSKRAIS TFDYSDLNAY LLVVVGLAKP EEEQIELYDH IAKSAQAQTP
     VALREIQPIL KKSELVALPA EATLDAAVEA FGSGIHRLLI TNSAGEVIGI LSQLRLLEFF
     WKEAVNFPVI DRLYGSVLRD LQIGSTQIIA VNADGPLADA LLLMHNEGLT SVAVVDQGLN
     VLGNISTADL RLLTSTNNLP LLKRSCMHFI SVILNERGVE HGRDSFPVFY VNPYSTLAHT
     VAKLVATRSH RMWVVETASP SPSAPATPLL QPVQLGVTAA TAPPPTSVTG VGSSSSPGPQ
     PTVLVSSQTP SAPQSPLPGQ SFPSVPSASL PGAHVSGRLS GVVSLTDVLN LFAKSSGLRP
     SDPSEQRARR RRSSSASVRP SLDAGRGSVD FRR