ID E4ZSL7_LEPMJ Unreviewed; 1321 AA.
AC E4ZSL7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=LEMA_P121610.1 {ECO:0000313|EMBL:CBX94397.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; FP929122; CBX94397.1; -; Genomic_DNA.
DR RefSeq; XP_003837841.1; XM_003837793.1.
DR STRING; 985895.E4ZSL7; -.
DR EnsemblFungi; CBX94397; CBX94397; LEMA_P121610.1.
DR GeneID; 13290953; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_005327_1_2_1; -.
DR InParanoid; E4ZSL7; -.
DR OMA; YWDLTIS; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000002668; Genome.
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; 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; PF16866; PHD_4; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 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:UP000002668};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00146}.
FT DOMAIN 263..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 632..909
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 150..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 808
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1321 AA; 145185 MW; 1BA8F7B680861C74 CRC64;
MGPLPSTSRI GCSRLWTSAI LRPRPLSTSL NYSMIAASPG RPEQFTVVAT GHLDLGHGNQ
ETRLQSRRTS NQGVLTHSSH RITTPRSYFH NQDAAATLAY FASKLAAVVS FAMAEPGRLM
GQTTSNPGPE DMDADGEYEM DHVEYGQAHA EEEGEEHHHH HTDAEGHTTD AEGSDIDAEG
EEVDEDEDEA EPVGAVKIAQ RRTHSSDGEV EYEDDDAPGE LLSDAPSHES DDDDSSSAES
EEENQWQAED DGGEEDEVAK SNPNACTYCN QDENDDPSPE FEEYLACVVC GDNAHQQCAR
DNHTLGPDDD AKQWRCTACI QNDLHANGDA EQEPEQPYTR RRLSSGNKLT KELLPSYRGV
DPGGHSIFKE LLLPDEPTDG PRSLRKRKNS HEEEPLPLRQ TRKKRRSSEL SPSAVQPSVA
ASSPRPSSRG VRAANSTMNG HESESKEDAA HSGSDQEGAR LRSSRARRGQ PKRSDKRPLA
WIEEQQGLSL IMAFHLNNEK VQKIVTAKPR KKTLTVEQER QERRRERDRE RRERNRRAAQ
AARESPEISH YPAIQVQASP FHGFIDREPD ETKSKPYGGV LSEADADTSK TYPSQSDRRR
FEDARTKAEE AWIEKQAALY PPEPSRPSKQ AATASKIKCV NFGGWEIDTW HAAPYPEEYS
KNRVLYICEF CLKYMNSDYV AWRHKLKCPA KHPPGDEIYR DRKYSFFEVD GRKNPVYCQN
LCLLAKLFLG SKTLYYDVEP FLFYVMTEND EYGCHFVGYF SKEKRPSSLN NVSCILVLPI
HMRKGYGQYL IEFSYLLTRV EKKTGSPEKP LSDMGLVSYR KYWRLVLCEE LLAQHGNVSN
ISISSLSERT GMTPDDIVSA LEGMRALVRD PVTKSYAFRL DIPYFKQYIE KCNAAGNQKI
NPDCLVWTPY VMGRLGQYED GPALQTVQQR DEVEEQDKPA PEEGVQIAST AKSKGKEKAR
SNNTDHTSPT PPTLSLETSL NGAATPPAPN TPLANGSTIA LAGSSHTPTS NDPALAIPPS
RYEIFPPIPG QPAPRRRPGR PFGSRRRTTS TPNRVRGTPS LAGTGAGHQT VQPVSRIRLT
PRGGAGNNAN GNGKASPTMG TRNAPLAAAG TPVRGSLRRT RSRLGESVTN GEEAGAGAAG
AGAGDEGGAV KAPGAGFASA AGAAAGRRSM RSSASSLGSP RDRARVSVVI GKARGAGAGT
GIEKGNTRAA AAMTATAHTN NNHHIGNHVP SNEHHDHDHD HDHNRDGEPE DDEDDDVDAE
YDEEEDDHFP AHSHSQTQNQ HLAHAHAHNA LDTHAHADED EDDDMDIDAE GEEDDDVVMA
G
//