GenomeNet

Database: UniProt/TrEMBL
Entry: T1L0F9_TETUR
LinkDB: T1L0F9_TETUR
Original site: T1L0F9_TETUR 
ID   T1L0F9_TETUR            Unreviewed;       465 AA.
AC   T1L0F9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   Name=107369145 {ECO:0000313|EnsemblMetazoa:tetur30g00500.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur30g00500.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur30g00500.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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}.
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; CAEY01000863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015792553.1; XM_015937067.1.
DR   AlphaFoldDB; T1L0F9; -.
DR   STRING; 32264.T1L0F9; -.
DR   EnsemblMetazoa; tetur30g00500.1; tetur30g00500.1; tetur30g00500.
DR   GeneID; 107369145; -.
DR   KEGG; tut:107369145; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_1_1; -.
DR   OMA; ILCEVDK; -.
DR   OrthoDB; 118560at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
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; IPR000953; Chromo/chromo_shadow_dom.
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; 1.
DR   Pfam; PF11717; Tudor-knot; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SMART; SM00298; CHROMO; 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   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          184..457
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        360
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   465 AA;  53567 MW;  9F8A5DF263D0F07D CRC64;
     MTDNVSNASP SSDNATSDSR DSFKSGGEND LSNGNSQSNS SDNNKGEYKE NEDIVLDIGD
     HFLVRRSDNT WHSAEVIEVR SNPQEGGRYE YYVHYEGLNR RLDEWVGRDR VDISSGSRAK
     AEADARAAKE SAVITPQITD DGKPERKITR NQKRKHDEIN HVQKTFAEMD PTTAALEREH
     EAITKVKYVD KIQFGKYEID AWYFSPFPED YGKQPKLWIC EYCIKYMKLE KTYRYHQATC
     SWRQPPGKEI YRKGTISVYE VDGREHKIYA QNLCLLAKLF LDHKTLFFDV EPFLFYILCE
     VDNQGAHLVG YFSKEKESPD GNNLACILTL PPYQRKGYGK FLIAFSYEVS KLENVIGSPE
     KPLSDLGKLS YRSYWSFVLL EILRDFRGTL SIRDLSQMTS ITQSDIISTL QSLNMVKYWK
     GQHVICVTSK LVEEHLKSAQ YKKPRLTVDV SCLRWAPPKK TVKKK
//
DBGET integrated database retrieval system