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243  structures 1539  species 0  interactions 2644  sequences 63  architectures

Family: NMT (PF01233)

Summary: Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "Glycylpeptide N-tetradecanoyltransferase". More...

Glycylpeptide N-tetradecanoyltransferase Edit Wikipedia article

In enzymology, a glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) is an enzyme that catalyzes the chemical reaction

tetradecanoyl-CoA + glycylpeptide CoA + N-tetradecanoylglycylpeptide

Thus, the two substrates of this enzyme are tetradecanoyl-CoA and glycylpeptide, whereas its two products are CoA and N-tetradecanoylglycylpeptide.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is tetradecanoyl-CoA:glycylpeptide N-tetradecanoyltransferase. Other names in common use include peptide N-myristoyltransferase, myristoyl-CoA-protein N-myristoyltransferase, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoylating enzymes, and protein N-myristoyltransferase.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1IIC, 1IID, 1IYK, 1IYL, 1RXT, 2NMT, 2P6E, 2P6F, and 2P6G.

References

Template:Enzyme references

  • Guertin D, Grise-Miron L, Riendeau D (1986). "Identification of a 51-kilodalton polypeptide fatty acyl chain acceptor in soluble extracts from mouse cardiac tissue". Biochem. Cell. Biol. 64: 1249–55. PMID 3566958.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Heuckeroth RO, Towler DA, Adams SP, Glaser L, Gordon JI (1988). "11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase". J. Biol. Chem. 263: 2127–33. PMID 3123489.{{cite journal}}: CS1 maint: multiple names: authors list (link)

External links

The CAS registry number for this enzyme class is Template:CAS registry.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This is the Wikipedia entry entitled "Glycylpeptide N-tetradecanoyltransferase 2". More...

Glycylpeptide N-tetradecanoyltransferase 2 Edit Wikipedia article

Template:PBB Controls

NMT2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNMT2, N-myristoyltransferase 2
External IDsOMIM: 603801 MGI: 1202298 HomoloGene: 101539 GeneCards: NMT2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001308295
NM_004808

NM_001290368
NM_001290369
NM_001290370
NM_008708

RefSeq (protein)

NP_001295224
NP_004799

NP_001277297
NP_001277298
NP_001277299
NP_032734

Location (UCSC)Chr 10: 15.1 – 15.17 MbChr 2: 3.29 – 3.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

N-myristoyltransferase 2, also known as NMT2, is a human gene.

Template:PBB Summary

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000152465 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026643 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain Provide feedback

The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.

Literature references

  1. 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; , Nat Struct Biol 1998;5:213-221.: Crystal structure of the anti-fungal target N-myristoyl transferase. PUBMED:9501915 EPMC:9501915


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR022676

Myristoyl-CoA:protein N-myristoyltransferase ( EC ) (Nmt) [ PUBMED:8322618 ] 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.

The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold. This entry represents the N-terminal region.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(112)
Full
(2644)
Representative proteomes UniProt
(4519)
RP15
(501)
RP35
(1145)
RP55
(2052)
RP75
(2741)
Jalview View  View  View  View  View  View  View 
HTML View  View           
PP/heatmap 1 View           

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(112)
Full
(2644)
Representative proteomes UniProt
(4519)
RP15
(501)
RP35
(1145)
RP55
(2052)
RP75
(2741)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(112)
Full
(2644)
Representative proteomes UniProt
(4519)
RP15
(501)
RP35
(1145)
RP55
(2052)
RP75
(2741)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A , Griffiths-Jones SR
Number in seed: 112
Number in full: 2644
Average length of the domain: 152.5 aa
Average identity of full alignment: 58 %
Average coverage of the sequence by the domain: 31.77 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.1 25.2
Noise cut-off 24.8 24.9
Model length: 160
Family (HMM) version: 22
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the NMT domain has been found. There are 243 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044VE37 View 3D Structure Click here
A0A077ZDL5 View 3D Structure Click here
A0A0D2GTA6 View 3D Structure Click here
A0A0H5SBS7 View 3D Structure Click here
A0A0K0DUP5 View 3D Structure Click here
A0A0N4U7U7 View 3D Structure Click here
A0A144A366 View 3D Structure Click here
A0A175W597 View 3D Structure Click here
A0A1C1D0N5 View 3D Structure Click here
A0A1D6G321 View 3D Structure Click here
A0A3P7E1V8 View 3D Structure Click here
A0A3Q0KKD2 View 3D Structure Click here
A4I7H1 View 3D Structure Click here
A7YT82 View 3D Structure Click here
B6T7G0 View 3D Structure Click here
B8JIQ9 View 3D Structure Click here
C0NUK3 View 3D Structure Click here
C0P5P9 View 3D Structure Click here
C1GYK9 View 3D Structure Click here
F1M110 View 3D Structure Click here
F1QY00 View 3D Structure Click here
I1KG93 View 3D Structure Click here
I1KUQ9 View 3D Structure Click here
I1L1K9 View 3D Structure Click here
I1MHA1 View 3D Structure Click here
O43010 View 3D Structure Click here
O60551 View 3D Structure Click here
O61613 View 3D Structure Click here
O70310 View 3D Structure Click here
O70311 View 3D Structure Click here
O74234 View 3D Structure Click here
P0CP20 View 3D Structure Click here
P14743 View 3D Structure Click here
P30418 View 3D Structure Click here
P30419 View 3D Structure Click here
P31717 View 3D Structure Click here
P46548 View 3D Structure Click here
Q388H8 View 3D Structure Click here
Q3EBG4 View 3D Structure Click here
Q4DK26 View 3D Structure Click here