ID   NMT_CRYNE               Reviewed;         491 AA.
AC   P34809;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 3.
DT   28-JAN-2026, entry version 107.
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   Cryptococcus neoformans (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=5207;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-487.
RC   STRAIN=L210425;
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 = N-
CC         tetradecanoylglycyl-[protein] + CoA + H(+); Xref=Rhea:RHEA:15521,
CC         Rhea:RHEA-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; L25116; AAA17547.1; -; Genomic_DNA.
DR   PIR; A49993; A49993.
DR   SMR; P34809; -.
DR   EnsemblFungi; AAW47000; AAW47000; CNN00080.
DR   VEuPathDB; FungiDB:CKF44_07926; -.
DR   VEuPathDB; FungiDB:CNAG_07926; -.
DR   VEuPathDB; FungiDB:CNBN0070; -.
DR   VEuPathDB; FungiDB:CNN00080; -.
DR   VEuPathDB; FungiDB:LQV05_002182; -.
DR   PHI-base; PHI:19; -.
DR   FunFam; 3.40.630.30:FF:000042; Glycylpeptide N-tetradecanoyltransferase; 1.
DR   FunFam; 3.40.630.30:FF:000056; Glycylpeptide N-tetradecanoyltransferase; 1.
DR   Gene3D; 3.40.630.30; -; 2.
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:SF5; GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE; 1.
DR   PANTHER; PTHR11377; N-MYRISTOYL TRANSFERASE; 1.
DR   Pfam; PF01233; NMT; 1.
DR   Pfam; PF02799; NMT_C; 1.
DR   PIRSF; PIRSF015892; N-myristl_transf; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR   PROSITE; PS00975; NMT_1; 1.
DR   PROSITE; PS00976; NMT_2; 1.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IEA:UniProtKB-EC.
DR   AlphaFoldDB; P34809; -.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..491
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000064239"
FT   REGION          53..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        491
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..48
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         182..184
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         190..194
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   MUTAGEN         487
FT                   /note="G->D: Causes temperature-dependent reduction in
FT                   catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:8300631"
SQ   SEQUENCE   491 AA;  54819 MW;  BF84A3BC61349B9F CRC64;
     MDSSDNKAAT DEEIRRALKA ADLMKILDGK MALGNKSGTK NLGEHKFWKT QPVPQITGSG
     ASAPMEEGPI DDPKTPADVK QEPGVLPAGF EWSTIDINDE EQSKEVYVLL CENYVEDDDA
     MFRFNYSREF LLWALTAPGY LPDWHIGVRV QKTKKLVAFI SGIKIDIRVR AKTFPAAEIN
     FLCVHKKLRS KRLAPVLIKE VTRRVNLTNI WQAIYTAGVI LPTPIGTCRY FHRNLNPPKL
     VDIGFSPLPR GSTIARLVQQ YSVPSHPRIP GFREMKKEDV PQVGALLRRY LDRFDVAQAF
     KDDDEVEHWF LSGQGKEVGG RRVEQVVWAY VVEDPTTHRI TDLISFYALP STIMKHPKHN
     LLNAAYMFYY ATDVIFPPPS SSAHSDADVN AGESSVAAVG TGGEDAKTKK KLETRLNALT
     ADLLIIAKQA GFDVFNALTL LDNNMFLQEQ KFGPGDGYLN YYLYNWNCAP IDGGQHSTTA
     KQGSKIGVVM L
//