ID K3VN79_FUSPC Unreviewed; 1103 AA.
AC K3VN79;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN ORFNames=FPSE_04641 {ECO:0000313|EMBL:EKJ75168.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ75168.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ75168.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ75168.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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:EKJ75168.1}.
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DR EMBL; AFNW01000095; EKJ75168.1; -; Genomic_DNA.
DR RefSeq; XP_009256034.1; XM_009257759.1.
DR AlphaFoldDB; K3VN79; -.
DR EnsemblFungi; EKJ75168; EKJ75168; FPSE_04641.
DR GeneID; 20363259; -.
DR KEGG; fpu:FPSE_04641; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_005327_1_2_1; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000007978; Chromosome 2.
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; 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; PF16866; PHD_4; 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; 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:UP000007978};
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 194..253
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 532..813
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 708
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1103 AA; 122169 MW; 0FFC21172C00785E CRC64;
MEEDRQQGVM ASDEDAEYET AGEAGGHTTI IATGSREDER VSSVDRDPSD NGDIELSDRD
ASGEDVDASG EEDNEYTAPP QLSSHNSRQT DQEEQDEAGE EAEAGDAEEE HDDADADAEG
DEDVDAEGEE YEDDEGVGAV KFQPGTRNHD DDEDSESDKS DFPSANEEES DEEAAWDDAA
EAEEDHDDEE TAAPSHCVFC NQSEDDDPSE EFETYLACTR CGNNAHQQCA RDVAAMSTEN
TPDHWKCPDC FGRESDAEGE DEEMEDHDVE DDAGLPSQQS EIPELSGEAH FDQRMEDEDA
SSHHESQHED DDGLDEGLRE QPRTLRKRKS SSLEVDGNTI SLRKRRRNQS NDAASEGTAR
NGSAEPGRHN PSRTLRLKVT RPPPVTIKKH TRTSLVLKLQ VKPGNLKEVL GRKKRETRRQ
PGTITRPPPQ RPVPTPRATA IAAISVLPTP FTSDNYSQPL YFDCDLDEMQ GKPYGGILSE
GEADTSKTLP AEEDENRFKD ALQKADEEWR ARLLAMQEES NVPIRKAKKT ADNASHIECI
EFGGWEIDTW YAAPYPAEYC TTRVLYICEF CLKYMASDYV AWRHKLKCPA KHPPGDEIYR
HGSVSVFEVD GRKNPVYCQN LCLLAKLFLG SKTLYYDVEP FLFYVLCEYN ETGYHFVGYF
SKEKRASSQN NVSCILTLPI HQRKGYGNLL IDFSYLLTKV EEKTGSPEKP LSDMGLVSYR
NYWRLVMCRY FLTAMKEEKY ATEGLSIKRI SDNTGMTPDD VISALEGLRA LVRDPQTKTY
AFRVDLDYCR QYVGKWEAKG YVQLKPEALV WTPYVMGRSN AVNFELGPPI NTIAPREDDE
AKVDEGLGAA GTGGQTLING QKNEEDAAGL NIDTGAETEA NVNGEAQDDE VETDNAEPAP
VQSIEDVAPG QEKDKDVEME DAESDGPPAW LKPYQDIPYT RFEVFPAIPG GRRERARPSV
NRPTVPRTTS SAPRQKRSSG SHRTSSSRPK SASKKKTGGT GRGPGRWPKG TKKSDYGNAT
SGPGLPPGWQ DKQVKLRAIT EGNDPDQEVA VEEPAEDSVV VSMRANGTKV NNRNAATRKA
SVADANGEQA GEGEDVDAEG EDI
//
