Reviewed, UniProtKB/Swiss-Prot O74234 (NMT_CANGA)

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

Gene names

Name:	NMT1
Ordered Locus Names:	CAGL0A04059g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the NMT family.
Sequence caution	The sequence AAC26048.1 differs from that shown. Reason: Frameshift at positions 10 and 21.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064237
Regions
	Region	34 – 37	4	Myristoyl CoA-binding By similarity
	Region	164 – 200	37	Myristoyl CoA-binding By similarity
Sites
	Active site	451	1	Proton acceptor; via carboxylate By similarity
Experimental info
	Sequence conflict	338	1	Y → F in AAC26048. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O74234-1 [UniParc]. Last modified August 31, 2004. Version 2. Checksum: 514364B1FE3A2CC9	FASTA	451	52,659
	10 20 30 40 50 60 MSEKKIEELL KLLSMNNGDM SKLTANQRKE MKEYKFWKTQ PVTKFDEEVK EEGPIHEEKT 70 80 90 100 110 120 PADIPDEPLP LLPDFEWCAI DVDDEKQLED VFVLLNENYV EDRDASFRFN YTREFFNWAL 130 140 150 160 170 180 KSPGWTPDWH IGVRVKASKK LIAFISAIPV RLRVRAKVID SVEINFLCVH KQLRSKRLTP 190 200 210 220 230 240 VLIKEITRRV NKRNIWHALY TAGVVLPAPV STCRYAHRPL NWDKLYEVQF TDLPPNATKA 250 260 270 280 290 300 EMVAKYTLPK ATKTAGLREL RLEDVDQALA LFNRYQSRFD IVQEFTKEEF IHWFINDKNV 310 320 330 340 350 360 VEQDKRVVFS YVVESEGKVT DFFSFYSLPF TILNNSRYKD LGIGYLYYYA SDADFKFEDR 370 380 390 400 410 420 FDKEGTSLLK QRLSTLVQDA CIIAAQNKMD VFNALSSQDN TLFLEDLKFG PGDGFLNFYL 430 440 450 FNYRTFPITG GLTEDQHFDT EHRSNVGVVM L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the gene encoding the myristoyl-CoA:protein N-myristoyltransferase from the pathogenic yeast, Candida glabrata." Hosking S.L., Massey S.E., Egerton M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF073886 Genomic DNA. Translation: AAC26048.1. Frameshift. CR380947 Genomic DNA. Translation: CAG57836.1.
RefSeq	XP_444943.1.
3D structure databases
HSSP	HSSP built from PDB template 1IIC based on UniProtKB P14743.
SMR	O74234. Positions 31-451.
ModBase	Search...
Protein-protein interaction databases
STRING	O74234.
Genome annotation databases
GeneID	2886412.
GenomeReviews	Gene locus CAGL0A04059g in contig CR380947_GR.
KEGG	cgr:CAGL0A04059g.
Phylogenomic databases
HOGENOM	O74234.
OMA	VEDDDSM.
Enzyme and pathway databases
BRENDA	2.3.1.97. 189220.
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...

Entry information

Entry name

NMT_CANGA

Accession

Primary (citable) accession number: O74234
Secondary accession number(s): Q6FY92

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	August 31, 2004
Last modified:	November 3, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)