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O43010 (NMT_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycylpeptide N-tetradecanoyltransferase
EC=2.3.1.97
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase
Short name=NMT
Peptide N-myristoyltransferase
Gene names
Name:nmt1
ORF Names:SPBC2G2.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processN-terminal protein myristoylation

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionglycylpeptide N-tetradecanoyltransferase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Glycylpeptide N-tetradecanoyltransferase
PRO_0000064247

Regions

Region51 – 544Myristoyl CoA-binding By similarity
Region182 – 21837Myristoyl CoA-binding By similarity

Sites

Active site4661Proton acceptor; via carboxylate By similarity

Amino acid modifications

Modified residue171Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
O43010 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 307B42A7EA33BA61

FASTA46653,696
        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

« Hide

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. expand/collapse author list , 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: 972 / ATCC 24843.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA17891.1.
PIRT40150.
RefSeqNP_596440.1. NM_001022359.1.

3D structure databases

ProteinModelPortalO43010.
SMRO43010. Positions 69-466.
ModBaseSearch...

Protein-protein interaction databases

STRINGO43010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC2G2.11.1; SPBC2G2.11.1:pep; SPBC2G2.11.
GeneID2540407.
GenomeReviewsGene locus nmt1 in contig CU329671_GR.
KEGGspo:SPBC2G2.11.
NMPDRfig|4896.1.peg.2306.

Organism-specific databases

GeneDB_SpombeSPBC2G2.11.

Phylogenomic databases

eggNOGfuNOG07746.
GeneTreeEFGT00050000004932.
HOGENOMHBG314670.
OMAEHAKGSP.
OrthoDBEOG4V9XZZ.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004444-MONOMER.

Gene expression databases

ArrayExpressO43010.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
KOK00671.
PANTHERPTHR11377. Myristoyl_trans. 1 hit.
PfamPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 2 hits.
PROSITEPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNMT_SCHPO
AccessionPrimary (citable) accession number: O43010
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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