ID   SGF11_LODEL             Reviewed;          90 AA.
AC   A5DZI5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=SGF11 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=LELG_02772;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981526; EDK44593.1; -; Genomic_DNA.
DR   RefSeq; XP_001526214.1; XM_001526164.1.
DR   AlphaFoldDB; A5DZI5; -.
DR   SMR; A5DZI5; -.
DR   EnsemblFungi; EDK44593; EDK44593; LELG_02772.
DR   GeneID; 5233317; -.
DR   KEGG; lel:LELG_02772; -.
DR   VEuPathDB; FungiDB:LELG_02772; -.
DR   eggNOG; ENOG502SG7T; Eukaryota.
DR   HOGENOM; CLU_130538_0_0_1; -.
DR   InParanoid; A5DZI5; -.
DR   OMA; RFASHIS; -.
DR   OrthoDB; 1407283at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000124; C:SAGA complex; IEA:UniProtKB-UniRule.
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:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03047; Sgf11; 1.
DR   InterPro; IPR013246; SAGA_su_Sgf11.
DR   Pfam; PF08209; Sgf11; 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..90
FT                   /note="SAGA-associated factor 11"
FT                   /id="PRO_0000367541"
FT   ZN_FING         63..84
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
SQ   SEQUENCE   90 AA;  10135 MW;  9EFF1C4F06D7F563 CRC64;
     MINNIIRNQV VTHFADHACM AQATVSIPEL DKLATNLQLA DTNKDIFGQD RSKLKGIEAS
     RYFSCDNCGR KIAGGRFAQH INKCLDRKRK