ID A0A165VMR2_9AGAM Unreviewed; 1164 AA.
AC A0A165VMR2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=NEOLEDRAFT_1174884 {ECO:0000313|EMBL:KZT29906.1};
OS Neolentinus lepideus HHB14362 ss-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT29906.1, ECO:0000313|Proteomes:UP000076761};
RN [1] {ECO:0000313|EMBL:KZT29906.1, ECO:0000313|Proteomes:UP000076761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT29906.1,
RC ECO:0000313|Proteomes:UP000076761};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; KV425553; KZT29906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165VMR2; -.
DR STRING; 1314782.A0A165VMR2; -.
DR InParanoid; A0A165VMR2; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000076761; 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; cd15526; PHD1_MOZ_d4; 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; 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; IPR019787; Znf_PHD-finger.
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; PF00628; PHD; 2.
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 PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076761};
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 143..201
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 198..248
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 482..795
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 653
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1164 AA; 129208 MW; FDF81707A8BA1D6E CRC64;
MPGLPFPSNP VFARENSEFD HGASTPLSNV DDVPIDPALS EPPIDPAILV EGKDGVVERQ
RRVASRNVTI NNAFAWVSSM QPQEPLPKSS PEVSKRMPAP VHQYSLGPQG DPFAPPPPAY
FIPEEQPAPS SKPLKRKRKP RREPECGFCQ GDGSKNKNGE PERMVSCDEC GRSGHPTCMQ
LADISETIFS YPWKCMECKN CEICQEKGDD NRILFCDFCD RGWHMDCLDP PLDEEPPGKW
HCPLCPPLPP DSTQDVAMGE IPDYRESSIA STSHSGPDRK GKGKAVERAT QESDVEVEVD
GEGGVKVPKG RKRSSRKIKA RPRADADIYA EPSSVRSTSK RMRIKIPTSP VRTPTQRKMV
VRLKLPTRDK GKEKEDSDPE SPKGLFDEVL RPEERDTSRT SIEAGDKIRF DRSRTWSEAK
LNPLPLSASE DPQTPVAGPS SRPLRSAMQY RSMAISIPSP GPSASPAPST PAPDSAKIDS
SSRPLRIRTI RFGEYDIQTW YDAPFPEEYA NIPDGRLWIC EFCLKYMRSR FQAVRHATKC
KARHPPGDEI YRDGFVSIFE IYCQNLCLLS KMFLDHKSLF YDVEPFLFYV ITEVDELGAR
FVGYFSKEKH SPKDYNVSCI MTLPVRQRKG WGNLLIDFSY LLSKKERRAG SPEKPLSSLG
ALSYKNYWTL AVMQYLNIAP HDPKLEDISS ATSMTVEDIY NTLVQQNMIT AKEHTPSSRP
APGQSIKFPR GRKNGVARRH LQRPQTQDEE KPRGPFTPPR DYTIHWDPEE VQQYLMNWES
KGYLRLKPEK LKWSPFLMTR ARRSQILGSG MGTKTEMAPL VDPLTAKSQP PDVDLDVSVF
GEGPSTPRRG RHNDLQRDLA RTDSPAAALF DADEEVIDAR SGMVTPSNPS LAAQASSSPV
PSDDEDSLNR GVRTLALSNT RSIRTRSNRS QSLRNTVSVS PTLSRTRSAP AKIAKVRKDL
DEQPNTLNDE ALAAQLAREG FRQLRSRSAA VVPLLAENDR KRGTPTTTPR AISPRKRRRV
ESSPEFDLLL PSTPLNGQSS SSRLLAPRPR TATHSSRLLA GNDTIAEEDT TALQILASAA
NGAGAEQHLN GDVKAEDIST PSTAVASRHS VPSEDTTVES DSLVKVKVVQ QDVVMADGTT
SDMDAEGEED ADEDAEGEPD DEAL
//