ID   SGF11_MUSDO             Reviewed;         220 AA.
AC   B1PM81;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047};
GN   Name=Sgf11 {ECO:0000255|HAMAP-Rule:MF_03047};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=18980233; DOI=10.1002/arch.20283;
RA   An S., Wang S., Stanley D., Song Q.;
RT   "Identification of a novel bursicon-regulated transcriptional regulator,
RT   md13379, in the house fly Musca domestica.";
RL   Arch. Insect Biochem. Physiol. 70:106-121(2009).
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. {ECO:0000255|HAMAP-Rule:MF_03047}.
CC   -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT
CC       complexes. Within the SAGA complex, participates in a subcomplex of
CC       SAGA called the DUB module (deubiquitination module) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03047}.
CC   -!- INDUCTION: By bursicon. {ECO:0000269|PubMed:18980233}.
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 forms part of the
CC       'catalytic lobe' of the SAGA deubiquitination module.
CC       {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; EU477240; ACA48515.1; -; mRNA.
DR   RefSeq; NP_001273803.1; NM_001286874.1.
DR   AlphaFoldDB; B1PM81; -.
DR   STRING; 7370.XP_005187611.1; -.
DR   GeneID; 101888544; -.
DR   KEGG; mde:101888544; -.
DR   CTD; 40035; -.
DR   VEuPathDB; VectorBase:MDOA001579; -.
DR   eggNOG; KOG2612; Eukaryota.
DR   Proteomes; UP000095301; Unplaced.
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   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..220
FT                   /note="SAGA-associated factor 11 homolog"
FT                   /id="PRO_0000367535"
FT   ZN_FING         126..147
FT                   /note="SGF11-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03047"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  23900 MW;  F4B31D7A3A929DFA CRC64;
     MSTGTANSAV SSKSTNSTTS TSKVPVNEKS NNSQNANTST ASIIKSYREI VNDPKNLDEA
     ANYLYQSLLD DAVVGVFLEI HHLRKTGNLT AMDGVNEDES ETSFRIVDMP NFDIFGISTA
     KKPMDCTCPN CDRPVSAARF APHLEKCMGM GRISSRIASR RLATKESNSA SSSSSSSYLQ
     TTNAGSDDED DVDWSSEKRR KKSSQNSRNN GSKKNNGKTF