ID   NMT_YARLI               Reviewed;         443 AA.
AC   Q6C7G2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE            EC=2.3.1.97;
DE   AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE            Short=NMT;
DE   AltName: Full=Peptide N-myristoyltransferase;
GN   Name=NMT1; OrderedLocusNames=YALI0E01078g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC       certain cellular proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC         N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC         COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC         ChEBI:CHEBI:133050; EC=2.3.1.97;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG78979.1; -; Genomic_DNA.
DR   RefSeq; XP_503400.1; XM_503400.1.
DR   AlphaFoldDB; Q6C7G2; -.
DR   SMR; Q6C7G2; -.
DR   STRING; 4952.CAG78979; -.
DR   EnsemblFungi; CAG78979; CAG78979; YALI0_E01078g.
DR   GeneID; 2912937; -.
DR   KEGG; yli:YALI0E01078g; -.
DR   VEuPathDB; FungiDB:YALI0_E01078g; -.
DR   HOGENOM; CLU_022882_1_0_1; -.
DR   InParanoid; Q6C7G2; -.
DR   OMA; RDWHVGV; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000903; NMT.
DR   InterPro; IPR022677; NMT_C.
DR   InterPro; IPR022678; NMT_CS.
DR   InterPro; IPR022676; NMT_N.
DR   PANTHER; PTHR11377; PTHR11377; 1.
DR   Pfam; PF01233; NMT; 1.
DR   Pfam; PF02799; NMT_C; 1.
DR   PIRSF; PIRSF015892; N-myristl_transf; 1.
DR   SUPFAM; SSF55729; SSF55729; 2.
DR   PROSITE; PS00975; NMT_1; 1.
DR   PROSITE; PS00976; NMT_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..443
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000064246"
FT   ACT_SITE        443
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..37
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         167..169
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         175..179
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
SQ   SEQUENCE   443 AA;  51097 MW;  6F53890F089E579B CRC64;
     MSADKFNEIL KMFQQQMAMQ DIPDREKAKK WEEYLFWKTQ PVPKFDEDID SEGPIEHKKL
     EDVRPTPYNL PAEYEWSDVD IENPEHIQEV YDLLYDNYVE DDDATFRFKY SASFLDWALK
     PPGWQKTWYP CVRVAATGKM VAFISAIPTS IQLRDNDLIK AVEINFLCVH KKLRSKRLAP
     VLIKEITRRV NQKDIWQALY TAGVVLPSPV STCRYYHRPL NWTKLYEIGF SAIPPNQTAA
     SMVARYTLPK EVPLKVRAMT KADVKAVHAI LQNYLSAASE MSQHFSEEEV AHWFVDPISE
     DKNDDKIVYS YVVEEDGKVI DFFSFYKLDH TVLKEWATES NLRAAYGFYY ATSSLSSAKA
     RQDRVKELIG SAVILANNLG FEVYNELTLL DNPSHLDDLK FGCGDGYLNY YLFNYRAQPV
     HGGLDKQKQL EQLDGKGVGV IML