ID A0A0P1BCQ8_9BASI Unreviewed; 287 AA.
AC A0A0P1BCQ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000256|ARBA:ARBA00015043};
DE EC=2.3.1.257 {ECO:0000256|ARBA:ARBA00012950};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH13497.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH13497.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000221; CEH13497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BCQ8; -.
DR STRING; 401625.A0A0P1BCQ8; -.
DR OrthoDB; 2047206at2759; -.
DR Proteomes; UP000054845; 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:UP000054845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEH13497.1}.
FT DOMAIN 103..268
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 287 AA; 32257 MW; CDB17231154200AE CRC64;
MPSHGRLSAR GKAAGADGFS APPALLSAKQ VAARAQKIAA AQLLELLDHE RLRNDAQNGA
LSDESTVSRE NRSDRMSRTL KIANAEYTLL VATTAGLSNA EKEEVFALFQ ANMQSHYERS
TQGWAPAEKR TEIFHHQSRF LILVEGAQSS VTRPAAFAVW RFDTEECDPS DPAQRHRPGR
RREEEIEVAY CYEVQVSLPH RKHGLGRFLM QQLEHIACKT RMRKVMLTVF SNNLEAKAFY
KKIGYWTDSI SPSQWSTESA TPLDQKGDNE TEYDYDILSK SVVPSTQ
//
