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SGF11_DROVI
ID   SGF11_DROVI             Reviewed;         189 AA.
AC   B4LDA6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=Sgf11 {ECO:0000255|HAMAP-Rule:MF_03047}; ORFNames=GJ14101;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Component of the transcription regulatory histone acetylation
CC       (HAT) complex SAGA, a multiprotein complex that activates transcription
CC       by remodeling chromatin and mediating histone acetylation and
CC       deubiquitination. Within the SAGA complex, participates in a subcomplex
CC       that specifically deubiquitinates histone H2B. The SAGA complex is
CC       recruited to specific gene promoters by activators, where it is
CC       required for transcription. Required for nuclear receptor-mediated
CC       transactivation. Binds independently on SAGA to promoters in an RNA-
CC       dependent manner. Binds to mRNA and is essential for total mRNA export
CC       from the nucleus. Required to counteract heterochromatin silencing.
CC       Controls the development of neuronal connectivity in visual system by
CC       being required for accurate axon targeting in the optic lobe. Required
CC       for expression of ecdysone-induced genes such as br/broad.
CC       {ECO:0000255|HAMAP-Rule:MF_03047}.
CC   -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC       complexes, at least composed of Ada2b, not/nonstop, Pcaf/Gcn5, Sgf11
CC       and Spt3. Within the SAGA complex, Sgf11, e(y)2, and not/nonstop form
CC       an additional subcomplex of SAGA called the DUB module
CC       (deubiquitination module). Interacts directly with not/nonstop.
CC       Interacts with the AMEX complex component xmas-2. Interacts with Cbp80;
CC       important for promoter recruitment of Sgf11 that is not associated with
CC       the DUB module. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC       Rule:MF_03047}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03047}.
CC       Note=Localizes to nuclear periphery, in contact with the nuclear pore
CC       complex (NPC). {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 not/nonstop forms the 'catalytic lobe'
CC       of the 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; CH940647; EDW71013.1; -; Genomic_DNA.
DR   RefSeq; XP_002048671.2; XM_002048635.2.
DR   AlphaFoldDB; B4LDA6; -.
DR   STRING; 7244.FBpp0228518; -.
DR   EnsemblMetazoa; FBtr0230026; FBpp0228518; FBgn0201319.
DR   GeneID; 6624587; -.
DR   KEGG; dvi:6624587; -.
DR   eggNOG; KOG2612; Eukaryota.
DR   HOGENOM; CLU_100743_0_0_1; -.
DR   InParanoid; B4LDA6; -.
DR   OMA; EDSTYRM; -.
DR   OrthoDB; 1407283at2759; -.
DR   PhylomeDB; B4LDA6; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071819; C:DUBm complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-UniRule.
DR   GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR   GO; GO:0016578; P:histone deubiquitination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006406; P:mRNA export from nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Cytoplasm; Metal-binding; mRNA transport;
KW   Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW   Transcription; Transcription regulation; Translocation; Transport; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..189
FT                   /note="SAGA-associated factor 11 homolog"
FT                   /id="PRO_0000367531"
FT   ZN_FING         94..115
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT   REGION          128..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   189 AA;  20562 MW;  0A524A2B29179041 CRC64;
     MAQGHTTASA ILHNFRELIK EPKGLDDAAN YLFQGLLDDV VAGIFIEIHH LRKTGNLTAL
     DGVGEENAES AYRICEMPNL DIFGISTAKK PMDCTCPNCD RLVAATRFAP HLEKCMGMGR
     ISSRIASRRL ATKEGSSASS TSTSTYLQSG NTGGTDDEDD VDWSSDKRKK KSTQNSRNNG
     SKKNNGKTF
 
 
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