| Tag |
Content |
LipidDB ID |
LipidDB-36329-01124 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
7.49 |
Molecular Weight |
32497.06 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
|
Protein Synonyms/Alias |
Adenylate kinase; 2.7.4.3; |
Gene Name |
|
Gene Synonyms/Alias |
PF08_0062; |
Created Date |
01-MAR-2003 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGSCYSRKN | [1] | N-Myristoylation |
|
Organism |
Plasmodium falciparum (isolate 3D7) |
NCBI Taxa ID |
36329 |
Reference |
[1] Rahlfs S, Koncarevic S, Iozef R, Mailu BM, Savvides SN, Schirmer RH, Becker K.Myristoylated adenylate kinase-2 of Plasmodium falciparum forms a heterodimerwith myristoyltransferase. Mol Biochem Parasitol. 2009 Feb;163(2):77-84. doi:10.1016/j.molbiopara.2008.09.008. Epub 2008 Oct 8.[ PMID:18973776]
|
Functional Description |
|
Sequence Annotation |
|
Protein Length |
275 AA. |
Protein Sequence
(Canonical) |
MGSCYSRKNK VSTISLDEEE KKKEKKKKKK IYILNGASGS GKDTQCRLLE KKYNYKIICI 60
SKLLKEYKEE YNKENVLNEE ENYFDEIEKC MIDGSLVNDQ IVIEIFHKQL NKYINDDKYN 120
GIIINGFPRN YEQALLIIQN NISITKFINI QVGKDTLWTR INNRIIDPIT NISYNENIIQ 180
IIKKKREGQE LSDKEQKQLI IDNHLYNNLS NDILERLTKR KDDEEQVFNK RFQLYIESEQ 240
KINSLFKNIC KNVDGEKSIN DIFDQICSII DDNPN 275
|
FASTA
(Canonical) |
>LipidDB-36329-01124|Q8IB06
MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICI
SKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYN
GIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQ
IIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQ
KINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN
|
Gene Ontology |
GO:0020005; C:symbiont-containing vacuole membrane; IDA:GeneDB_Pfalciparum GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC GO:0005524; F:ATP binding; IEA:InterPro |
Interpro |
|
Pfam |
|
SMART |
|
PROSITE |
|
PRINTS |
|