ID   SGF11_SCHPO             Reviewed;         117 AA.
AC   Q5FC18;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=sgf11; ORFNames=SPAC57A10.14;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329670; CAI46282.1; -; Genomic_DNA.
DR   RefSeq; NP_001018231.1; NM_001018740.2.
DR   AlphaFoldDB; Q5FC18; -.
DR   SMR; Q5FC18; -.
DR   BioGRID; 280473; 7.
DR   IntAct; Q5FC18; 2.
DR   MINT; Q5FC18; -.
DR   STRING; 4896.SPAC57A10.14.1; -.
DR   SwissPalm; Q5FC18; -.
DR   MaxQB; Q5FC18; -.
DR   PaxDb; Q5FC18; -.
DR   EnsemblFungi; SPAC57A10.14.1; SPAC57A10.14.1:pep; SPAC57A10.14.
DR   PomBase; SPAC57A10.14; sgf11.
DR   VEuPathDB; FungiDB:SPAC57A10.14; -.
DR   eggNOG; ENOG502RAWA; Eukaryota.
DR   HOGENOM; CLU_1928800_0_0_1; -.
DR   InParanoid; Q5FC18; -.
DR   OMA; DYTHELT; -.
DR   PRO; PR:Q5FC18; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0071819; C:DUBm complex; IBA:GO_Central.
DR   GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
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; ISO:PomBase.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
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..117
FT                   /note="SAGA-associated factor 11"
FT                   /id="PRO_0000337264"
FT   ZN_FING         72..93
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
SQ   SEQUENCE   117 AA;  13139 MW;  F971CF402AE8F411 CRC64;
     MQPASLAGIS CTIFENLLKD YTHELTQTVH KNAKLSLQKC PACNKHCRQY CTKPGYDIYG
     NSVQTPSNVP YYSCLMCKRE IAASRYAAHL EKCKGRSLSN ATSYSTLFED DNADEED