SDS23_PHANO
ID SDS23_PHANO Reviewed; 536 AA.
AC Q0U194;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Protein SDS23;
GN Name=SDS23; ORFNames=SNOG_14603;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445356; EAT78143.1; -; Genomic_DNA.
DR RefSeq; XP_001804785.1; XM_001804733.1.
DR AlphaFoldDB; Q0U194; -.
DR SMR; Q0U194; -.
DR STRING; 13684.SNOT_14603; -.
DR EnsemblFungi; SNOT_14603; SNOT_14603; SNOG_14603.
DR GeneID; 5981710; -.
DR KEGG; pno:SNOG_14603; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_024459_0_0_1; -.
DR InParanoid; Q0U194; -.
DR OMA; HRMWVTD; -.
DR OrthoDB; 1471847at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
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; 3.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..536
FT /note="Protein SDS23"
FT /id="PRO_0000324956"
FT DOMAIN 105..170
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 198..256
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 274..331
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 335..391
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 536 AA; 57174 MW; 7C0568F426476607 CRC64;
MADHADATKK DGRIPSPLHS LASSTASLGR SPPPALKMAS SPDPRSHRGS FAEQMRGTPS
SPRASRQPSL TQSALQELLN NPPTKGGDAK FQSRDWSSVR LGELVDPSLV RFVEYDTSVE
DATSILVQHG APNVILLRDT KDTRYATGTF DYSDLNAYLL LVVGLAHPDE EDVASFDELA
KKGREGKPIP LRDVKEVGNK KEPLITLPHT ADLTKAIEVF GSGVHRVLVA EEGTTDVIGV
LTQLQLVKFF WENRQSFPDV DQLYPRLIKD LAIGSKTVLA INGDKPLASA LELMNNEGVS
SLPVLDAQNN VIGNISHVDV RLLTKSTSLP LLRSSCIHFI SVILSERGMN DGKDSFPVFH
VNPYSTLAHT VAKLVATRSH RMWVVDSPSP SSSGPPTPAL QPASLVPPSP ITPLPATHIG
PTPVNSTSPT HLAGTGAVAP AISASAISGA SLSGRLSGVI SLTDVLNLFA KASGLHPHDP
DEARRARRRS SSSSMRRSMD SARSESVSAI AGRRGSVNER EKNVQGLGIA RGRGNA