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Database: UniProt
Entry: A0A0C2DM19_9BILA
LinkDB: A0A0C2DM19_9BILA
Original site: A0A0C2DM19_9BILA 
ID   A0A0C2DM19_9BILA        Unreviewed;       353 AA.
AC   A0A0C2DM19;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Histone acetyltransferase {ECO:0000256|RuleBase:RU361211};
DE            EC=2.3.1.48 {ECO:0000256|RuleBase:RU361211};
GN   ORFNames=ANCDUO_06039 {ECO:0000313|EMBL:KIH63657.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH63657.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH63657.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH63657.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361211}.
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DR   EMBL; KN728519; KIH63657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2DM19; -.
DR   Proteomes; UP000054047; Unassembled WGS sequence.
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   Gene3D; 3.40.630.30; -; 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   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Nucleus {ECO:0000256|RuleBase:RU361211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047}.
FT   DOMAIN          171..353
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
SQ   SEQUENCE   353 AA;  40558 MW;  13644F55A02B443C CRC64;
     MYTFAYYSIS FNDSVNSCFK SLVVLLFDFA SSVMGEPKAA ATNETERTAT RMDDVKINER
     VVVWRVVNGE RRRVLATLLK KRNRVPKSES NEVNGEKSEL ETNAPTCEVV FFFLNDSQSL
     KNRLEACFNF LDVIVAGGGD TRLTRKRRKN DDELVALDDA GGRGDQHRKP PPEKNIERVI
     FGGYEIQCWY YSPYRLKKKS VERLYVCENC LLYTDDVQMY ACHLAKDCER ASPPGVLIYE
     EGDVQIYEVF GALQKFYCQR LCLLAKLFID HKTLCFDVEN FIFYLLCEKD KDGAHIAAMF
     SKEMHSSNNL ACIMTLPCYQ RKGYGNLLIQ LSEFTREMLA VKSSTVILHI LRL
//
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