ID A0A1I8CFN8_9BILA Unreviewed; 568 AA.
AC A0A1I8CFN8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000384200.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000384200.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000384200.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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 AlphaFoldDB; A0A1I8CFN8; -.
DR WBParaSite; RSKR_0000384200.1; RSKR_0000384200.1; RSKR_0000384200.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF102; HISTONE ACETYLTRANSFERASE; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 277..531
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 138..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 456
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 568 AA; 64452 MW; 76316ECB9AB29294 CRC64;
MSSLILSPKA KRKRLGQSLS THQRCKKCAK VLDEDTIDEG VIECVTCAEV YHKVCQGLEG
LSSQFFSIPK NKSVFKCNRC QSCAGCNKFI VDPLNIECKR CRITYCGPCS LPKRINGFLP
NWTCSDCEKA LKHSNHKAIG TPKKNQNGQY SQNSQNSQNS PGKARNISKK SGSKSHHKLL
SSDASDSYDE IDKAERAFAV KIQNKLENRQ TFDVLMHTDP ILTEAIFKLK GGHESMSHQS
FSEASKERLM KQLSKTPATI LYSNIKEATK DKMALKTAEE GKSKLHYHGY TMEAQFESKY
PDDIKNAADI FVCRFCLLPF ASTGPFEFHI KQCTRKHPPG NEIYRDSEKR MISVFELSGE
NETAYCRRIC WLASLFIPHK VTVNHVHLFK FYILTEISEA GFTPVGYFSK EHKPASNNNL
SCILTFPHRM GLGYGQLLID LSYKLSLREK KIGSPEHPLS DNGLIAYRKY WKSVILCHLR
QKYLNKETTI SFNNLSKMTG ISIDDLISTC LSLNIIGYTK IVDTYLIDLG PALDASLKDL
RRNVIEDKKL IWVFPFESSE TEFGRYDN
//
