ID A0A2A2LYV5_9BILA Unreviewed; 1010 AA.
AC A0A2A2LYV5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=WR25_12626 {ECO:0000313|EMBL:PAV91369.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV91369.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV91369.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV91369.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV91369.1}.
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DR EMBL; LIAE01006322; PAV91369.1; -; Genomic_DNA.
DR EMBL; LIAE01006322; PAV91374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2LYV5; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
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 CDD; cd15489; PHD_SF; 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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
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; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 398..687
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 592
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1010 AA; 116272 MW; 192EF9236FE313B9 CRC64;
MVASRRSAGS LAAVGRRSLL SAPSARSAQP TQTQAQAARR VKSPGTSSPA SRTRHSLAEQ
GHKSLRTPRE QQQQRASRVS GAARSTSADA SSKPKSVQRK ESIQKKKEPV RVKQEEPQPA
QASNDDDKIK TRRLHKTVVE KMPRCTICKQ PKPELYACSG CGLYYHLRKC YRLPERQVAN
VFASKHWFCA KCVRCQACNE MIDDPSNVEC VQCGLVWHGR CRPQKGSSID GQWACAKCTR
KEKTDKPGAG NSNKKKDARL EAKKDVYDFD GDDTAMFAPD FTLRKMDQSS PGSLLGSVKQ
EELGSSSDNS KKKGKPSKSD SRKRKMVDKQ QQDVLNDEKR LILDARSEIY DELLDAHNRR
VQTEGSGARK SASRSPTKSP EKKSRRLVLQ EDKDLFMSTL KEYQSIKREA VPAATSSTID
KWVYLGGTQK MKAIYESPYP EEIRRAPAIY VCAFCLTAQE DKERYRIHQS NCEFRHPPGN
EIYRDSEISF FEIDGSKQQW YCRNLCLLAK LFISSKTLHH EVDTFFFYVL TEHTEEGCQL
VGYFSKEKNP SKNNNLSCLL TLPTSQRSGY GRLLIDMSYE LSRVERKVGS PEHPLSDLGL
LTYRGYWRSS ILCYLRAIRQ NPHTSIKDMS LQTRIHPTDI INQLMHDRLL VYKHGVYYIK
AAKRAYKWPL STCRRRTVDS SKLQWKPSFD ETQLDPSRLN YYNVKLVCKK FNNIVSNEQW
WRVQINRKKY YLTHTEANDP KFLAVRTFEN IRKEERRWLH DNENVVQQFT EPCASTIDGV
RLFRTKDPDL RRFCLAGCRD RSLTLWHLQD IENPNDTLPV CLQKIDGAHD GWIWRIDKVT
EEGKFMTCGW DQICKEWQIG ENGMITELSK YELPSAATCS ARITPHQFIV GTFNHTIHLF
DTREPPKKYG NQFDLHKRAI IGLENKDHYI YTTSEDRHIF MSDIRMTSPK AINDKILRVY
APSLSLNANQ LICGYGNRIR IMDPLTLDTV HEFVVTFISI FQRRLYFQGT
//
