ID   NMT_NEUCR               Reviewed;         569 AA.
AC   Q7S3C8; V5ILB4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 106.
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=gtt-1; Synonyms=nmt1; ORFNames=NCU06925;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002242; ESA41844.1; -; Genomic_DNA.
DR   RefSeq; XP_011395353.1; XM_011397051.1.
DR   AlphaFoldDB; Q7S3C8; -.
DR   SMR; Q7S3C8; -.
DR   STRING; 5141.EFNCRP00000006724; -.
DR   ESTHER; neucr-q7s3c8; AlphaBeta_hydrolase.
DR   EnsemblFungi; ESA41844; ESA41844; NCU17177.
DR   GeneID; 23569828; -.
DR   KEGG; ncr:NCU17177; -.
DR   VEuPathDB; FungiDB:NCU17177; -.
DR   HOGENOM; CLU_013257_0_0_1; -.
DR   InParanoid; Q7S3C8; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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   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..569
FT                   /note="Glycylpeptide N-tetradecanoyltransferase"
FT                   /id="PRO_0000064244"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        569
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158..161
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         291..293
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
FT   BINDING         299..303
FT                   /ligand="tetradecanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57385"
FT                   /evidence="ECO:0000250|UniProtKB:P14743"
SQ   SEQUENCE   569 AA;  64151 MW;  1DBBD286BD6DAA4A CRC64;
     MPPTEESKPV DPAQEKQAAE ALASLKEAQQ PAADESGSED EGADGTAQEA GSGSTKKKNK
     KKSKKKNKDK SASTESSAEV GLTEALAQAD PKSALSGLTP KQIQEFIDLN PALANELLAA
     SGSSGTTDVM EAFKKLKIQD IITGLASSGK NRKDMASYKF WATQPVPQFD EKPAIFEEGP
     LKIQKVEDIP DEPIPLNLAP FRWVTMDLTD EKQMQEVEKL LYGHFVEDDE AMFRFKYSTS
     ILKWSLMSPG WRKEWHVGIR SGDTLCAFIA AVPTEIRVRD KVIQGSEVNF LCIHKKLRGK
     RLAPVLIKEI TRRINREGIW QAIYTGGIVL PRPVSTCRYY HRALNWQKLY EVGFSPCPSN
     SKPAFQVRKY ALPEQTSTKG LRELQVKDLD AVHSLLERYL KRFDLTPVFN REETEHWLLH
     KKDSYAEQVI YSYVVEDASG KITDFFSFYL LESTVIRHPK HNSIRAAYMF YYATETAFTE
     PFDKGALTKR LNDLMADALI LAKRHNFDVF NALSLMDNAL FLEKQKFGPG DGQLHYYLFN
     YKANPIHGGV DKKNRLDEDN LSGVGFVMV