SDS24_YEAS7
ID SDS24_YEAS7 Reviewed; 527 AA.
AC A6ZLF4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Protein SDS24;
GN Name=SDS24; ORFNames=SCY_0424;
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; AAFW02000011; EDN64823.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZLF4; -.
DR SMR; A6ZLF4; -.
DR PRIDE; A6ZLF4; -.
DR EnsemblFungi; EDN64823; EDN64823; SCY_0424.
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; 1.
DR PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 1.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT CHAIN 1..527
FT /note="Protein SDS24"
FT /id="PRO_0000324964"
FT DOMAIN 114..175
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 283..342
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 443..512
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 424..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38314"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38314"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38314"
SQ SEQUENCE 527 AA; 57187 MW; DC2741550A69C154 CRC64;
MASTSNTFPP SQSNSSNNLP TSRHASIVEM LSTPPLLPHV QVNDTDDKEQ PEESTPPTAT
AAAPGPGCAA TPAPLRDEKP QFKLSAVPMT QTPSQCLSCV HAQKWQHIPL SQLIEQNKLI
FVPGSISVEE AFNTLIKYHL NSIPVESFPG DMNCFTFDYN DLNSYLLLVL NKITVSNKQL
TADCQNGKPV PVGEMVKLTP KNPFYKLPEN ESLSTVMGIL GSGVHRVAIT NEEMTKVKGI
LSQRRLIKYL WDNARSFTSL EPLLNSSLQD LHIGVLNIQS KPTSRQSRVI SIQGEEPLIM
GLYKMHVERI SSIAVIDKQG NLLGNISVTD VKHVTRTSQY PLLHKTCRHF ISVILNSRGL
ETGKDSFPIF HVYPSSSLAR TLAKLVATKS HRLWIVQPPE SSTSASSTNL TAANTAANAV
SATAQSSANG ATPMSKSSSS TSLNSHSPLM TAMEDPPSPR SSAIAIPPPS PASSTNTPNL
FEKEYRTGKL IGVVSLTDII NLLARKQTGN KEVDPQSARR QRGSIAM