Reviewed, UniProtKB/Swiss-Prot P34809 (NMT_CRYNV)

Names and origin

Protein names	Recommended name:     Glycylpeptide N-tetradecanoyltransferase     EC=2.3.1.97 Alternative name(s):     Peptide N-myristoyltransferase     Myristoyl-CoA:protein N-myristoyltransferase       Short name=NMT
Organism	Cryptococcus neoformans var. grubii (Filobasidiella neoformans var. grubii)
Taxonomic identifier	178876 [NCBI]
Taxonomic lineage	Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 – 491	491	Glycylpeptide N-tetradecanoyltransferase		PRO_0000064239
Regions
	Region	45 – 48	4	Myristoyl CoA-binding By similarity
	Region	179 – 215	37	Myristoyl CoA-binding By similarity
Sites
	Active site	491	1	Proton acceptor; via carboxylate By similarity
Experimental info
	Mutagenesis	487	1	G → D: Causes temperature-dependent reduction in catalytic activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P34809-1 [UniParc]. Last modified January 10, 2006. Version 3. Checksum: BF84A3BC61349B9F	FASTA	491	54,819
	10 20 30 40 50 60 MDSSDNKAAT DEEIRRALKA ADLMKILDGK MALGNKSGTK NLGEHKFWKT QPVPQITGSG 70 80 90 100 110 120 ASAPMEEGPI DDPKTPADVK QEPGVLPAGF EWSTIDINDE EQSKEVYVLL CENYVEDDDA 130 140 150 160 170 180 MFRFNYSREF LLWALTAPGY LPDWHIGVRV QKTKKLVAFI SGIKIDIRVR AKTFPAAEIN 190 200 210 220 230 240 FLCVHKKLRS KRLAPVLIKE VTRRVNLTNI WQAIYTAGVI LPTPIGTCRY FHRNLNPPKL 250 260 270 280 290 300 VDIGFSPLPR GSTIARLVQQ YSVPSHPRIP GFREMKKEDV PQVGALLRRY LDRFDVAQAF 310 320 330 340 350 360 KDDDEVEHWF LSGQGKEVGG RRVEQVVWAY VVEDPTTHRI TDLISFYALP STIMKHPKHN 370 380 390 400 410 420 LLNAAYMFYY ATDVIFPPPS SSAHSDADVN AGESSVAAVG TGGEDAKTKK KLETRLNALT 430 440 450 460 470 480 ADLLIIAKQA GFDVFNALTL LDNNMFLQEQ KFGPGDGYLN YYLYNWNCAP IDGGQHSTTA 490 KQGSKIGVVM L

References

	« Hide 'large scale' referencesShow 'large scale' 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], MUTAGENESIS OF GLY-487. Strain: L210425.
[2]	"Genome sequence of Cryptococcus neoformans serotype A." Birren B.W., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-Zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.M., Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T., Blitshteyn B. , Bloom T., Boguslavkiy L., Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S.E., Camarata J., Campo K., Chang J., Choepel Y., Collymore A., Cook A., Cooke P., Corum B., DeArellano K., Diaz J.S., Dodge S., Dooley K., Dorris L., Elkins T., Engels R., Erickson J., Faro S., Ferreira P., FitzGerald M., Gage D., Galagan J.E., Gardyna S., Gnerre S., Graham L., Grand-Pierre N., Hafez N., Hagopian D., Hagos B., Hall J., Horton L., Hulme W., Iliev I., Jaffe D., Johnson R., Jones C., Kamal M., Kamat A., Karatas A., Kells C., Landers T., Levine R., Lindblad-Toh K., Liu G., Lui A., Ma L.-J., Mabbitt R., MacLean C., Macdonald P., Major J., Manning J., Matthews C., Mauceli E., McCarthy M., Meldrim J., Meneus L., Mihova T., Mlenga V., Murphy T., Naylor J., Nguyen C., Nicol R., Nielsen C.B., Norbu C., O'Connor T., O'Donnell P., O'Neil D., Oliver J., Peterson K., Phunkhang P., Pierre N., Purcell S., Rachupka A., Ramasamy U., Raymond C., Retta R., Rise C., Rogov P., Roman J., Schauer S., Schupback R., Seaman S., Severy P., Smirnov S., Smith C., Spencer B., Stange-Thomann N., Stojanovic N., Stubbs M., Talamas J., Tesfaye S., Theodore J., Topham K., Travers M., Vassiliev H., Venkataraman V.S., Viel R., Vo A., Wang S., Wilson B., Wu X., Wyman D., Young G., Zainoun J., Zembek L., Zimmer A., Zody M., Lander E.S. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: H99.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L25116 Genomic DNA. Translation: AAA17547.1. AACO02000127 Genomic DNA. No translation available.
PIR	A49993.
3D structure databases
HSSP	HSSP built from PDB template 1NMT based on UniProtKB P30418.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.3.1.97. 303268.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000903. Myristoyl_trans. [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.
PROSITE	PS00975. NMT_1. 1 hit. PS00976. NMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NMT_CRYNV

Accession

Primary (citable) accession number: P34809

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 10, 2006
Last modified:	June 16, 2009
This is version 58 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)