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Database: UniProt
Entry: T1KUQ3_TETUR
LinkDB: T1KUQ3_TETUR
Original site: T1KUQ3_TETUR 
ID   T1KUQ3_TETUR            Unreviewed;       524 AA.
AC   T1KUQ3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=107367519 {ECO:0000313|EnsemblMetazoa:tetur22g00860.1};
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:tetur22g00860.1, 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:tetur22g00860.1}
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}.
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DR   EMBL; CAEY01000578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015790710.1; XM_015935224.1.
DR   AlphaFoldDB; T1KUQ3; -.
DR   STRING; 32264.T1KUQ3; -.
DR   EnsemblMetazoa; tetur22g00860.1; tetur22g00860.1; tetur22g00860.
DR   GeneID; 107367519; -.
DR   KEGG; tut:107367519; -.
DR   eggNOG; KOG2747; Eukaryota.
DR   HOGENOM; CLU_011815_2_0_1; -.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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:SF161; HISTONE ACETYLTRANSFERASE KAT5; 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   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:UP000015104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          237..515
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51726"
FT   REGION          182..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        413
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ   SEQUENCE   524 AA;  60435 MW;  200A0FAEF08F1122 CRC64;
     MKPGANLKLP DKMIDVTEGC LVPVRMKFTN EWHMGEVISI KNSENGDNLY YVHFIDFNKR
     LDEWVTKDRM NLEKIHLPTR EEAALKLQEM PISPDDRITT TEVEEVQRNN NSLNNTLNNT
     LNNNLNNNLN NNLNITISNN LSNNLNNNLN NNLNNSINNS INNSINNSIN CPPISPVNKF
     VLGPKKGRGR KRKLPSFTSQ SENPDHSPNL WAGGSGAVVA PRTNGSLSSH NPDDILTRIR
     NIDLIEIGQH RIKPWYFSPY PQRLTSLPCI YLCEYCLKYV KSRTCLIRHF TKCKLRHPPG
     NEIYRKGTIS FFEIDGRSNR IYAQNLCLLA KCFLDHKTLY YDTDPFLFYI MTETDDRGCH
     IVGYFSKEKV SSEDYNVACI LTLPPYQRKG YGKIMIEFSY ELSKFEGKTG SPEKPLSDLG
     LLSYRSYWAE TILELIINLK TPEGSIRPQI SINEISEMTS IKKEDVISTL QFLNMINYYK
     GEYIITLSKE VIASFERISK KRRLRIDPGC LHWTPRDWTK RGKW
//
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