ID A0A0L0BVI2_LUCCU Unreviewed; 232 AA. AC A0A0L0BVI2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 02-JUN-2021, entry version 19. DE RecName: Full=SAGA-associated factor 11 homolog {ECO:0000256|HAMAP-Rule:MF_03047}; GN Name=Sgf11 {ECO:0000256|HAMAP-Rule:MF_03047}; GN ORFNames=FF38_11604 {ECO:0000313|EMBL:KNC23993.1}; OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea; OC Calliphoridae; Luciliinae; Lucilia. OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC23993.1, ECO:0000313|Proteomes:UP000037069}; RN [1] {ECO:0000313|EMBL:KNC23993.1, ECO:0000313|Proteomes:UP000037069} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LS {ECO:0000313|EMBL:KNC23993.1, RC ECO:0000313|Proteomes:UP000037069}; RC TISSUE=Full body {ECO:0000313|EMBL:KNC23993.1}; RX PubMed=26108605; DOI=10.1038/ncomms8344; RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C., RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R., RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H., RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P., RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C., RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.; RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future RT interventions."; RL Nat. Commun. 6:7344-7344(2015). 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:0000256|HAMAP-Rule:MF_03047, CC ECO:0000256|RuleBase:RU261113}. CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT CC complexes. {ECO:0000256|RuleBase:RU261113}. CC -!- SUBUNIT: Component of some SAGA transcription coactivator-HAT CC complexes. Within the SAGA complex, participates to a subcomplex of CC SAGA called the DUB module (deubiquitination module). CC {ECO:0000256|HAMAP-Rule:MF_03047}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03047, CC ECO:0000256|RuleBase:RU261113}. CC -!- DOMAIN: The C-terminal SGF11-type zinc-finger domain forms part of the CC 'catalytic lobe' of the SAGA deubiquitination module. CC {ECO:0000256|HAMAP-Rule:MF_03047}. CC -!- DOMAIN: The long N-terminal helix forms part of the 'assembly lobe' of CC the SAGA deubiquitination module. {ECO:0000256|HAMAP-Rule:MF_03047}. CC -!- SIMILARITY: Belongs to the SGF11 family. {ECO:0000256|HAMAP- CC Rule:MF_03047, ECO:0000256|RuleBase:RU261113}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KNC23993.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JRES01001278; KNC23993.1; -; Genomic_DNA. DR EnsemblMetazoa; KNC23993; KNC23993; FF38_11604. DR OMA; EDSTYRM; -. DR OrthoDB; 1407283at2759; -. DR Proteomes; UP000037069; Unassembled WGS sequence. 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: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 {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_03047}; KW Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03047}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03047}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03047}; KW Reference proteome {ECO:0000313|Proteomes:UP000037069}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_03047}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP- KW Rule:MF_03047}; Zinc {ECO:0000256|HAMAP-Rule:MF_03047}; KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_03047}. FT ZN_FING 139..160 FT /note="SGF11-type" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03047" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 173..197 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 232 AA; 24990 MW; 0C41E885CC3CC908 CRC64; MSTGAPNNNN AASSNNSGSK TTTNSTSSTK VPAGNEKSNN VTTTTQNANT STAAILKSYR EIIKDPKSLD EAANYLYQTL LDDAIVGVFI EIHHLRKTGN LTALDGVPDE EAETSSFRIV DMPNFDIFGI STAKKPMDCT CPNCDRPVSA ARFAPHLEKC MGMGRISSRI ASRRLATKES NSASSSSSSS YLQTNAGSDD EDDVDWSSEK RRKKSSQNSR NNGSKKNNGK TF //