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Database: UniProt
Entry: A0A182SVT7_9DIPT
LinkDB: A0A182SVT7_9DIPT
Original site: A0A182SVT7_9DIPT 
ID   A0A182SVT7_9DIPT        Unreviewed;       466 AA.
AC   A0A182SVT7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   RecName: Full=Histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
DE            EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184, ECO:0000256|RuleBase:RU361211};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM014447-PA, ECO:0000313|Proteomes:UP000075901};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
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 maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMAM014447-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM014447-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|RuleBase:RU361211};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU361211}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC       {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
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DR   AlphaFoldDB; A0A182SVT7; -.
DR   EnsemblMetazoa; AMAM014447-RA; AMAM014447-PA; AMAM014447.
DR   VEuPathDB; VectorBase:AMAM014447; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000075901; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR025995; Tudor-knot.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF82; HISTONE ACETYLTRANSFERASE KAT8; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Nucleus {ECO:0000256|RuleBase:RU361211};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          181..453
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          60..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        357
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   466 AA;  53389 MW;  61AB0A3AEA017C79 CRC64;
     GNKDELVIGE EYLVQRQDGS WHLAQLIQSR QNPCDPKQLE YYIHYEGLNR RLDQWVTRDR
     ISSDGIPGGS PTGAGGDRPT SVSIPSSASG DGTSARKSPL GSSTVNAKDR FCGLKPGSKE
     AGALLTSGAD YIGSSLDGTD TDRKITRNQK RRHDEINHVQ KTYADMDPTT AALEKEHEAI
     TKVKYIDKLR IGKYEIDTWY FSPYPEEYGK VGTMYVCEYC LRYMRLAKTL KEHKAVCTRR
     QPPGNEIYRK GTLSIFEIDG KDHRFYCQTL CLMAKLFLDH KTLYYDVDPF YFYVLCEIDR
     EGQHIVGYFS KEKESPEGNN VACILILPPY QRKGYGKLLI AFSYELSRRE GIIGSPEKPL
     SDLGKLSYRS YWAYTLLKLI KDYRTTTIKE LSELSGITPE DIIYTLQSMN MVKYWKGQHV
     ICVTVKLIQE HLQMPQFKKP KLMVDPAYLK WTPQKRNNPA KQIKKN
//
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