ID   NMT_CRYNB               Reviewed;         493 AA.
AC   P0CP21; Q55HW5; Q5K7E9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
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   OrderedLocusNames=CNBN0070;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL17377.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAEY01000065; EAL17377.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_772024.1; XM_766931.1.
DR   AlphaFoldDB; P0CP21; -.
DR   SMR; P0CP21; -.
DR   EnsemblFungi; AAW47000; AAW47000; CNN00080.
DR   EnsemblFungi; EAL17377; EAL17377; CNBN0070.
DR   GeneID; 4939624; -.
DR   KEGG; cnb:CNBN0070; -.
DR   HOGENOM; CLU_022882_2_0_1; -.
DR   Proteomes; UP000001435; Chromosome 14.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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..493
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000410167"
FT   REGION          53..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        493
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"
SQ   SEQUENCE   493 AA;  54964 MW;  CC82641C5B7CFB02 CRC64;
     MDSSDSKAAT DEEIRRALKA ADLMKILDGK IALGNKSGTK NLGEHKFWKT QPVPQITGSG
     APAPIEEGPI DDPKTPADVR QEPGVLPAGF EWSTIDINDE EQSKEVYVLL CENYVEDDDA
     MFRFNYSREF LLWALTAPGY LPDWHIGVRV QKTKKLVAFI SGIKIDIRVR AKTFPAAEIN
     FLCVHKKLRS KRLAPVLIKE VTRRVNLTNI WQAIYTAGVI LPTPIGTCRY FHRNLNPPKL
     VDIGFSPLPR GSTIARLVQQ YSVPSHPRIP GFREMKKEDV PQVGALLRRY LDRFDVAQAF
     RDDDEVEHWL LSGQGKEVGG RRVEQVVWAY VVEDPTTHRI TDLISFYALP STIMKHPKHN
     LLNAAYMFYY ATDVVFPPSS SSANSDVDVD ANAGESSVAA VGTGGEDAKT KKKLETRLNA
     LTADILIIAK QAGFDVFNAL TLLDNNMFLQ EQKFGPGDGY LNYYLYNWNC APIDGGHHST
     TAKQGSKIGV VML