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SGF11_ASHGO
ID   SGF11_ASHGO             Reviewed;         105 AA.
AC   Q751G1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=SAGA-associated factor 11 {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=SGF11 {ECO:0000255|HAMAP-Rule:MF_03047}; OrderedLocusNames=AGL255W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54236.1; -; Genomic_DNA.
DR   RefSeq; NP_986412.1; NM_211474.1.
DR   AlphaFoldDB; Q751G1; -.
DR   SMR; Q751G1; -.
DR   STRING; 33169.AAS54236; -.
DR   EnsemblFungi; AAS54236; AAS54236; AGOS_AGL255W.
DR   GeneID; 4622705; -.
DR   KEGG; ago:AGOS_AGL255W; -.
DR   eggNOG; KOG2612; Eukaryota.
DR   HOGENOM; CLU_2320099_0_0_1; -.
DR   InParanoid; Q751G1; -.
DR   OMA; SSQYFHC; -.
DR   Proteomes; UP000000591; Chromosome VII.
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..105
FT                   /note="SAGA-associated factor 11"
FT                   /id="PRO_0000367536"
FT   ZN_FING         76..97
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
SQ   SEQUENCE   105 AA;  11831 MW;  505FB1FDF228610A CRC64;
     MTLGRDAMTP LTILSVSETI YHNLLTSMVQ DIVSRTTSRQ QLQDARYPGL APLHHDQRGA
     LDVYGRPKPQ EASVYFRCPN CSRDLSANRF AAHLERCMSR GARRG
 
 
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