ID SDS23_PICST Reviewed; 530 AA.
AC A3LQC5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Protein SDS23;
GN Name=SDS23; ORFNames=PICST_88034;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; CP000496; ABN64657.2; -; Genomic_DNA.
DR RefSeq; XP_001382686.2; XM_001382649.1.
DR AlphaFoldDB; A3LQC5; -.
DR SMR; A3LQC5; -.
DR STRING; 322104.A3LQC5; -.
DR GeneID; 4837336; -.
DR KEGG; pic:PICST_88034; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_024459_1_0_1; -.
DR InParanoid; A3LQC5; -.
DR OMA; MAPTNLC; -.
DR OrthoDB; 1449566at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
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 CDD; cd02205; CBS_pair_SF; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR016711; Ssd23.
DR PANTHER; PTHR13780; AMP-ACTIVATED PROTEIN KINASE, GAMMA REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR13780:SF163; PROTEIN SDS23-RELATED; 1.
DR Pfam; PF00571; CBS; 2.
DR PIRSF; PIRSF018148; UCP018148_CBS_YBR214w; 1.
DR SMART; SM00116; CBS; 3.
DR SUPFAM; SSF54631; CBS-domain pair; 2.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..530
FT /note="Protein SDS23"
FT /id="PRO_0000324958"
FT DOMAIN 213..274
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 289..347
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58600 MW; 19CA0E2799401F91 CRC64;
MSNPPFQRQQ PSSPLTTPNH HPSNHQHHAS RKPSIVELLS SPPPLPNNTI DDEIHQFSLS
RNTSISSRTS SFSQQQHGAP HHGSNSHHLS VSGMDWSEIP LSELTESNKL IYINSSYSVQ
KAFETLVSNN LTSVPVSISS SNENDLSSCL TFDYSDLNTY LLLIMNKINL SELSVSEIGN
EHDSTAKKHE IITQTINKAK RGEEVPIEFI IKLHPKNPFI KFTENDTLFK VMETLGNGVH
RVAITNLEST KITGILSQRR LIKYMWENAR RFPSLDFYLN STLQDLKIGS STPIFIYEDQ
LLIEALYKMF NERVSSLAVI DRTKSLIGNI SIVDVKNVSS SKNSHLLFKS VLTFISYNLS
QKGIEEGQDQ YPIFHVNKQS SLGRVIAKLV ATQSHRLWIV ESNTRTHQNS ISSPVTIEAT
LNVSANPSSA SSSNANTPEG NFGLPGKLIG VVTLTDILGL FATSKGTKTD PQFARNQRRR
SSTSTTRSSI DSAISVGDGS ARTTNANADS EIFRKSYTAA AKNESAISKD
//
