ID   SGF11_PICST             Reviewed;         102 AA.
AC   A3LPV8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=SGF11 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=PICST_56322;
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: 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; CP000496; ABN65110.2; -; Genomic_DNA.
DR   RefSeq; XP_001383139.2; XM_001383102.1.
DR   AlphaFoldDB; A3LPV8; -.
DR   SMR; A3LPV8; -.
DR   PRIDE; A3LPV8; -.
DR   EnsemblFungi; ABN65110; ABN65110; PICST_56322.
DR   GeneID; 4836883; -.
DR   KEGG; pic:PICST_56322; -.
DR   eggNOG; ENOG502SG7T; Eukaryota.
DR   HOGENOM; CLU_130538_0_0_1; -.
DR   InParanoid; A3LPV8; -.
DR   OMA; RFASHIS; -.
DR   OrthoDB; 1407283at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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..102
FT                   /note="SAGA-associated factor 11"
FT                   /id="PRO_0000367542"
FT   ZN_FING         75..96
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
SQ   SEQUENCE   102 AA;  11553 MW;  79C6AA2227A26AC7 CRC64;
     MTEQPITLDL VDIVDNIVRK QTLSSFARHV SVQSQTLGNH DTNVPVISNF AVGSNKDIFN
     QDKTKLKTSE ASRYFSCENC GRKIAGGRYA QHVNKCLERR RR