NAA30_SCHPO
ID NAA30_SCHPO Reviewed; 150 AA.
AC O74311;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=N-alpha-acetyltransferase 30;
DE EC=2.3.1.256 {ECO:0000250|UniProtKB:Q147X3};
DE AltName: Full=N-terminal acetyltransferase C complex catalytic subunit mak3 homolog;
DE AltName: Full=NatC catalytic subunit;
GN Name=naa30; Synonyms=mak3; ORFNames=SPBC15D4.06;
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).
CC -!- FUNCTION: Catalytic component of the NatC N-terminal acetyltransferase.
CC {ECO:0000250|UniProtKB:Q03503}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-leucyl-[protein] = CoA +
CC H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-leucyl-[protein];
CC Xref=Rhea:RHEA:50520, Rhea:RHEA-COMP:12711, Rhea:RHEA-COMP:12712,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133377, ChEBI:CHEBI:133378; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-isoleucyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-isoleucyl-
CC [protein]; Xref=Rhea:RHEA:50524, Rhea:RHEA-COMP:12713, Rhea:RHEA-
CC COMP:12714, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133379, ChEBI:CHEBI:133380; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-phenylalanyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-phenylalanyl-
CC [protein]; Xref=Rhea:RHEA:50528, Rhea:RHEA-COMP:12715, Rhea:RHEA-
CC COMP:12716, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133382, ChEBI:CHEBI:133383; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tryptophyl-[protein] =
CC CoA + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tryptophyl-
CC [protein]; Xref=Rhea:RHEA:50560, Rhea:RHEA-COMP:12724, Rhea:RHEA-
CC COMP:12725, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133386, ChEBI:CHEBI:133387; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N-terminal L-methionyl-L-tyrosyl-[protein] = CoA
CC + H(+) + N-terminal N(alpha)-acetyl-L-methionyl-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:50532, Rhea:RHEA-COMP:12717, Rhea:RHEA-COMP:12718,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:133384, ChEBI:CHEBI:133385; EC=2.3.1.256;
CC Evidence={ECO:0000250|UniProtKB:Q147X3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. MAK3 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA20481.1; -; Genomic_DNA.
DR PIR; T39482; T39482.
DR RefSeq; NP_596246.1; NM_001022165.2.
DR PDB; 7L1K; EM; 3.16 A; A=1-150.
DR PDBsum; 7L1K; -.
DR AlphaFoldDB; O74311; -.
DR SMR; O74311; -.
DR BioGRID; 276384; 1.
DR STRING; 4896.SPBC15D4.06.1; -.
DR MaxQB; O74311; -.
DR PaxDb; O74311; -.
DR EnsemblFungi; SPBC15D4.06.1; SPBC15D4.06.1:pep; SPBC15D4.06.
DR GeneID; 2539835; -.
DR KEGG; spo:SPBC15D4.06; -.
DR PomBase; SPBC15D4.06; naa30.
DR VEuPathDB; FungiDB:SPBC15D4.06; -.
DR eggNOG; KOG3139; Eukaryota.
DR HOGENOM; CLU_013985_0_3_1; -.
DR InParanoid; O74311; -.
DR OMA; IVCKLEA; -.
DR PhylomeDB; O74311; -.
DR PRO; PR:O74311; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031417; C:NatC complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:PomBase.
DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IDA:PomBase.
DR GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IBA:GO_Central.
DR GO; GO:0051604; P:protein maturation; NAS:PomBase.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR044542; NAA30-like.
DR PANTHER; PTHR45896; PTHR45896; 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..150
FT /note="N-alpha-acetyltransferase 30"
FT /id="PRO_0000310302"
FT DOMAIN 2..150
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:7L1K"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7L1K"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:7L1K"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7L1K"
SQ SEQUENCE 150 AA; 17699 MW; 31413B59AE8937D4 CRC64;
MVTIVPYSHQ YLKDICQLIQ KDLSEPYSKY VYRYFVHQWP EFSFVALDND RFIGAVICKQ
DVHRGTTLRG YIAMLAIVKE YRGQGIATKL TQASLDVMKN RGAQEIVLET EVDNEAAMSF
YERLGFCRYK RLYRYYLNGT DAFRYILYPN
