ID A0A136IZT2_9PEZI Unreviewed; 670 AA.
AC A0A136IZT2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acyl-CoA N-acyltransferase {ECO:0000313|EMBL:KXJ90309.1};
GN ORFNames=Micbo1qcDRAFT_149207 {ECO:0000313|EMBL:KXJ90309.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ90309.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ964253; KXJ90309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136IZT2; -.
DR STRING; 196109.A0A136IZT2; -.
DR InParanoid; A0A136IZT2; -.
DR OrthoDB; 118560at2759; -.
DR Proteomes; UP000070501; Unassembled WGS sequence.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:InterPro.
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 InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF180; HISTONE ACETYLTRANSFERASE SAS2; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KXJ90309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW Transferase {ECO:0000313|EMBL:KXJ90309.1}.
FT DOMAIN 231..593
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 1..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 501
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 670 AA; 74359 MW; C8E47CE740A4EC8D CRC64;
MAVPKRKKLH DDRPPTEGTS TRRATRQHPT TATTDEPPKQ LRSGRTRAET LEPAPKPARI
KRKSDASVEE PRPPSREEPR RTAIPPPAIP SSPEETARTR RIPATQAPPK PTRQGRQRDS
AAAPGSPPPK RANVVPTETP ISPPKYPLQL EPRQPSLTSP RLPHAKTQGA VQTRVLPPPP
ILPQQSRPRH EQVSTGETLS GPAANTSAAI ASIKTTPKRQ ARPLRPPATP GPDRNIDKVF
LGNICFRAWY PSYYPKEVLA DPAGTKDGQH PREVGKVGGG KHTAPQPILD RLLVCPCCFK
YSRELAIWWE HVRYCERKCH VPGRKVYTHP RTGARQPKSQ GSAKSRRRGH EHANVQDDEH
ELSFSDTDNQ GEWSVWEVDG EKDGLFCQNL SLFAKLFLDN KSVFFDVTGF NYFLLVYTPK
DSNEDVQGAD NPASTSKDPH HRVQSRPQVV GFFSKEKVSW DNNNLACILV FPPWQRKGLG
SLLMGVSYAI SRREGVLGGP EKPISELGRK GYNRFWAAEV ARWLLSLPAS APRAEKRRAV
KDDKADLEVL VDVIDCSNAT WIVPEDCLQV LRDMGLLEEA GLGPQKDAQH RTSSNTDSAD
TKVQSAGDHT HHASGAVADG EAEKVMVPRV RLDKAAVQKW VEDHRINLER TCDPDGFVPG
YAIRDAMEVD
//