ID Q8SQM1_ENCCU Unreviewed; 288 AA.
AC Q8SQM1;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 110.
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};
GN OrderedLocusNames=ECU09_1310 {ECO:0000313|EMBL:CAD27102.1};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD27102.1, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD27102.1, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD27102.1,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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 EMBL; AL590451; CAD27102.1; -; Genomic_DNA.
DR RefSeq; XP_955683.1; XM_950590.1.
DR AlphaFoldDB; Q8SQM1; -.
DR STRING; 284813.Q8SQM1; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_1310; -.
DR HOGENOM; CLU_011815_0_4_1; -.
DR InParanoid; Q8SQM1; -.
DR OMA; LDNKSMY; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
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; 3.40.630.30; -; 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; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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 Reference proteome {ECO:0000313|Proteomes:UP000000819};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..277
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT ACT_SITE 205
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 288 AA; 32848 MW; 795909244E50A8E6 CRC64;
MDFDSEEMDL LGNDPEFMEY RRAMEKDHKA TDATPQMEFV KRNVEVTQAV FGDELLGFRN
RVWLFSDKNV VYICDRCLHQ YWDSTSLGRH RKECSQGIPG RHVYTDKDEG ISVIEIDGGC
ESVLCRRICT IGRAFIHRKT LHLDVDGYLF YVLLIGGRVA GFFSKEKESE KHNLSCLLVL
PPHRSRGYGS LMIDLSYILG PGTPEKPLSK EGRAVYKRYW RNMVLKTLRK MGGEEMSICS
ISAESGLSID DTIHGLELLG INPESHIYDV SGKVPVPLRE CKKNCLIF
//