ID   NMT_AJECA               Reviewed;         529 AA.
AC   P34763;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
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;
OS   Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=5037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26032 / G217B;
RX   PubMed=8300631; DOI=10.1016/s0021-9258(17)42038-2;
RA   Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I.;
RT   "Comparison of myristoyl-CoA:protein N-myristoyltransferases from three
RT   pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and
RT   Candida albicans.";
RL   J. Biol. Chem. 269:2996-3009(1994).
CC   -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC       certain cellular proteins.
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.
CC   -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR   EMBL; L25118; AAA17549.1; -; Unassigned_DNA.
DR   PIR; B49993; B49993.
DR   AlphaFoldDB; P34763; -.
DR   SMR; P34763; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; IEA:InterPro.
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; Transferase.
FT   CHAIN           1..529
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000064233"
FT   REGION          1..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        529
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..121
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         252..254
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         260..264
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
SQ   SEQUENCE   529 AA;  59364 MW;  E70BC013055F3112 CRC64;
     MSEQEGNQSE HQSEHVGESE GKLPNETPTT SQSTNASTGT AGKGEKKSSD GDPAAANPAT
     KLTPSMAESL LELNPALRSE LAGMDKEKAT EALRQMNISD LLTGLSVNPK NQKDMASFKF
     WQTQPVIRFD DRESESPDGP IKIVELDQVS REPIPLVDGF EWVTLDIDDE ADVKEFYELL
     ANHYVEDGSA MFRFNYSPAF LNWALKAPGW KREWHVGVRA SKSGKLVASI CGVPAEIAVR
     GKSLKVTEIN FLCVHKKLRS KRLTPVLIKE ITRRCYLNGI YQAIYTVGIM LPTPVSACRY
     YHRALDWLKL HEVGFSPLPI GSTKSRQVTR NHLPGHTSTP GLRPMQSKDI DAVQDLLNRY
     LKRFDLSQIF SRKEVDHLLL HKEKPGAEQI VWSYVAEEPG THRITDFAAF YSLESSVLQN
     SKHKNVKAAY LYYYATETAF AEKEKGLKER LLMLINDVLI LAKKERFDVM NALTLHDNPL
     FLEQLKFGAG DGQLHYYLFN YRTAPIAGGV NDKNLPDERK RGGVGVILV