NMT_CAEEL
ID NMT_CAEEL Reviewed; 450 AA.
AC P46548;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable 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=nmt-1; ORFNames=T17E9.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
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DR EMBL; FO080363; CCD63182.1; -; Genomic_DNA.
DR PIR; D88474; D88474.
DR RefSeq; NP_498326.1; NM_065925.3.
DR AlphaFoldDB; P46548; -.
DR SMR; P46548; -.
DR BioGRID; 41082; 3.
DR DIP; DIP-24373N; -.
DR STRING; 6239.T17E9.2b; -.
DR EPD; P46548; -.
DR PaxDb; P46548; -.
DR PeptideAtlas; P46548; -.
DR EnsemblMetazoa; T17E9.2a.1; T17E9.2a.1; WBGene00020549.
DR GeneID; 175861; -.
DR KEGG; cel:CELE_T17E9.2; -.
DR CTD; 175861; -.
DR WormBase; T17E9.2a; CE01406; WBGene00020549; nmt-1.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; P46548; -.
DR Reactome; R-CEL-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR PRO; PR:P46548; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020549; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P46548; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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..450
FT /note="Probable glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064229"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 68
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 69
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 200
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 201
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 202
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 203
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 209
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 211
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 212
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
FT BINDING 213
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P30419"
SQ SEQUENCE 450 AA; 50889 MW; 5A639808F7DDA38E CRC64;
MSHGHSHDGA PCGGHHGDDG AGGSRPSVND VQALVDQLRL AGVDVSNMPN IPTAPRDMDE
ARSKSFQFWS TQPVPQMDET VPADVNCAIE ENIALDKVRA EPFSLPAGFR WSNVDLSDEE
QLNELYNLLT RNYVEDDDSM FRFDYSADFL KWALQVPGFR PEWHCGVRAD SNNRLLAFIG
AVPQTVRVYD KTVNMVEINF LCVHKNLRSR RVAPVLIREI TRRVNVTGIF QAAFTAGIVI
PKPVSVCRYY HRSLNPRKLI DVRFSHLSAK MTMARTIKLY KLPEETATRN LREMKSTDVP
QVFKLLTTSL KQYSLAPVYN SEEELAHALV PKKGVVYSYV AENQNGKITD FVSFYSLPST
VMGHTTHKTI YAAYLYYYVA GSVTPKQLIN DSLILANREK FDVFNALDLM HNEKIFSDLK
FGKGDGNLQY YLYNWKCADM KPSQIGLVLQ
