ID C6LNH5_GIAIB Unreviewed; 418 AA.
AC C6LNH5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Histone acetyltransferase {ECO:0000256|RuleBase:RU361211};
DE EC=2.3.1.48 {ECO:0000256|RuleBase:RU361211};
GN ORFNames=GL50581_279 {ECO:0000313|EMBL:EET02441.1};
OS Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=598745 {ECO:0000313|EMBL:EET02441.1, ECO:0000313|Proteomes:UP000002488};
RN [1] {ECO:0000313|EMBL:EET02441.1, ECO:0000313|Proteomes:UP000002488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT is human giardiasis caused by two different species?";
RL PLoS Pathog. 5:E1000560-E1000560(2009).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EET02441.1}.
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DR EMBL; ACGJ01000415; EET02441.1; -; Genomic_DNA.
DR AlphaFoldDB; C6LNH5; -.
DR EnsemblProtists; EET02441; EET02441; GL50581_279.
DR VEuPathDB; GiardiaDB:GL50581_279; -.
DR OMA; KLHWIPY; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000002488; 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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR016197; Chromo-like_dom_sf.
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; 2.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|RuleBase:RU361211};
KW Transferase {ECO:0000313|EMBL:EET02441.1}.
FT DOMAIN 97..409
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 418 AA; 49057 MW; 8B70CF2416E06BD6 CRC64;
MAAKEPAEPY KKGLIFMACC REDVGTSLES TPRPVRIYDS REDPTTRGSY EYYVYFGGYN
ARLADWYPSS ALRSITDEER QLYAKEIGFF SQADKEFLPR NIDKVVISQY VMCPWYFSPL
PEEFFASRAV YICEYCFTML TTEQIYKRHI ARCTCRSPPG DLIYRDSEVC FFEINGSEHS
NYCRNICLVA RLFLQHKTLV ADVDVFLFYV MFAKTNSKRA SQAHKTPAEQ EQGVQREPEI
KRMPNQQKLE EHDDDSYHFV GFFSKEKQQE NSLSCIVALP CFQKKGYGNM MIDFSYMLSS
RECRLGGPEM PLSDLGLMSY LSYWKRRICE VLVRNTTSEI SLFEISKQTM ISYRNLIMAM
NKYGLLKETP SNTAIYFRDE MADELRACLE KEEKRGVHRL EDKYLHWVPY VNMCYEYK
//
