A5K1A2 (A5K1A2_PLAVS) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glycylpeptide N-tetradecanoyltransferase RuleBase RU000586
EC=2.3.1.97 RuleBase RU000586

Gene names

ORF Names:

PVX_085815 EMBL EDL47099.1

Organism

Plasmodium vivax (strain Salvador I) [Reference proteome]

Taxonomic identifier

126793 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Plasmodium) › Plasmodium vivax

Protein attributes

Sequence length	410 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 By similarity. RuleBase RU000586
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide. RuleBase RU000586
Sequence similarities	Belongs to the NMT family. RuleBase RU004178

Ontologies

Keywords
Molecular function	Acyltransferase RuleBase RU000586 Transferase
Technical term	3D-structure PDB 4A95 PDB 4B10 PDB 4B11 PDB 4B12 PDB 4B13 PDB 4B14 PDB 4BBH Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro
Molecular_function	glycylpeptide N-tetradecanoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A5K1A2 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 86D56189E9852475	FASTA	410	47,970
	10 20 30 40 50 60 MNDDNKEFSG RDIYQLIKNA KDKIKIDYKF WYTQPVPKIN DEFNESVNEP FISDNKVEDV 70 80 90 100 110 120 RKDEYKLPPG YSWYVCDVKD EKDRSEIYTL LTDNYVEDDD NIFRFNYSAE FLLWALTSPN 130 140 150 160 170 180 YLKTWHIGVK YDASNKLIGF ISAIPTDICI HKRTIKMAEV NFLCVHKTLR SKRLAPVLIK 190 200 210 220 230 240 EITRRINLEN IWQAIYTAGV YLPKPVSDAR YYHRSINVKK LIEIGFSSLN SRLTMSRAIK 250 260 270 280 290 300 LYRVEDTLNI KNMRLMKKKD VEGVHKLLGS YLEQFNLYAV FTKEEIAHWF LPIENVIYTY 310 320 330 340 350 360 VNEENGKIKD MISFYSLPSQ ILGNDKYSTL NAAYSFYNVT TTATFKQLMQ DAILLAKRNN 370 380 390 400 410 FDVFNALEVM QNKSVFEDLK FGEGDGSLKY YLYNWKCASF APAHVGIVLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of the neglected human malaria parasite Plasmodium vivax." Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E., Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V., Fernandez-Becerra C., Gilson P.R. , Gueye A.H., Guo X., Kang'a S., Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O., Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J., Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J., Galinski M.R., Barnwell J.W., Fraser-Liggett C.M. Nature 455:757-763(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Salvador I EMBL EDL47099.1.
[2]	"Discovery of Plasmodium vivax N-myristoyltransferase inhibitors: screening, synthesis, and structural characterization of their binding mode." Goncalves V., Brannigan J.A., Whalley D., Ansell K.H., Saxty B., Holder A.A., Wilkinson A.J., Tate E.W., Leatherbarrow R.J. J. Med. Chem. 55:3578-3582(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 27-410.
[3]	"Design and synthesis of inhibitors of Plasmodium falciparum N-myristoyltransferase, a promising target for antimalarial drug discovery." Yu Z., Brannigan J.A., Moss D.K., Brzozowski A.M., Wilkinson A.J., Holder A.A., Tate E.W., Leatherbarrow R.J. J. Med. Chem. 55:8879-8890(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-410.
[4]	"Discovery of novel and ligand-efficient inhibitors of Plasmodium falciparum and Plasmodium vivax N-myristoyltransferase." Rackham M.D., Brannigan J.A., Moss D.K., Yu Z., Wilkinson A.J., Holder A.A., Tate E.W., Leatherbarrow R.J. J. Med. Chem. 56:371-375(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 27-410.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AAKM01000002 Genomic DNA. Translation: EDL47099.1.

RefSeq

XP_001616826.1. XM_001616776.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4A95	X-ray	1.55	A/B/C	27-410	[»]
4B10	X-ray	1.56	A/B/C	27-410	[»]
4B11	X-ray	1.59	A/B/C	27-410	[»]
4B12	X-ray	1.79	A/B/C	27-410	[»]
4B13	X-ray	1.58	A/B/C	27-410	[»]
4B14	X-ray	1.50	A/B/C	27-410	[»]
4BBH	X-ray	1.63	A/B/C	27-410	[»]

ProteinModelPortal

A5K1A2.

SMR

A5K1A2. Positions 70-409.

ModBase

Search...

Protein-protein interaction databases

STRING

5855.PVX_085815.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

5476134.

KEGG

pvx:PVX_085815.

Organism-specific databases

EuPathDB

PlasmoDB:PVX_085815.

Phylogenomic databases

HOGENOM

HOG000189123.

KO

K00671.

ProtClustDB

CLSZ2428978.

Family and domain databases

Gene3D

3.40.630.30. 2 hits.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]

PANTHER

PTHR11377. PTHR11377. 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

A5K1A2_PLAVS

Accession

Primary (citable) accession number: A5K1A2

Entry history

Integrated into UniProtKB/TrEMBL:	July 10, 2007
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)