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Database: UniProt
Entry: A0A0N5AU29_9BILA
LinkDB: A0A0N5AU29_9BILA
Original site: A0A0N5AU29_9BILA 
ID   A0A0N5AU29_9BILA        Unreviewed;       509 AA.
AC   A0A0N5AU29;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-NOV-2023, entry version 34.
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   Syphacia muris.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Syphacia.
OX   NCBI_TaxID=451379 {ECO:0000313|Proteomes:UP000046393, ECO:0000313|WBParaSite:SMUV_0000835101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMUV_0000835101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N5AU29; -.
DR   STRING; 451379.A0A0N5AU29; -.
DR   WBParaSite; SMUV_0000835101-mRNA-1; SMUV_0000835101-mRNA-1; SMUV_0000835101.
DR   Proteomes; UP000046393; Unplaced.
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; 2.
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          201..491
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          488..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        393
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   509 AA;  59107 MW;  7FC2D80C3C1C7C66 CRC64;
     MRAKKDRHVM TTDLSLTPTT ELKIGETFVV LRRVQQKDNV SEERCVATLV EIRDHENDDE
     ASTSDEPVAK KVKYCGEELV YCCIEETVEY LIDEVCKVLN EDSGRQNAIV KKSKKLFYVH
     YDGMDRRLDE WVERERIVER AKPGAITPSI LTVPPALASA LEGTLTRSQR RIHEEFNHVQ
     KSYADMDATT AKLEKEHAEM TKVKNIEVIR YGDYEVEAWY VSPYPEKYSK LRKLWICEYC
     MAYMKDEKEY ICHMNHYCIR RQPPGDEIYR KGNLSVFEVD GKAYKAYCQC LCLLSKLFLD
     HKTLFYDVET FLFYVLCEVD QVGAHVVGHF SKERMSANNL ACIMVLPPFQ RKGYGKLLIQ
     LSTLPFIFCF IIVKSEVKCY ELSAREGIIG TPEKPLSDLG KVSYRSYWWY VILGTLDSLD
     IDDITVADLS LYSGIAEDDI MSTLQTMQLI KYWKGDHVVR MTRRLVDYCR SINMGRPPKL
     RLDPQCLRWQ PKSEKPPSRK ESKLSGLYT
//
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