ID A0A182MW85_9DIPT Unreviewed; 823 AA.
AC A0A182MW85;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 08-NOV-2023, entry version 36.
DE SubName: Full=Histone acetyltransferase {ECO:0000313|EnsemblMetazoa:ACUA027777-PA};
OS Anopheles culicifacies.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles; culicifacies species complex.
OX NCBI_TaxID=139723 {ECO:0000313|EnsemblMetazoa:ACUA027777-PA, ECO:0000313|Proteomes:UP000075883};
RN [1] {ECO:0000313|Proteomes:UP000075883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-37 {ECO:0000313|Proteomes:UP000075883};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles culicifacies species A.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACUA027777-PA}
RP IDENTIFICATION.
RC STRAIN=A-37 {ECO:0000313|EnsemblMetazoa:ACUA027777-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AXCM01002025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182MW85; -.
DR STRING; 139723.A0A182MW85; -.
DR EnsemblMetazoa; ACUA027777-RA; ACUA027777-PA; ACUA027777.
DR VEuPathDB; VectorBase:ACUA027777; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000075883; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 664..823
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 88291 MW; 1644FE5F44893CBB CRC64;
MPQRKKSTST ESSSGSSSDS SSSGSDSGSS GGSDSGSSSS ESDSSSSREP SPRPTNSNNA
VLAGATSGSV AQSKTNDKIV RRRSSEVGGA TLKTGSKPDS AKDKPLALKQ QKLSKSSISS
SDDDDSEPDT SKASTAGKKG PGGDMAKKKS VAAVQGKERA PGPLPIGGGK VPPSVIKQQH
QQHHQNATPA TKGAVKASTV VKSLHKSNNN GASAGSGVKK PTPNAAQSLT TPASKGKKKS
IFSPVNSSES EVETTPEKPD LPDRRTSSSS STSGNAASAA NTAASSELFD KNPSGGGASS
TAALQRGRGR PRKASQVGTQ NITGTKPVGQ VKPQISGASG ITKAVSPTAV PSSKSIKSPI
RALSSATSSS SESSSSGSSD SETETSDDSS PSISAAAAQN YKKSNNTMKR VLERTPQKTD
TKDGTGAGSD SETERLKQTR KLTRSASTRK SKHLLGKNAS ETDSDVDSVK NVASKSPAKK
APNVPSKGKA KNNIANALSS KRANDKPITK ELLIEEAPIE RRCPLQKCDS LGHMGGQFEK
HFTLEACPMY HNMTIEQTKQ LLQERKLRED ERRRSIPVYE NSKKIQTPEQ KLYAQKIRDL
RARFKPSSPT PLSERPKPLI DHDGNEIKAE PHIAGIVPDY DLQLFREAQA LASESIEKEL
GDMVTGKGTK YISMGRHCMQ VWYQSPYPDD ATRLPKLYLC EFCLRYQKSE VGMKRHAAKC
VWRHPPGDEI YRKGKLGVWQ VDGKRHKQYC QHLCLLAKFF LDHKTLYYDV EPFLFYVMTL
ADSDGCHTVG YFSKVSAIML MWNSCIRLYP IHGRLVNYNL IND
//