Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00911
Entry Name
UniProt Accession
Theoretical PI
8.33
Molecular Weight
66371.73
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
CDPK-related kinase 6
Protein Synonyms/Alias
AtCRK6; 2.7.11.1; Calcium/calmodulin-dependent protein kinase CRK6;
Gene Name
CRK6
Gene Synonyms/Alias
At3g49370; F2K15.230; T1G12.7;
Created Date
09-JAN-2013
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGHCYSRNI
[1]
N-Myristoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Boisson B, Giglione C, Meinnel T. Unexpected protein families including celldefense components feature in the N-myristoylome of a higher eukaryote. J BiolChem. 2003 Oct 31;278(44):43418-29. Epub 2003 Aug 11.[PMID:12912986]
Functional Description
May play a role in signal transduction pathways that involve calcium as a second messenger.
Sequence Annotation
Domain: 142 404 Protein kinase.
Domain: 445 480 EF-hand 1.
Domain: 481 516 EF-hand 2.
Domain: 517 556 EF-hand 3.
Domain: 557 586 EF-hand 4.
Nucleotide-binding: 148 156 ATP.
Region: 408 438 Autoinhibitory domain.
Region: 427 447 Calmodulin binding (CaMBD).
Active site: 270 270 Proton acceptor.
Binding site: 174 174 ATP.
Modified residue: 352 352 Phosphoserine; by CPK1, CPK10 and CPK34.
Protein Length
594 AA.
Protein Sequence
(Canonical)
MGHCYSRNIS TVDDDDEIPS ATAQLPHRSH QNHHQTSSSS SIPQSPATSE VNPYNISPFQ  60
SPLPAGVAPS PARTPGRKFK WPFPPPSPAK PIMAALRRRR GTAPHPRDGP IPEDSEAGGS  120
GGGIGERLDK NFGFAKNFEG KYELGREVGR GHFGHTCWAK AKKGKIKGQT VAVKIISKSK  180
MTSALSIEDV RREVKLLKAL SGHSHMVKFY DVFEDSDNVF VVMELCEGGE LLDSILARGG  240
RYPEAEAKRI LVQILSATAF FHLQGVVHRD LKPENFLFTS KNEDAVLKVI DFGLSDYARF  300
DQRLNDVVGS AYYVAPEVLH RSYSTEADIW SIGVISYILL CGSRPFYGRT ESAIFRCVLR  360
ANPNFDDLPW PSISPIAKDF VKRLLNKDHR KRMTAAQALA HPWLRDENPG LLLDFSIYKL  420
VKSYIRASPF RRAALKSLSK AIPEEELVFL KAQFMLLEPE DGGLHLHNFT TALTRYATDA  480
MIESRLPDIL NMMQPLAHKK LDFEEFCAAS VSVYQLEALE EWEQIATVAF EHFESEGSRA  540
ISVQELAEEM SLGPNAYPLL KDWIRSLDGK LNFLGYAKFL HGVTVRSSSS RPMR        594
FASTA
(Canonical)
>LipidDB-3702-00911|Q9SG12
MGHCYSRNISTVDDDDEIPSATAQLPHRSHQNHHQTSSSSSIPQSPATSEVNPYNISPFQ
SPLPAGVAPSPARTPGRKFKWPFPPPSPAKPIMAALRRRRGTAPHPRDGPIPEDSEAGGS
GGGIGERLDKNFGFAKNFEGKYELGREVGRGHFGHTCWAKAKKGKIKGQTVAVKIISKSK
MTSALSIEDVRREVKLLKALSGHSHMVKFYDVFEDSDNVFVVMELCEGGELLDSILARGG
RYPEAEAKRILVQILSATAFFHLQGVVHRDLKPENFLFTSKNEDAVLKVIDFGLSDYARF
DQRLNDVVGSAYYVAPEVLHRSYSTEADIWSIGVISYILLCGSRPFYGRTESAIFRCVLR
ANPNFDDLPWPSISPIAKDFVKRLLNKDHRKRMTAAQALAHPWLRDENPGLLLDFSIYKL
VKSYIRASPFRRAALKSLSKAIPEEELVFLKAQFMLLEPEDGGLHLHNFTTALTRYATDA
MIESRLPDILNMMQPLAHKKLDFEEFCAASVSVYQLEALEEWEQIATVAFEHFESEGSRA
ISVQELAEEMSLGPNAYPLLKDWIRSLDGKLNFLGYAKFLHGVTVRSSSSRPMR
Gene Ontology
GO:0005886; C:plasma membrane; IDA:TAIR
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW
Interpro
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF00069; Pkinase;
SMART
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS