ID A0A158R1K1_NIPBR Unreviewed; 674 AA.
AC A0A158R1K1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=NBR_LOCUS13926 {ECO:0000313|EMBL:VDL77515.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001392501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001392501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL77515.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107, ECO:0000256|RuleBase:RU361211}.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000256|ARBA:ARBA00009251}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYSL01021191; VDL77515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158R1K1; -.
DR STRING; 27835.A0A158R1K1; -.
DR WBParaSite; NBR_0001392501-mRNA-1; NBR_0001392501-mRNA-1; NBR_0001392501.
DR OMA; QDGMGQN; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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:0032422; F:purine-rich negative regulatory element binding; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
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; 2.30.30.140; -; 1.
DR Gene3D; 3.10.450.700; -; 1.
DR Gene3D; 3.30.2450.30; -; 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; IPR006628; PUR-bd_fam.
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:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF04845; PurA; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00712; PUR; 3.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361211};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 386..666
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 313..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 562
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 674 AA; 77517 MW; EBA35A2896EAD792 CRC64;
MSDGSVERAG SRRNEEELAS KQLNIQYKRY YVDVKQNNRG RFIKIAEMGS NYKSRLVLTM
SAAVQLCEQL SEMIKFSETL PEGAEATAEN GALKSEVLAF DSRRYYLDLK ENQRGRFLRI
AQTMANPRMS RAQIAIPAQG MVEMRDTLHE MLEKYSEGFL NDGNSTDATK TKQLTADNNK
TFYFDIGKND RGTFVRVTEV KQPAGYRTSI TIPQSALDKF RHLLDDVIED LAAPAAKAQL
LYEVAAPLFF ACVRALSLSC VYVPIFQRLV FPGDAEVLLV RNDPPRFYVH YIDCNRRLDE
WVPPENVNLE SLRMPQKGKK GGVAQSVEST SASGSPEREM SKKSAAMRKR KAANMDEDSQ
DGMGQNGAPS LRGSMSMVGH SEDALTRIRN IEMIELGRHR IQPWYFAPYP QQLVHLPCIY
ICEFCLKYVK SQTCLKTHMK KCYLKHPPGN EIYRNDQLSF FEIDGRKNKP YAQNLCLLAK
LFLDHKTLYY DTDPFLFYVL AYLDDRGFHI VGFFSKEKES AEEYNVACIL VLPPYQKMGY
GRLLIEFSYE LSKVEGKTGS PEKPLSDLGL LSYRSFWSAT IIEKLMQFKE EEMTSGEERT
ISVMDLSQMT SIRKEDVIST LQHLNLYKYY RGQYVIVITD DLKKAYQRMC EKITVRIDPT
KLRWQPKDWS RRKL
//
