ID A0A0V1LVD9_9BILA Unreviewed; 1499 AA.
AC A0A0V1LVD9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=Kat7 {ECO:0000313|EMBL:KRZ63491.1};
GN ORFNames=T02_15550 {ECO:0000313|EMBL:KRZ63491.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ63491.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ63491.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ63491.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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:KRZ63491.1}.
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DR EMBL; JYDW01000001; KRZ63491.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LVD9; -.
DR Proteomes; UP000054721; 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:0003676; F:nucleic acid binding; IEA:InterPro.
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; 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; IPR005312; DUF1759.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR008737; Peptidase_asp_put.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF05585; DUF1758; 1.
DR Pfam; PF03564; DUF1759; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF103637; CCHHC domain; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
DR PROSITE; PS51802; ZF_CCHHC; 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:UP000054721};
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:PRU00047}.
FT DOMAIN 509..523
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1227..1499
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 212..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1404
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1499 AA; 166524 MW; B765C65ED71E4FBB CRC64;
MPKIRKNGKE LANLKPLKTE SYISSSRAVI GKCPYPKCTG AGHLSGKFDT HLFIEACPLK
QKLTPETCVL FAKYRDLLKS SISKNDDVIH SHLPDDRTPS KLYLSIASVQ NPATVLYIGP
PSRIRQASPN GYSKLAANKV RLNCLLTELE ELSIDAVDDN LLGGQLELTE ALFRETDALQ
AEWEQDLEAG ERNAATEDWA KSRRRFLEAR ARAQGRLRPK QENGPSRGDG GNSGNSRQTA
APARIGNLPE LTLPQFDGEV LEFPTFWAQF EASVHANTEL DDATKFAYLL SNTTGRALGA
IAGIPITAAN YPQAVGILQK RFGRPKIVAR AHLLALWKAP ECREMTRQGI QTLVDEITKQ
LRCLAAMGKD PHAGELPWSE ALMPGLKEKF PRKLQRAWDL KVGSGTESED NLDNFLEFAQ
LQADSLSPPD EFSPEASSQG ERSEATRKDS NSAERKGRDR VTSSAAALVA SIQRVCPFCE
GDHDATGCQR FLDAEHSART RMSREKGVCY KCLKIGHRAR ECRTGPPCGV DGCHQPHHQL
LHPPATREPP RSLGPDQFHQ SLLAARNTPG GGLQTIRARA YGPDGSHVVV NCLFDTGSQV
SFIRKDVAEV LGLTGSHERC RFTTLGGRVG PVRRWRRVEF RLVAVESSGR PLTSTLIRAL
AIPRVCGKVQ PVPGERSDGA PAGTKPEMAQ RRKTPLMIDV LIGIDYYYEF VTGRMRRRAT
GGPVALETLL GWGVCGRTSP RRTAEVESFP TNPENSAVTL LRKNGEIDEV EILPEEDVPE
QNKEAREERE QTSTSGAAKR RISFSRRFGQ RGLSNVAKRT RRQLAVVERD LKVGRSKPLY
HAAAGRQHSE KDRAKPTPET GPLRRISLPT PHPGTAVGNP ATMGSRDAAP KKRATENPCR
LGPEWPAEPP QAKQRSHEDS GRTTWSPQRG KSPQGQSTLT APPRDPGIHR SRGMRRGCCE
SACTVSAPNS EAADGKKEPG HAGVHESPSS TAREARVDRD TDPSQTLGSA AHRGISDASR
DRATRLDPSR VHEAPGSMLR AAEAQKAQMA GSPMSNDRPV HTRTPTLGAR LVLPSATDGH
MVGPSTNAPT WNRKENRRRV HRKPGAVAEL STGREEIDGM RRCPPGKPVS ERNNTDLVGV
TWPGAGGRMS RVGRGQYPHT VGQIVISAYG SPCWGQRDPK ENRRKSTFEA GLRSLKQILR
DLKDVLYLES LADTAEFLEH EPNFRQPYSR KVEKIQLYDV EFTLPKNAVC IYPNCEVSCV
YVCERCFQYF FDKYAMQDHC LNVFPYEYPP GKLIYKEDSL LVYEVDGLKE SVYSMNLTMF
AKMFIPGKEY RSDVDIFKFY ILIKNDAIGW HTVGYFSKAK DSDSKHSLSC IMVMPTYGKQ
GYGGFLIDLS YILCKKENKI GTPERPFSID GLMAYRRYWL RIIVDYMVQK GTKRQFDIVE
LSKSTAVQEI DIVTTLFAYD MITKSTEKYW VVMSETFRKA YGKLYFGERS CRVNSACFV
//
