Q8TFN1 (NMT_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	swoF
Synonyms:	nmt1
ORF Names:	AN3839

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Ref.1
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the NMT family.
Sequence caution	The sequence AAL14203.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA59104.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 493	493	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064241
Regions
	Region	82 – 85	4	Myristoyl CoA-binding By similarity
	Region	213 – 249	37	Myristoyl CoA-binding By similarity
Sites
	Active site	493	1	Proton acceptor; via carboxylate By similarity
Experimental info
	Mutagenesis	370	1	D → Y: Causes a temperature sensitive growth defect. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8TFN1 [UniParc]. Last modified November 16, 2011. Version 2. Checksum: 3EAFEA4EC8A66A32	FASTA	493	56,419
	10 20 30 40 50 60 MSDSKDSKGK APQKPNDAEQ TPGGKLTPQA AEALLENNPS LKNELGGLDK DKALEALRKM 70 80 90 100 110 120 DISELLTGLS LTGKNKKDMA AFKFWQTQPV PRFDEAASNA AGGPIKMIDP EKVSKEPDAL 130 140 150 160 170 180 IEGFEWTTLD LTNEEELREL WDLLTYHYVE DDNAMFRFRY SKSFLHWALM SPGWRKEWHV 190 200 210 220 230 240 GVRATKSRKL VASISGVPTQ IRVRGQKIKV TEINFLCIHK KLRSKRLAPV LIKEITRRCY 250 260 270 280 290 300 LNGIYQAIYT AGVVLPTPVS SCRYYHRPLD WLKLYEVGFS PLPRGSTKAR QITKNHLPSH 310 320 330 340 350 360 TSTPNLRPME AKDVDAVHDL LERYLNQFDI HQAFTREEID HWLVYKESPQ KEQVIWSYVV 370 380 390 400 410 420 EDPETHKITD FFSFYNLEST VIQHPKHDCV RAAYLYYYAT ETAFLDDQKA LKNRLQMLMN 430 440 450 460 470 480 DALILAKKAQ FDVFNALTSH HNPLFLEQLK FGAGDGQLHF YLYNYRTAPI AGGVNEKNLP 490 DENRMGGVGV VML

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aspergillus nidulans swoF encodes an N-myristoyl transferase." Shaw B.D., Momany C., Momany M. Eukaryot. Cell 1:241-248(2002) [PubMed: 12455958] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, MUTAGENESIS OF ASP-370.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY057437 Genomic DNA. Translation: AAL14203.1. Sequence problems. AACD01000062 Genomic DNA. Translation: EAA59104.1. Sequence problems. BN001302 Genomic DNA. Translation: CBF75267.1.
RefSeq	XP_661443.1. XM_656351.1.
3D structure databases
ProteinModelPortal	Q8TFN1.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8TFN1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2873262.
KEGG	ani:AN3839.2.
Phylogenomic databases
OrthoDB	EOG4V9XZZ.
PhylomeDB	Q8TFN1.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000903. MyristoylCoA_TrFase. IPR022677. MyristoylCoA_TrFase_C. IPR022678. MyristoylCoA_TrFase_CS. IPR022676. MyristoylCoA_TrFase_N. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
KO	K00671.
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.
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 2 hits.
PROSITE	PS00975. NMT_1. 1 hit. PS00976. NMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NMT_EMENI

Accession

Primary (citable) accession number: Q8TFN1
Secondary accession number(s): C8V6J4, Q5B6J1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	November 16, 2011
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program