Reviewed, UniProtKB/Swiss-Prot O43010 (NMT_SCHPO)

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
ORF Names:	SPBC2G2.11

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins By similarity.
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the NMT family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
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 – 466	466	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064247
Regions
	Region	51 – 54	4	Myristoyl CoA-binding By similarity
	Region	182 – 218	37	Myristoyl CoA-binding By similarity
Sites
	Active site	466	1	Proton acceptor; via carboxylate By similarity
Amino acid modifications
	Modified residue	17	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O43010-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 307B42A7EA33BA61	FASTA	466	53,696
	10 20 30 40 50 60 MDNENNKNTK NSQQDSSFSE GGIRELLDRL ALRSLIEKEE AAAPPKTYED FKFWKTQPVP 70 80 90 100 110 120 KFDDECTQEG PIDPNTDINQ VPREPYRLLK EFEWATIDVT NDNELSEVHE LLTENYVEDA 130 140 150 160 170 180 TAMLRFAYIS EFLRWALMPP GYVKEWHVGV RVKSSRKLVA FISAVPLSIR VRDKIIKKCA 190 200 210 220 230 240 EVNFLCIHKK LRSKRLTPLL IKEVTRRCHL ENVWQAVYTA GVLLPSPVSL SRYMHRSLNW 250 260 270 280 290 300 KKLYDIGFAP FPLGSTEKKE TAKYHLPPNT QTPGLRPMEL KDVPAVQSLL SQYMERFELA 310 320 330 340 350 360 HLFSEEEVRH WFLYTDKVSS GPVVWSYVVE NPESKKITDF FSFYSLPSTV IGNPKYKDIQ 370 380 390 400 410 420 AAYLYYYASD SCPKDLSSES QLAFVERCKL IVNDALILAK KFHFDVFNAV TVLDNNLFLK 430 440 450 460 DLKFGEGDGF LNYYIYNYNC PKIPGGIDAS KSVDYSRPSG MGFVMI

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

[2]

"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA17891.1.
PIR	T40150.
RefSeq	NP_596440.1.
3D structure databases
HSSP	HSSP built from PDB template 1NMT based on UniProtKB P30418.
ModBase	Search...
Protein-protein interaction databases
STRING	O43010.
Genome annotation databases
GeneID	2540407.
GenomeReviews	Gene locus nmt1 in contig CU329671_GR.
KEGG	spo:SPBC2G2.11.
NMPDR	fig|4896.1.peg.2306.
Organism-specific databases
GeneDB_Spombe	SPBC2G2.11.
Phylogenomic databases
OMA	VEDDDSM.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004444-MON.
BRENDA	2.3.1.97. 653.
Gene expression databases
ArrayExpress	O43010.
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_SCHPO

Accession

Primary (citable) accession number: O43010

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)