P34763 (NMT_AJECA) 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
Organism	Ajellomyces capsulata (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifier	5037 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › Ajellomycetaceae › Ajellomyces

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the NMT family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
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 – 529	529	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064233
Regions
	Region	118 – 121	4	Myristoyl CoA-binding By similarity
	Region	249 – 285	37	Myristoyl CoA-binding By similarity
Sites
	Active site	529	1	Proton acceptor; via carboxylate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P34763 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: E70BC013055F3112	FASTA	529	59,364
	10 20 30 40 50 60 MSEQEGNQSE HQSEHVGESE GKLPNETPTT SQSTNASTGT AGKGEKKSSD GDPAAANPAT 70 80 90 100 110 120 KLTPSMAESL LELNPALRSE LAGMDKEKAT EALRQMNISD LLTGLSVNPK NQKDMASFKF 130 140 150 160 170 180 WQTQPVIRFD DRESESPDGP IKIVELDQVS REPIPLVDGF EWVTLDIDDE ADVKEFYELL 190 200 210 220 230 240 ANHYVEDGSA MFRFNYSPAF LNWALKAPGW KREWHVGVRA SKSGKLVASI CGVPAEIAVR 250 260 270 280 290 300 GKSLKVTEIN FLCVHKKLRS KRLTPVLIKE ITRRCYLNGI YQAIYTVGIM LPTPVSACRY 310 320 330 340 350 360 YHRALDWLKL HEVGFSPLPI GSTKSRQVTR NHLPGHTSTP GLRPMQSKDI DAVQDLLNRY 370 380 390 400 410 420 LKRFDLSQIF SRKEVDHLLL HKEKPGAEQI VWSYVAEEPG THRITDFAAF YSLESSVLQN 430 440 450 460 470 480 SKHKNVKAAY LYYYATETAF AEKEKGLKER LLMLINDVLI LAKKERFDVM NALTLHDNPL 490 500 510 520 FLEQLKFGAG DGQLHYYLFN YRTAPIAGGV NDKNLPDERK RGGVGVILV

References

[1]	"Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans." Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I. J. Biol. Chem. 269:2996-3009(1994) [PubMed: 8300631] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26032 / G217B.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L25118 Unassigned DNA. Translation: AAA17549.1.
PIR	B49993.
3D structure databases
ProteinModelPortal	P34763.
SMR	P34763. Positions 114-529.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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_AJECA

Accession

Primary (citable) accession number: P34763

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 31, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program