SDS23_ASHGO
ID SDS23_ASHGO Reviewed; 487 AA.
AC Q75EC0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Protein SDS23;
GN Name=SDS23; OrderedLocusNames=AAR154W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50521.1; -; Genomic_DNA.
DR RefSeq; NP_982697.1; NM_208050.1.
DR AlphaFoldDB; Q75EC0; -.
DR SMR; Q75EC0; -.
DR STRING; 33169.AAS50521; -.
DR EnsemblFungi; AAS50521; AAS50521; AGOS_AAR154W.
DR GeneID; 4618713; -.
DR KEGG; ago:AGOS_AAR154W; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_024459_1_1_1; -.
DR InParanoid; Q75EC0; -.
DR OMA; HRMWVTD; -.
DR Proteomes; UP000000591; Chromosome I.
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; 3.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 3: Inferred from homology;
KW CBS domain; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..487
FT /note="Protein SDS23"
FT /id="PRO_0000324945"
FT DOMAIN 105..165
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 189..248
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 274..333
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 396..469
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 52792 MW; F331B7CA0FFEB6B8 CRC64;
MREKQQGTTG AGGMSSGAAA ASPGQRHASI VEMLSTPPPA IVVQTGMEDE NVRATGGETA
ADGDERRTLS RQSSTSSTES HASATSCLTK VHAQKWQHIE LSQLVEENKL VFINAEMSVE
EAFNTLVEHN LTSLPVERYP GDMDCVTFDY NDLNSYLLLV LGKTTVADEE ITRQCQSGQP
VPVGRIVKLT PKNPFYKVPE TEDLSTVMGI LGSGVHRVAI VDSTSSSIRG ILSQRRLMKY
LWDNARQFSN LEVLLNSSLQ KLGIGVLDPH TPPTSRQSRV ISILDTEPLL VALHKMHTER
ISSIAVIDHQ GMLLGNISVT DVKQVTRTSQ YPLLHNTCRH FISVILNNRG LEMGKDSFPI
FHVYPTSSLA RTVAKLVATK AHRLWIVQPV EQGVLVSPPV APTTIDGSSE FSSRHVSPSP
APSPAGSHGP LTTSASPLGT LDKEYSTGKL IGVVSLTDIL GLLARKHTEN KLVDPLSARR
QRGSVAR