ID   SUC1_CANAL              Reviewed;         501 AA.
AC   P33181; A0A1D8PTX7; Q5A3Z0;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Probable sucrose utilization protein SUC1;
GN   Name=SUC1; OrderedLocusNames=CAALFM_CR09210WA; ORFNames=CaO19.7319;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1729210; DOI=10.1128/jb.174.1.222-232.1992;
RA   Kelly R., Kwon-Chung K.J.;
RT   "A zinc finger protein from Candida albicans is involved in sucrose
RT   utilization.";
RL   J. Bacteriol. 174:222-232(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Affects sucrose utilization and alpha-glucosidase activity.
CC       Probable transcriptional activator.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MAL13 family. {ECO:0000305}.
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DR   EMBL; S75352; AAB20826.2; -; Genomic_DNA.
DR   EMBL; CP017630; AOW31586.1; -; Genomic_DNA.
DR   PIR; A43302; A43302.
DR   RefSeq; XP_716453.1; XM_711360.1.
DR   AlphaFoldDB; P33181; -.
DR   SMR; P33181; -.
DR   STRING; 237561.P33181; -.
DR   PRIDE; P33181; -.
DR   GeneID; 3641916; -.
DR   KEGG; cal:CAALFM_CR09210WA; -.
DR   CGD; CAL0000197139; SUC1.
DR   VEuPathDB; FungiDB:CR_09210W_A; -.
DR   eggNOG; ENOG502S2FW; Eukaryota.
DR   HOGENOM; CLU_016574_7_1_1; -.
DR   InParanoid; P33181; -.
DR   OMA; WPVIDHE; -.
DR   OrthoDB; 1082475at2759; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000025; P:maltose catabolic process; IMP:CGD.
DR   GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:CGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:CGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR   GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..501
FT                   /note="Probable sucrose utilization protein SUC1"
FT                   /id="PRO_0000114981"
FT   DNA_BIND        13..39
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
SQ   SEQUENCE   501 AA;  57110 MW;  E9BC5BFC2C8183E9 CRC64;
     MSKGKRAPYT RPCDSCSFRK VKCDMKTPCS RCVLNNLKCT NNRIRKKCGP KKIRDRTREA
     INNLSNKEDP KTNSFIPHFQ LDKLQPCLET YQTWYYGIWP VLSISDLNMK ITKRDVSAYA
     LACALSAAIL NQIDFISNNG TYCIPEDVKK LDFIGECIRA RTFMNYQMTP TLETILTSFF
     LHVAEVNKGS KPAAIIYLRE AITMAQIIGL HNESTYKSKP VAEAHRMRKI YFMLMVTERF
     MCIDDLIPVV LENSIKEFSL DDEQYSVLID GFKELVKVFS IPSKAIFDRF IQMNDSISMP
     PETAGLLNKI QLELESICIS PVAPDIQKAN IIVSKYWMKA LTWKITRKNN LLDDFVTTLC
     VKYPIELSEQ FLGEIKSIPL RAFESNGPGV VFKLLSIATV LIDSINLSND VSGYESLQRM
     FDLISKLKKT DMIIPRREYD RIKEALTKME IDIFFSSAQS GGYISEVESN GSLDAFLTDP
     LVFYSGSNDN PTPSYIPDYQ K