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Database: UniProt
Entry: A0A165VMR2_9AGAM
LinkDB: A0A165VMR2_9AGAM
Original site: A0A165VMR2_9AGAM 
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
//
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