ID T1KSI0_TETUR Unreviewed; 735 AA.
AC T1KSI0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=107366746 {ECO:0000313|EnsemblMetazoa:tetur19g03210.1};
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:tetur19g03210.1, 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:tetur19g03210.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; CAEY01000425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015789864.1; XM_015934378.1.
DR AlphaFoldDB; T1KSI0; -.
DR STRING; 32264.T1KSI0; -.
DR EnsemblMetazoa; tetur19g03210.1; tetur19g03210.1; tetur19g03210.
DR GeneID; 107366746; -.
DR KEGG; tut:107366746; -.
DR eggNOG; KOG1512; Eukaryota.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_377370_0_0_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000015104; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 4.10.320.30; -; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF210; HISTONE ACETYLTRANSFERASE KAT7; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 69..127
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 453..727
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 130..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 629
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 735 AA; 84611 MW; A841FDB79579D6AE CRC64;
MPLRKRRKSR TSSESSGLGQ CFICLRQDSN ESLITCQLCA NQFHSVKCLR MLPNTVNRIR
SNQWSCPKCK SCEICGRKTR ALRSAAENNL LLCKGCDRGF HRNCIQTEDG INIEDEKNWH
CLNCEDDLSP LNENDSSDEV DENISESSDE DEDNKIEADE SDKSGEESAE IEPDEIDSEK
EDEEEDEEDE EEDDEEEEDG NEEDEDEDED EEDDDDESED DQYEGSDERP QPRLTRSKAA
AERSECDKNS EIQALHEETN IEDDSADSGS DKASKILPPK GKRGRKRKNG LTPSNLLTPK
KVKSEDENSR NEEEEAQCRV PGCDSKGHLS GKYSTHFTSS TCPVFHNLSH EECEDRYRNR
LRRKDARESN QKVSTRKSPY KDEKLNCLIE QRKKECNQIA NGPSIKKNNS SHSLTSREPE
LKSLAPIFDY EMFREAQSRA AELMQEQMKE NPPKKTGIKT IEMGKYEMDV WYSSPYPSDY
ACLPKLYICE FCLKYFNSSL TMKRHSLKCP LHCPPGNEIY RKANISVFEI DGEKNKLYCQ
NLCLLAKLFL DHKTLYYDVE PFRFYIMTES DNDGFHIIGY FSKEKNSFLN YNVSCILTLP
PYQKQGFGRM LIDFSYLLTR VEGKVGSPEK PLSDLGLISY RSYWKNVILE YLCNYQGSEI
SIKDLSHETA INAYDIVSTL QALGMLKYWK GKHLVLTRKD ILDDYKTKNK KRKNTKAIDP
SCLKWTPPNS SNSIK
//
