SGF11_CANGA
ID SGF11_CANGA Reviewed; 99 AA.
AC Q6FKC2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN Name=SGF11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN OrderedLocusNames=CAGL0L12738g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complex SAGA. At the promoters, SAGA is
CC required for recruitment of the basal transcription machinery. It
CC influences RNA polymerase II transcriptional activity through different
CC activities such as TBP interaction and promoter selectivity,
CC interaction with transcription activators, and chromatin modification
CC through histone acetylation and deubiquitination. SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). Involved in transcriptional regulation of a subset of SAGA-
CC regulated genes. Within the SAGA complex, participates in a subcomplex,
CC that specifically deubiquitinates histones H2B. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA transcription coactivator-HAT
CC complex. SAGA is built of 5 distinct domains with specialized
CC functions. Within the SAGA complex, SUS1, SGF11, SGF73 and UBP8 form an
CC additional subcomplex of SAGA called the DUB module (deubiquitination
CC module). Interacts directly with SGF73, SUS1 and UBP8.
CC {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of
CC the SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain together with the
CC C-terminal catalytic domain of UBP8 forms the 'catalytic lobe' of the
CC SAGA deubiquitination module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000255|HAMAP-
CC Rule:MF_03047}.
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DR EMBL; CR380958; CAG62296.1; -; Genomic_DNA.
DR RefSeq; XP_449322.1; XM_449322.1.
DR AlphaFoldDB; Q6FKC2; -.
DR SMR; Q6FKC2; -.
DR STRING; 5478.XP_449322.1; -.
DR EnsemblFungi; CAG62296; CAG62296; CAGL0L12738g.
DR GeneID; 2890608; -.
DR KEGG; cgr:CAGL0L12738g; -.
DR CGD; CAL0135254; CAGL0L12738g.
DR VEuPathDB; FungiDB:CAGL0L12738g; -.
DR eggNOG; KOG2612; Eukaryota.
DR HOGENOM; CLU_2320099_0_0_1; -.
DR InParanoid; Q6FKC2; -.
DR OMA; SSQYFHC; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:EnsemblFungi.
DR GO; GO:0008047; F:enzyme activator activity; IEA:EnsemblFungi.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IEA:EnsemblFungi.
DR GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR HAMAP; MF_03047; Sgf11; 1.
DR InterPro; IPR013246; SAGA_su_Sgf11.
DR InterPro; IPR041216; Sgf11_N.
DR Pfam; PF08209; Sgf11; 1.
DR Pfam; PF18519; Sgf11_N; 1.
PE 3: Inferred from homology;
KW Activator; Chromatin regulator; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..99
FT /note="SAGA-associated factor 11"
FT /id="PRO_0000367538"
FT ZN_FING 71..92
FT /note="SGF11-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
SQ SEQUENCE 99 AA; 11531 MW; 03A9F1B99E00FED6 CRC64;
MTEQHETIQS VTDGIYNNLV TSMIHSIVSK ETAREKLLRS RYGSYKQYHY DPNSQLDIHG
NPKQQDSSQY FYCENCGREV SGNRFAAHLQ RCLTRGSRR