ID F8PYZ2_SERL3 Unreviewed; 1506 AA.
AC F8PYZ2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 08-NOV-2023, entry version 55.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=SERLA73DRAFT_160636 {ECO:0000313|EMBL:EGN99105.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
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DR EMBL; GL945480; EGN99105.1; -; Genomic_DNA.
DR STRING; 936435.F8PYZ2; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_001196_2_0_1; -.
DR InParanoid; F8PYZ2; -.
DR OMA; IECKNCE; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000008063; 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 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; IPR019786; Zinc_finger_PHD-type_CS.
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; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00249; PHD; 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; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
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 14..64
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 306..627
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 108..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1436..1463
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 108..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..300
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1506 AA; 169019 MW; F99BA32A51BFABEB CRC64;
MWTKRSYDWK CLECKNCEVC REKGDDERIL FCDFCDRGWH MDCLQPPLQE SPPGKWHCPY
CPPVDQCYPP IFDPQFLSSQ PETSNSSNIS PQPVYQTKMD VDVDIEGEDE EAEQQEEEEE
ETEEAEPEEE EDSTPVPQSK RKKKSSARKR ANEEVPSSPV VRPIKRMRIR VHSPAPPLVV
RLRIPPKGKG KEREDDEERK NIFDDFLSPN ERDTSKTTIE AYDKQRFEKS RLSAEEKLAP
PPLPPPPAVP EVPETPVAGP SSRPLRSGTV HQLIIPPAPP TPSPVPSTPS AFPSTPGFVP
PTPTSTNTLR IRTIRFGQFD IQTWYDAPFP EEYANIPDGR LWICEFCLKY MKSKFASSRH
RMKCKARHPP GDEIYRDGAV SIFEVDGRKN KIYCQNLCLL SRMFLDHKSL FYDVEPFLFY
VMTEVDDVGA RFVGYFSKEK RSPKDYNVSC IMTLPVRQRQ GWGGLLIDFS YLLSKKEQRS
GSPEKPLSGL GALGYKNYWT LAVMRYLATA PDDPHLEDIS KATSMTIEDI HVTLTQQNMI
FHREATPQPV RPTPGQSIKF PRGRKNGIAR KHLQRNQLQD EEGTKTPFSP PTHYDIRWDR
EKVKQYLEKW EVKGYLKLKP ERLKWTPFVL ARTKNVEVLQ TPTGEASGSV DGSTKTAVTP
AEDIGVGGNA TKFPIPATDA QNTEGMITQD TGAVNVTASP AARLFDDEPV IEVETPLPKK
HLRNHKPSGV ETPRTGFSRN HSNRLKVTNL RSATRRHTPS ALASALPVEA EQTAELIENG
AMEQGALTPA SQKRRRARVP RTKPLKSLTD REMSADVKRT TSPVLTPTSG LPRKRQRVES
PECESVAEET PIIVNGHNRD DGDDQGQPSV EHHCPIETLE PPSSAQSQPS IAENNREMEL
PPTVLTVSDA TPAPKGGMNG QVEQTEHVDV KSEDTGTPLT GSTSRHSVPS DDTVFMAEHV
NADNVGGKEG AVERERVEMA ERDEDGAAED VEETGRVLRV DEFGCGPEFT SSLVLLEEWR
KARGRERLRA VHWFARMDSQ THSDPGMSYS HIPLNDRRDQ SLQSSVNVSS LNQALGSHLT
PLGPRPPFPT HDTYRLSDSP PNIIDPTGSS QRAPVPGPPH SPIHDFSVPL QPDSQASALK
RKQGDVLGHP QLGGKRRRDE DMTDAFDSDG AHGAKHWSDE EKSKLFNWLM GPGEDDHWNA
LRATKNSCLR ECAADVFGGK KTYQALKGCY ERNFNLFKQI YAFEAFNLQI GNGPVNSINE
GDRLREFERR LQGARKAGCD VGNVHARTID HWHRSGWYNL FYRRWNGDPA TTRPIARPNH
TGTSVSGAGD DGEVDDEPPM DFTEPAQPHP ISHPQNGTPP QPLRYHPSEY SISDAVPLNI
PSRTLSTVSQ PSPSLSSADQ PIVNIAVPQN TISACVQLLQ LQSQYSKLKV EYMRRREERE
EKDSTLRREM DRLRQEREAA EWEHTKQTAS VKQKAQLATE LLANPSVDSS VRQAAGDYLK
RLFVTE
//
