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Q5RAF3 (NMT1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycylpeptide N-tetradecanoyltransferase 1

EC=2.3.1.97
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase 1
Short name=NMT 1
Short name=Type I N-myristoyltransferase
Peptide N-myristoyltransferase 1
Gene names
Name:NMT1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the NMT family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processN-terminal protein myristoylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycylpeptide N-tetradecanoyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Glycylpeptide N-tetradecanoyltransferase 1
PRO_0000064223

Amino acid modifications

Modified residue311Phosphoserine By similarity
Modified residue471Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RAF3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: A8D8AA6834B81680

FASTA49656,746
        10         20         30         40         50         60 
MADESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN DTGAKKKKKK 

        70         80         90        100        110        120 
QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW 

       130        140        150        160        170        180 
DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGSTWDA LDLGDRGVLK ELYTLLNENY 

       190        200        210        220        230        240 
VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK 

       250        260        270        280        290        300 
KMVEINFLCV HKKLRSKRVA PVLIREITRR IHLEGVFQAV YTAGVVLPKP VGTCRYWHRS 

       310        320        330        340        350        360 
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP METKDIPVVH QLLTRYLKQF 

       370        380        390        400        410        420 
HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY 

       430        440        450        460        470        480 
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN 

       490 
WKCPSMGAEK VGLVLQ 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859064 mRNA. Translation: CAH91257.1.
RefSeqNP_001127395.1. NM_001133923.1.
UniGenePab.19086.

3D structure databases

ProteinModelPortalQ5RAF3.
SMRQ5RAF3. Positions 155-496.
ModBaseSearch...

Proteomic databases

PRIDEQ5RAF3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174462.
KEGGpon:100174462.

Organism-specific databases

CTD4836.

Phylogenomic databases

HOVERGENHBG003404.

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 nameNMT1_PONAB
AccessionPrimary (citable) accession number: Q5RAF3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families