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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

nmt1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei466 – 4661Proton acceptor; via carboxylateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-SPO-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

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
Gene namesi
Name:nmt1
ORF Names:SPBC2G2.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC2G2.11.
PomBaseiSPBC2G2.11.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Glycylpeptide N-tetradecanoyltransferasePRO_0000064247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43010.

PTM databases

iPTMnetiO43010.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

MINTiMINT-4674611.

Structurei

3D structure databases

ProteinModelPortaliO43010.
SMRiO43010. Positions 69-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 544Myristoyl CoA-bindingBy similarity
Regioni182 – 21837Myristoyl CoA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

HOGENOMiHOG000189123.
InParanoidiO43010.
KOiK00671.
OMAiATFRFKY.
OrthoDBiEOG78SQSW.
PhylomeDBiO43010.

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.

O43010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNENNKNTK NSQQDSSFSE GGIRELLDRL ALRSLIEKEE AAAPPKTYED
60 70 80 90 100
FKFWKTQPVP KFDDECTQEG PIDPNTDINQ VPREPYRLLK EFEWATIDVT
110 120 130 140 150
NDNELSEVHE LLTENYVEDA TAMLRFAYIS EFLRWALMPP GYVKEWHVGV
160 170 180 190 200
RVKSSRKLVA FISAVPLSIR VRDKIIKKCA EVNFLCIHKK LRSKRLTPLL
210 220 230 240 250
IKEVTRRCHL ENVWQAVYTA GVLLPSPVSL SRYMHRSLNW KKLYDIGFAP
260 270 280 290 300
FPLGSTEKKE TAKYHLPPNT QTPGLRPMEL KDVPAVQSLL SQYMERFELA
310 320 330 340 350
HLFSEEEVRH WFLYTDKVSS GPVVWSYVVE NPESKKITDF FSFYSLPSTV
360 370 380 390 400
IGNPKYKDIQ AAYLYYYASD SCPKDLSSES QLAFVERCKL IVNDALILAK
410 420 430 440 450
KFHFDVFNAV TVLDNNLFLK DLKFGEGDGF LNYYIYNYNC PKIPGGIDAS
460
KSVDYSRPSG MGFVMI
Length:466
Mass (Da):53,696
Last modified:June 1, 1998 - v1
Checksum:i307B42A7EA33BA61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17891.1.
PIRiT40150.
RefSeqiNP_596440.1. NM_001022359.2.

Genome annotation databases

EnsemblFungiiSPBC2G2.11.1; SPBC2G2.11.1:pep; SPBC2G2.11.
GeneIDi2540407.
KEGGispo:SPBC2G2.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17891.1.
PIRiT40150.
RefSeqiNP_596440.1. NM_001022359.2.

3D structure databases

ProteinModelPortaliO43010.
SMRiO43010. Positions 69-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4674611.

PTM databases

iPTMnetiO43010.

Proteomic databases

MaxQBiO43010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC2G2.11.1; SPBC2G2.11.1:pep; SPBC2G2.11.
GeneIDi2540407.
KEGGispo:SPBC2G2.11.

Organism-specific databases

EuPathDBiFungiDB:SPBC2G2.11.
PomBaseiSPBC2G2.11.

Phylogenomic databases

HOGENOMiHOG000189123.
InParanoidiO43010.
KOiK00671.
OMAiATFRFKY.
OrthoDBiEOG78SQSW.
PhylomeDBiO43010.

Enzyme and pathway databases

ReactomeiR-SPO-2514859. Inactivation, recovery and regulation of the phototransduction cascade.

Miscellaneous databases

PROiO43010.

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

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNMT_SCHPO
AccessioniPrimary (citable) accession number: O43010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.