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InterPro: IPR000903 Myristoyl-CoA:protein N-myristoyltransferase

Protein matchesHelp
UniProtKB
Matches:
241 proteins
AccessionHelp IPR000903 Myristoyl_trans
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR016181 Acyl-CoA N-acyltransferase
GO Term annotationHelp
Process GO:0006499 N-terminal protein myristoylation
Function GO:0004379 glycylpeptide N-tetradecanoyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Myristoyl-CoA:protein N-myristoyltransferase (EC:2.3.1.97) (Nmt) [1] is the enzyme responsible for transferring a myristate group on the N-terminal glycine of a number of cellular eukaryotics and viral proteins. Nmt is a monomeric protein of about 50 to 60kDa whose sequence appears to be well conserved.

Structural linksHelp
SCOP: d.108.1.2
CATH: 3.40.630.30
Database linksHelp
PDBe-motif: PS00975 , PS00976
Enzyme: EC:2.3.1.97
PROSITE doc: PDOC00752
PANDIT: PF01233 , PF02799
Blocks: IPB000903
Pfam Clan: CL0257.5

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000903 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O61613 Glycylpeptide N-tetradecanoyltransferase

O70310 Glycylpeptide N-tetradecanoyltransferase 1

P14743 Glycylpeptide N-tetradecanoyltransferase

P30419 Glycylpeptide N-tetradecanoyltransferase 1

P46548 Probable glycylpeptide N-tetradecanoyltransferase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000903 Myristoyl-CoA:protein N-myristoyltransferase
IPR016181 Acyl-CoA N-acyltransferase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Rudnick DA, McWherter CA, Gokel GW, Gordon JI.
MyristoylCoA:protein N-myristoyltransferase.
Adv. Enzymol. Relat. Areas Mol. Biol. 67 375-430 1993 [PubMed: 8322618]

Additional ReadingHelp
Farazi TA, Waksman G, Gordon JI.
Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis.
Biochemistry 40 2001 6335-43 [PubMed: 11371195]
http://dx.doi.org/10.1021/bi0101401
Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA.
Crystal structure of the anti-fungal target N-myristoyl transferase.
Nat. Struct. Biol. 5 1998 213-21 [PubMed: 9501915]
http://dx.doi.org/10.1038/nsb0398-213
Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T.
Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors.
Chem. Biol. 9 2002 1119-28 [PubMed: 12401496]
http://dx.doi.org/10.1016/S1074-5521(02)00240-5
Bhatnagar RS, Futterer K, Farazi TA, Korolev S, Murray CL, Jackson-Machelski E, Gokel GW, Gordon JI, Waksman G.
Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs.
Nat. Struct. Biol. 5 1998 1091-7 [PubMed: 9846880]
http://dx.doi.org/10.1038/4202
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InterPro 23.1