SDS23_YEAS7
ID SDS23_YEAS7 Reviewed; 527 AA.
AC A6ZUC0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Protein SDS23;
GN Name=SDS23; ORFNames=SCY_2003;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Involved in DNA replication and cell separation during
CC budding. {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; AAFW02000099; EDN62058.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZUC0; -.
DR SMR; A6ZUC0; -.
DR EnsemblFungi; EDN62058; EDN62058; SCY_2003.
DR HOGENOM; CLU_024459_1_1_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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; 3.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT CHAIN 1..527
FT /note="Protein SDS23"
FT /id="PRO_0000324963"
FT DOMAIN 101..162
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 185..243
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 272..330
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..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53172"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53172"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53172"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53172"
SQ SEQUENCE 527 AA; 58098 MW; 8AB2A9E337887F19 CRC64;
MPQNTRHTSI VEMLSTPPQL PNSTDLNSLS EQTDKNTEAN KSDTESLHKS ISKSSSSSSL
STLDNTEYSN NNGNSLSTLN SQNLLSVHRQ EWQHTPLSNL VEQNKLIFIR GSISVEEAFN
TLVKHQLTSL PVENFPGDMN CLTFDYNDLN AYLLLVLNRI KVSNDKITSD CQNGKSVPVG
EIVKLTPKNP FYKLPETENL STVIGILGSG VHRVAITNVE MTQIKGILSQ RRLIKYLWEN
ARSFPNLKPL LDSSLEELNI GVLNAARDKP TFKQSRVISI QGDEHLIMAL HKMYVERISS
IAVVDPQGNL IGNISVTDVK HVTRTSQYPL LHNTCRHFVS VILNLRGLET GKDSFPIFHV
YPTSSLARTF AKLVATKSHR LWIVQPNDNQ PTASSEKSSS PSPSTPPVTT LPSLASSYHS
NTQSSRMANS PVLKSSDTSN NKINVNINLS GPSPSQPQSP STAMPPPQSP SNCPASPTPA
HFEKEYRTGK LIGVVSLTDI LSVLARKQTH HKEIDPQMAR KQRGHIG