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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

NMT

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.UniRule annotation

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi175 – 1751Magnesium; via carbonyl oxygenCombined sources
Metal bindingi178 – 1781Magnesium; via amide nitrogenCombined sources
Metal bindingi180 – 1801Magnesium; via amide nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationImported, Transferase

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

SABIO-RKQ4Q5S8.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferaseUniRule annotation (EC:2.3.1.97UniRule annotation)
Gene namesi
Name:NMTImported
ORF Names:LMJF_32_0080Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 32

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1949483.

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.32.0080.

Chemistry

BindingDBiQ4Q5S8.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WSAX-ray1.60A5-421[»]
3H5ZX-ray1.49A5-421[»]
4A2ZX-ray2.31A5-421[»]
4A30X-ray1.50A5-421[»]
4A31X-ray2.09A5-421[»]
4A32X-ray2.20A5-421[»]
4A33X-ray2.40A5-421[»]
4C7HX-ray1.40A11-421[»]
4C7IX-ray1.30A11-421[»]
4CGLX-ray1.48A11-421[»]
4CGMX-ray1.70A11-421[»]
4CGNX-ray1.69A11-421[»]
4CGOX-ray1.30A11-421[»]
4CGPX-ray1.40A11-421[»]
4CYNX-ray1.40A11-421[»]
4CYOX-ray1.50A11-421[»]
4CYPX-ray1.55A11-421[»]
4CYQX-ray1.65A11-421[»]
4UCMX-ray2.32A5-421[»]
4UCNX-ray1.80A5-421[»]
4UCPX-ray1.50A5-421[»]
5A27X-ray1.37A11-421[»]
5A28X-ray1.48A11-421[»]
5AG4X-ray1.99A5-421[»]
5AG5X-ray2.00A5-421[»]
5AG6X-ray2.00A5-421[»]
5AG7X-ray2.60A5-421[»]
5AGEX-ray2.00A5-421[»]
ProteinModelPortaliQ4Q5S8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4Q5S8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 213178NMTInterPro annotationAdd
BLAST
Domaini229 – 412184NMT_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 154Coenzyme A bindingCombined sources
Regioni169 – 1713Coenzyme A bindingCombined sources
Regioni177 – 1815Coenzyme A bindingCombined sources

Sequence similaritiesi

Belongs to the NMT family.UniRule annotation

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
HOGENOMiHOG000189123.
InParanoidiQ4Q5S8.
KOiK00671.
OMAiATFRFKY.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 2 hits.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4Q5S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRNPSNSDA AHAFWSTQPV PQTEDETEKI VFAGPMDEPK TVADIPEEPY
60 70 80 90 100
PIASTFEWWT PNMEAADDIH AIYELLRDNY VEDDDSMFRF NYSEEFLQWA
110 120 130 140 150
LCPPNYIPDW HVAVRRKADK KLLAFIAGVP VTLRMGTPKY MKVKAQEKGE
160 170 180 190 200
GEEAAKYDEP RHICEINFLC VHKQLREKRL APILIKEATR RVNRTNVWQA
210 220 230 240 250
VYTAGVLLPT PYASGQYFHR SLNPEKLVEI RFSGIPAQYQ KFQNPMAMLK
260 270 280 290 300
RNYQLPSAPK NSGLREMKPS DVPQVRRILM NYLDSFDVGP VFSDAEISHY
310 320 330 340 350
LLPRDGVVFT YVVENDKKVT DFFSFYRIPS TVIGNSNYNL LNAAYVHYYA
360 370 380 390 400
ATSIPLHQLI LDLLIVAHSR GFDVCNMVEI LDNRSFVEQL KFGAGDGHLR
410 420
YYFYNWAYPK IKPSQVALVM L
Length:421
Mass (Da):48,514
Last modified:July 19, 2005 - v1
Checksum:iE29E51E961B90B44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796428 Genomic DNA. Translation: CAJ08448.1.
RefSeqiXP_001685320.1. XM_001685268.1.

Genome annotation databases

EnsemblProtistsiLmjF.32.0080:mRNA; LmjF.32.0080:pep; LmjF.32.0080.
GeneIDi5656116.
KEGGilma:LMJF_32_0080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796428 Genomic DNA. Translation: CAJ08448.1.
RefSeqiXP_001685320.1. XM_001685268.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WSAX-ray1.60A5-421[»]
3H5ZX-ray1.49A5-421[»]
4A2ZX-ray2.31A5-421[»]
4A30X-ray1.50A5-421[»]
4A31X-ray2.09A5-421[»]
4A32X-ray2.20A5-421[»]
4A33X-ray2.40A5-421[»]
4C7HX-ray1.40A11-421[»]
4C7IX-ray1.30A11-421[»]
4CGLX-ray1.48A11-421[»]
4CGMX-ray1.70A11-421[»]
4CGNX-ray1.69A11-421[»]
4CGOX-ray1.30A11-421[»]
4CGPX-ray1.40A11-421[»]
4CYNX-ray1.40A11-421[»]
4CYOX-ray1.50A11-421[»]
4CYPX-ray1.55A11-421[»]
4CYQX-ray1.65A11-421[»]
4UCMX-ray2.32A5-421[»]
4UCNX-ray1.80A5-421[»]
4UCPX-ray1.50A5-421[»]
5A27X-ray1.37A11-421[»]
5A28X-ray1.48A11-421[»]
5AG4X-ray1.99A5-421[»]
5AG5X-ray2.00A5-421[»]
5AG6X-ray2.00A5-421[»]
5AG7X-ray2.60A5-421[»]
5AGEX-ray2.00A5-421[»]
ProteinModelPortaliQ4Q5S8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.32.0080.

Chemistry

BindingDBiQ4Q5S8.
ChEMBLiCHEMBL1949483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.32.0080:mRNA; LmjF.32.0080:pep; LmjF.32.0080.
GeneIDi5656116.
KEGGilma:LMJF_32_0080.

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
HOGENOMiHOG000189123.
InParanoidiQ4Q5S8.
KOiK00671.
OMAiATFRFKY.

Enzyme and pathway databases

SABIO-RKQ4Q5S8.

Miscellaneous databases

EvolutionaryTraceiQ4Q5S8.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 2 hits.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 5-421.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 5-421.
  5. "Diverse modes of binding in structures of Leishmania major N-myristoyltransferase with selective inhibitors."
    Brannigan J.A., Roberts S.M., Bell A.S., Hutton J.A., Hodgkinson M.R., Tate E.W., Leatherbarrow R.J., Smith D.F., Wilkinson A.J.
    IUCrJ 1:250-260(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 11-421.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 11-421.
  7. "Peptidomimetic inhibitors of N-myristoyltransferase from human malaria and leishmaniasis parasites."
    Olaleye T.O., Brannigan J.A., Roberts S.M., Leatherbarrow R.J., Wilkinson A.J., Tate E.W.
    Org. Biomol. Chem. 12:8132-8137(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 11-421 IN COMPLEX WITH COENZYME A AND MAGNESIUM.
  8. "Identification and structure solution of fragment hits against kinetoplastid N-myristoyltransferase."
    Robinson D.A., Wyatt P.G.
    Acta Crystallogr F Struct Biol Commun 71:586-593(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 5-421.
  9. "Development of Small-Molecule Trypanosoma brucei N-Myristoyltransferase Inhibitors: Discovery and Optimisation of a Novel Binding Mode."
    Spinks D., Smith V., Thompson S., Robinson D.A., Luksch T., Smith A., Torrie L.S., McElroy S., Stojanovski L., Norval S., Collie I.T., Hallyburton I., Rao B., Brand S., Brenk R., Frearson J.A., Read K.D., Wyatt P.G., Gilbert I.H.
    ChemMedChem 10:1821-1836(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 5-421.

Entry informationi

Entry nameiQ4Q5S8_LEIMA
AccessioniPrimary (citable) accession number: Q4Q5S8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.