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Database: UniProt
Entry: M2UBV0_COCH5
LinkDB: M2UBV0_COCH5
Original site: M2UBV0_COCH5 
ID   M2UBV0_COCH5            Unreviewed;       238 AA.
AC   M2UBV0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE            EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
GN   ORFNames=COCHEDRAFT_1103859 {ECO:0000313|EMBL:EMD91181.1};
OS   Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD91181.1, ECO:0000313|Proteomes:UP000016936};
RN   [1] {ECO:0000313|EMBL:EMD91181.1, ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000016936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) +
CC         N-terminal N(alpha)-acetyl-L-seryl-[histone H2A];
CC         Xref=Rhea:RHEA:50600, Rhea:RHEA-COMP:12742, Rhea:RHEA-COMP:12744,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00000345};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N-terminal L-seryl-[histone H4] = CoA + H(+) + N-
CC         terminal N(alpha)-acetyl-L-seryl-[histone H4]; Xref=Rhea:RHEA:50596,
CC         Rhea:RHEA-COMP:12740, Rhea:RHEA-COMP:12743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738,
CC         ChEBI:CHEBI:83690; EC=2.3.1.257;
CC         Evidence={ECO:0000256|ARBA:ARBA00001388};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008870}.
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DR   EMBL; KB445577; EMD91181.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2UBV0; -.
DR   STRING; 701091.M2UBV0; -.
DR   eggNOG; KOG2488; Eukaryota.
DR   HOGENOM; CLU_051699_2_1_1; -.
DR   OMA; ETNVGPY; -.
DR   Proteomes; UP000016936; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043998; F:histone H2A acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0010485; F:histone H4 acetyltransferase activity; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039949; NAA40.
DR   PANTHER; PTHR20531; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   PANTHER; PTHR20531:SF1; N-ALPHA-ACETYLTRANSFERASE 40; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016936};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          74..238
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   238 AA;  27279 MW;  CC5859C92FB3E371 CRC64;
     MPHVVQRTLI VKTLFEDKLV GFKSYESPNQ PFPLSFDLVT SGTQLKEEDL QACIELVEQT
     SGDDYRASRI GWNTRKKREE MMDKDMIYLL RRKLDPSSPQ HVQPDDLEQL AQTYTSISTP
     TPPPPPASPN PPILGFISFM FTWDDPPHQD RPVVYIYEIH LSPPLRHQGL GSRLMTFVEA
     VARACSIGKT MLTVFVANEG AKKMYEKLGY QRDECSPVDR VMRRKVVKAE YVIMSKKM
//
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