NAA40_SCHPO
ID NAA40_SCHPO Reviewed; 204 AA.
AC Q9USH6;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=N-alpha-acetyltransferase 40 {ECO:0000312|PomBase:SPCC825.04c};
DE EC=2.3.1.257 {ECO:0000250|UniProtKB:Q04751, ECO:0000250|UniProtKB:Q86UY6};
GN Name=naa40 {ECO:0000312|PomBase:SPCC825.04c}; ORFNames=SPCC825.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3] {ECO:0000312|PDB:4UA3}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 13-204 IN COMPLEX WITH
RP ACETYL-COA.
RX PubMed=25619998; DOI=10.1016/j.str.2014.10.025;
RA Magin R.S., Liszczak G.P., Marmorstein R.;
RT "The molecular basis for histone H4- and H2A-specific amino-terminal
RT acetylation by NatD.";
RL Structure 23:332-341(2015).
CC -!- FUNCTION: N-alpha-acetyltransferase that specifically mediates the
CC acetylation of the N-terminal residues of histones H4 and H2A.
CC {ECO:0000250|UniProtKB:Q04751, ECO:0000250|UniProtKB:Q86UY6}.
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:0000250|UniProtKB:Q04751,
CC ECO:0000250|UniProtKB:Q86UY6};
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:0000250|UniProtKB:Q04751,
CC ECO:0000250|UniProtKB:Q86UY6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. NAA40 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAB58412.1; -; Genomic_DNA.
DR PIR; T41625; T41625.
DR RefSeq; NP_588054.1; NM_001023046.2.
DR PDB; 4UA3; X-ray; 1.85 A; A/B=13-204.
DR PDBsum; 4UA3; -.
DR AlphaFoldDB; Q9USH6; -.
DR SMR; Q9USH6; -.
DR BioGRID; 276011; 11.
DR STRING; 4896.SPCC825.04c.1; -.
DR MaxQB; Q9USH6; -.
DR PaxDb; Q9USH6; -.
DR EnsemblFungi; SPCC825.04c.1; SPCC825.04c.1:pep; SPCC825.04c.
DR GeneID; 2539448; -.
DR KEGG; spo:SPCC825.04c; -.
DR PomBase; SPCC825.04c; naa40.
DR VEuPathDB; FungiDB:SPCC825.04c; -.
DR eggNOG; KOG2488; Eukaryota.
DR HOGENOM; CLU_051699_2_2_1; -.
DR InParanoid; Q9USH6; -.
DR OMA; RALNWYK; -.
DR PhylomeDB; Q9USH6; -.
DR PRO; PR:Q9USH6; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990189; F:peptide-serine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IC:PomBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR039949; NAA40.
DR PANTHER; PTHR20531; PTHR20531; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..204
FT /note="N-alpha-acetyltransferase 40"
FT /id="PRO_0000310299"
FT DOMAIN 39..202
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 120..122
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:25619998,
FT ECO:0000312|PDB:4UA3"
FT BINDING 128..133
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:25619998,
FT ECO:0000312|PDB:4UA3"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT BINDING 159
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:25619998,
FT ECO:0000312|PDB:4UA3"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT SITE 119
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q86UY6"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:4UA3"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:4UA3"
FT HELIX 46..66
FT /evidence="ECO:0007829|PDB:4UA3"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:4UA3"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:4UA3"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4UA3"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:4UA3"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:4UA3"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:4UA3"
SQ SEQUENCE 204 AA; 24561 MW; 31465DC4BC2B151B CRC64;
MHFLKQYLFY SPRRMKTQEI KNVTLEDVDF LKNLGVWVEI YHHLEKGLLQ QCFNLVKKNM
EALYRQSSFG WDDSEKLKEM EMEKLEYICI FEKTSKKLVG FLSFEDTVEA GLTCLYIYEI
QLDEHIRGRN VGKWLLKNAS ILAYRRNLKY IFLTVFSANL NALNFYHHFD FVPHESSPQE
KKFRSGKVIH PDYYILYTKS RKDW
