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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

nmt1

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei492 – 4921Proton acceptor; via carboxylateBy similarity

GO - Molecular functioni

  1. glycylpeptide N-tetradecanoyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. N-terminal protein myristoylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

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:AFUA_4G08070
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Glycylpeptide N-tetradecanoyltransferasePRO_0000064235Add
BLAST

Proteomic databases

PRIDEiQ9UVX3.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi102 – 1043Combined sources
Helixi109 – 1113Combined sources
Beta strandi123 – 1275Combined sources
Helixi133 – 14614Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi155 – 1584Combined sources
Helixi161 – 1688Combined sources
Helixi175 – 1773Combined sources
Beta strandi178 – 1836Combined sources
Turni184 – 1863Combined sources
Beta strandi189 – 20214Combined sources
Beta strandi205 – 21713Combined sources
Helixi219 – 2213Combined sources
Beta strandi223 – 2253Combined sources
Helixi226 – 24015Combined sources
Beta strandi246 – 2527Combined sources
Beta strandi258 – 26912Combined sources
Helixi270 – 2756Combined sources
Helixi287 – 2937Combined sources
Beta strandi305 – 3073Combined sources
Helixi310 – 3123Combined sources
Helixi313 – 32412Combined sources
Beta strandi327 – 3315Combined sources
Helixi335 – 3428Combined sources
Turni346 – 3483Combined sources
Beta strandi354 – 3607Combined sources
Turni362 – 3643Combined sources
Beta strandi366 – 38217Combined sources
Beta strandi387 – 39913Combined sources
Helixi400 – 4045Combined sources
Helixi407 – 42721Combined sources
Beta strandi431 – 4377Combined sources
Helixi441 – 4433Combined sources
Turni444 – 4496Combined sources
Beta strandi451 – 46515Combined sources
Beta strandi477 – 4793Combined sources
Helixi481 – 4833Combined sources
Beta strandi485 – 4884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CAVX-ray1.89A86-492[»]
4CAWX-ray2.50A86-492[»]
4CAXX-ray1.85A86-492[»]
4UWIX-ray1.80A86-492[»]
4UWJX-ray1.70A86-492[»]
ProteinModelPortaliQ9UVX3.
SMRiQ9UVX3. Positions 78-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 854Myristoyl CoA-bindingBy similarity
Regioni212 – 24837Myristoyl CoA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

eggNOGiCOG5092.
HOGENOMiHOG000189123.
InParanoidiQ9UVX3.
KOiK00671.
OMAiATFRFKY.
OrthoDBiEOG78SQSW.

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.

Q9UVX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSKDRKGK APEGQSSEKK DGAVNITPQM AESLLENNPA LRNETAGMDK
60 70 80 90 100
DKAAEAMRKM NIAELLTGLS VSGKNQKDMA SYKFWQTQPV PRFDETSTDT
110 120 130 140 150
GGPIKIIDPE KVSKEPDALL EGFEWATLDL TNETELQELW DLLTYHYVED
160 170 180 190 200
DNAMFRFRYS QSFLHWALMS PGWKKEWHVG VRATKSRKLV ASICGVPTEI
210 220 230 240 250
NVRNQKLKVV EINFLCIHKK LRSKRLTPVL IKEITRRCYL NGIYQAIYTA
260 270 280 290 300
GVVLPTPVSS CRYYHRPLDW LKLYEVGFSP LPAGSTKARQ ITKNHLPSTT
310 320 330 340 350
STPGLRPMEP KDIDTVHDLL QRYLSRFALN QAFTREEVDH WLVHKPETVK
360 370 380 390 400
EQVVWAYVVE DPETHKITDF FSFYNLESTV IQNPKHDNVR AAYLYYYATE
410 420 430 440 450
TAFTNNMKAL KERLLMLMND ALILAKKAHF DVFNALTLHD NPLFLEQLKF
460 470 480 490
GAGDGQLHFY LYNYRTAPVP GGVNEKNLPD EKRMGGVGIV ML
Length:492
Mass (Da):56,255
Last modified:May 1, 2000 - v1
Checksum:i921C0C5FF805F000
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035414 mRNA. Translation: BAA87865.1.
AAHF01000005 Genomic DNA. Translation: EAL89981.1.
RefSeqiXP_752019.1. XM_746926.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00007889; CADAFUAP00007889; CADAFUAG00007889.
GeneIDi3508953.
KEGGiafm:AFUA_4G08070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035414 mRNA. Translation: BAA87865.1.
AAHF01000005 Genomic DNA. Translation: EAL89981.1.
RefSeqiXP_752019.1. XM_746926.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CAVX-ray1.89A86-492[»]
4CAWX-ray2.50A86-492[»]
4CAXX-ray1.85A86-492[»]
4UWIX-ray1.80A86-492[»]
4UWJX-ray1.70A86-492[»]
ProteinModelPortaliQ9UVX3.
SMRiQ9UVX3. Positions 78-492.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9UVX3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00007889; CADAFUAP00007889; CADAFUAG00007889.
GeneIDi3508953.
KEGGiafm:AFUA_4G08070.

Phylogenomic databases

eggNOGiCOG5092.
HOGENOMiHOG000189123.
InParanoidiQ9UVX3.
KOiK00671.
OMAiATFRFKY.
OrthoDBiEOG78SQSW.

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

« Hide 'large scale' publications
  1. "N-myristoyl transferase."
    Sakata K., Hashido K., Aoki Y., Arisawa M.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry nameiNMT_ASPFU
AccessioniPrimary (citable) accession number: Q9UVX3
Secondary accession number(s): Q4WP53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 92 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.