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
//