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Database: UniProt
Entry: A0A182R4W4_ANOFN
LinkDB: A0A182R4W4_ANOFN
Original site: A0A182R4W4_ANOFN 
ID   A0A182R4W4_ANOFN        Unreviewed;       457 AA.
AC   A0A182R4W4;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
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 funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN001206-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN001206-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN001206-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; A0A182R4W4; -.
DR   STRING; 62324.A0A182R4W4; -.
DR   EnsemblMetazoa; AFUN001206-RA; AFUN001206-PA; AFUN001206.
DR   VEuPathDB; VectorBase:AFUN001206; -.
DR   VEuPathDB; VectorBase:AFUN2_003544; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000075900; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR000953; Chromo/chromo_shadow_dom.
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:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SMART; SM00298; CHROMO; 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   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|RuleBase:RU361211};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          170..448
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          81..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        346
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   457 AA;  53038 MW;  08201F0D21EB6464 CRC64;
     MDSEDAAQTI FDSASSLVEG CRLPVKMSGT NDWPLAEIIS IREGSDRKCY YYVHYVDFNK
     RLDEWVTEEY LDMRKVQFPR KDGMTTGQNT GVTTPKRLPP ALTCSRPASP VQTPEITVNG
     GAVLEAALQK KISRKRKATS TENEDSEDVP STPTPRQSGS MVAHHDDVVT RMKNVQLIEL
     GRHRIKPWYF APYPQEMCTM SCIYICEFCL KYRKSRKCLE RHTKKCNLRH PPGNEIYRKS
     TISFFEIDGR KNKSYAQNLC LLAKLFLDHK TLYYDTDPFL FYVMTEYDTR GFHIVGYFSK
     EKESTEDYNV ACILTIPPYQ RKGYGKLLIE FSYELSKFEG KTGSPEKPLS DLGLLSYRSY
     WAQTILEILI LQKPTGDNEK PQITINEICE LTSIKKEDVI STLQILNLIN YYKGQYIICI
     NKETIEQHKK AMEKRKIRID SKCLHWTPKD WSKRSKW
//
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