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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

Nmt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  • glycylpeptide N-tetradecanoyltransferase activity Source: UniProtKB

GO - Biological processi

  • dorsal closure Source: FlyBase
  • neurogenesis Source: FlyBase
  • N-terminal protein myristoylation Source: FlyBase
  • sensory perception of pain Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferase (EC:2.3.1.97)
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase
Short name:
NMT
Peptide N-myristoyltransferase
dNMT
Gene namesi
Name:Nmt
ORF Names:CG7436
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0020392. Nmt.

Subcellular locationi

  • Membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 472472Glycylpeptide N-tetradecanoyltransferasePRO_0000064228Add
BLAST

Proteomic databases

PaxDbiO61613.
PRIDEiO61613.

Expressioni

Gene expression databases

BgeeiO61613.
GenevisibleiO61613. DM.

Interactioni

Protein-protein interaction databases

BioGridi64329. 3 interactions.
MINTiMINT-818590.
STRINGi7227.FBpp0076451.

Structurei

3D structure databases

ProteinModelPortaliO61613.
SMRiO61613. Positions 91-471.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni92 – 943Myristoyl-CoA bindingBy similarity
Regioni224 – 2263Myristoyl-CoA bindingBy similarity
Regioni232 – 2365Myristoyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
InParanoidiO61613.
KOiK00671.
OMAiSARNVQM.
OrthoDBiEOG76DTS3.
PhylomeDBiO61613.

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. 1 hit.
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.

O61613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNENAEDLS GQELKQKAKE VADASEAMLE KVVAGLNIQD TASTNAAGNE
60 70 80 90 100
DAEQPDGAKN EASVSANASK QALLQAVSDA MASTRQMAKK FAFWSTQPVT
110 120 130 140 150
KLDEQVTTNE CIEPNKEISE IRALPYTLPG GFKWVTLDLN DANDLKELYT
160 170 180 190 200
LLNENYVEDD DAMFRFDYQP EFLKWSLQPP GWKRDWHVGV RVEKSGKLVG
210 220 230 240 250
FISAIPSKLK SYDKVLKVVD INFLCVHKKL RSKRVAPVLI REITRRVNLT
260 270 280 290 300
GIFQAAYTAG VVLPTPVATC RYWHRSLNPK KLVDVRFSHL ARNMTMQRTM
310 320 330 340 350
KLYKLPDQPK TKGYRRITAK DMDKAHKLLE DYLKRFQLSP VFSKEEFRHW
360 370 380 390 400
FTPKEGIIDC FVVADEKGNI TDLTSYYCLP SSVMHHPVHK TVRAAYSFYN
410 420 430 440 450
VSTKTPWLDL MNDALISARN VQMDVYNALD LMENKKYFAP LKFGAGDGNL
460 470
QYYLYNWRCP SMQPEEIALI LM
Length:472
Mass (Da):53,833
Last modified:June 7, 2005 - v2
Checksum:i21A0961A9127A7FA
GO

Sequence cautioni

The sequence AAC08578.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301Missing in AAC08578 (PubMed:9044045).Curated
Sequence conflicti244 – 2441T → S in AAC08578 (PubMed:9044045).Curated
Sequence conflicti412 – 4121N → G in AAC08578 (PubMed:9044045).Curated
Sequence conflicti466 – 4727EIALILM → RLL in AAC08578 (PubMed:9044045).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053725 Genomic DNA. Translation: AAC08578.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF50476.1.
AF132556 mRNA. Translation: AAD27855.1.
AY118963 mRNA. Translation: AAM50823.1.
RefSeqiNP_523969.1. NM_079245.3.
UniGeneiDm.7798.

Genome annotation databases

EnsemblMetazoaiFBtr0076728; FBpp0076451; FBgn0020392.
GeneIDi38909.
KEGGidme:Dmel_CG7436.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053725 Genomic DNA. Translation: AAC08578.1. Sequence problems.
AE014296 Genomic DNA. Translation: AAF50476.1.
AF132556 mRNA. Translation: AAD27855.1.
AY118963 mRNA. Translation: AAM50823.1.
RefSeqiNP_523969.1. NM_079245.3.
UniGeneiDm.7798.

3D structure databases

ProteinModelPortaliO61613.
SMRiO61613. Positions 91-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64329. 3 interactions.
MINTiMINT-818590.
STRINGi7227.FBpp0076451.

Proteomic databases

PaxDbiO61613.
PRIDEiO61613.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076728; FBpp0076451; FBgn0020392.
GeneIDi38909.
KEGGidme:Dmel_CG7436.

Organism-specific databases

CTDi38909.
FlyBaseiFBgn0020392. Nmt.

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
InParanoidiO61613.
KOiK00671.
OMAiSARNVQM.
OrthoDBiEOG76DTS3.
PhylomeDBiO61613.

Miscellaneous databases

GenomeRNAii38909.
NextBioi810959.
PROiO61613.

Gene expression databases

BgeeiO61613.
GenevisibleiO61613. DM.

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. 1 hit.
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. "Sequence and expression of Drosophila myristoyl-CoA: protein N-myristoyl transferase: evidence for proteolytic processing and membrane localisation."
    Ntwasa M., Egerton M., Gay N.J.
    J. Cell Sci. 110:149-156(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Ovary.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiNMT_DROME
AccessioniPrimary (citable) accession number: O61613
Secondary accession number(s): Q9XZ55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 7, 2005
Last modified: May 11, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.