Reviewed, UniProtKB/Swiss-Prot O61613 (NMT_DROME)

Names and origin

Protein names

Recommended name:
    Glycylpeptide N-tetradecanoyltransferase
    EC=2.3.1.97
Alternative name(s):
    Peptide N-myristoyltransferase
    Myristoyl-CoA:protein N-myristoyltransferase
      Short name=NMT
    dNMT

Gene names

Name:	Nmt
ORF Names:	CG7436

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Subcellular location	Membrane; Peripheral membrane protein. Ref.1
Sequence similarities	Belongs to the NMT family.
Sequence caution	The sequence AAC08578.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Membrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal peptidyl-glycine N-myristoylation Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB dorsal closure Traceable author statement. Source: FlyBase
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 472	472	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064228
Experimental info
	Sequence conflict	130	1	Missing in AAC08578. Ref.1
	Sequence conflict	244	1	T → S in AAC08578. Ref.1
	Sequence conflict	412	1	N → G in AAC08578. Ref.1
	Sequence conflict	466 – 472	7	EIALILM → RLL in AAC08578. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O61613-1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 21A0961A9127A7FA	FASTA	472	53,833
	10 20 30 40 50 60 MPNENAEDLS GQELKQKAKE VADASEAMLE KVVAGLNIQD TASTNAAGNE DAEQPDGAKN 70 80 90 100 110 120 EASVSANASK QALLQAVSDA MASTRQMAKK FAFWSTQPVT KLDEQVTTNE CIEPNKEISE 130 140 150 160 170 180 IRALPYTLPG GFKWVTLDLN DANDLKELYT LLNENYVEDD DAMFRFDYQP EFLKWSLQPP 190 200 210 220 230 240 GWKRDWHVGV RVEKSGKLVG FISAIPSKLK SYDKVLKVVD INFLCVHKKL RSKRVAPVLI 250 260 270 280 290 300 REITRRVNLT GIFQAAYTAG VVLPTPVATC RYWHRSLNPK KLVDVRFSHL ARNMTMQRTM 310 320 330 340 350 360 KLYKLPDQPK TKGYRRITAK DMDKAHKLLE DYLKRFQLSP VFSKEEFRHW FTPKEGIIDC 370 380 390 400 410 420 FVVADEKGNI TDLTSYYCLP SSVMHHPVHK TVRAAYSFYN VSTKTPWLDL MNDALISARN 430 440 450 460 470 VQMDVYNALD LMENKKYFAP LKFGAGDGNL QYYLYNWRCP SMQPEEIALI LM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9044045] [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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila complementary DNA resource." Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M., Harvey D.A. Science 287:2222-2224(2000) [PubMed: 10731138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Ovary.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF053725 Genomic DNA. Translation: AAC08578.1. Sequence problems. AE014296 Genomic DNA. Translation: AAF50476.1. AF132556 mRNA. Translation: AAD27855.1. AY118963 mRNA. Translation: AAM50823.1.
RefSeq	NP_523969.1.
UniGene	Dm.7798
3D structure databases
HSSP	HSSP built from PDB template 1IYL based on UniProtKB P30418.
ModBase	Search...
Protein-protein interaction databases
IntAct	O61613. 2 interactions.
STRING	O61613.
Genome annotation databases
Ensembl	FBtr0076728; FBpp0076451; FBgn0020392; Drosophila melanogaster. [Genome view]
GeneID	38909.
KEGG	dme:Dmel_CG7436.
NMPDR	fig|7227.3.peg.8800.
Organism-specific databases
CTD	38909.
FlyBase	FBgn0020392. Nmt.
Phylogenomic databases
HOGENOM	O61613.
OMA	VEDDDSM.
Enzyme and pathway databases
BRENDA	2.3.1.97. 48.
Gene expression databases
Bgee	O61613.
GermOnline	CG7436. Drosophila melanogaster.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000903. Myristoyl_trans. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
PANTHER	PTHR11377. Myristoyl_trans. 1 hit.
Pfam	PF01233. NMT. 1 hit. PF02799. NMT_C. 1 hit. [Graphical view]
PIRSF	PIRSF015892. N-myristl_transf. 1 hit.
PROSITE	PS00975. NMT_1. 1 hit. PS00976. NMT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	810959.

Entry information

Entry name

NMT_DROME

Accession

Primary (citable) accession number: O61613
Secondary accession number(s): Q9XZ55

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 7, 2005
Last modified:	November 3, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project