ID B9SDM2_RICCO Unreviewed; 641 AA.
AC B9SDM2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Calcium-dependent protein kinase, putative {ECO:0000313|EMBL:EEF38301.1};
DE EC=2.7.11.17 {ECO:0000313|EMBL:EEF38301.1};
GN ORFNames=RCOM_0422070 {ECO:0000313|EMBL:EEF38301.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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DR EMBL; EQ973928; EEF38301.1; -; Genomic_DNA.
DR RefSeq; XP_002524091.1; XM_002524045.2.
DR AlphaFoldDB; B9SDM2; -.
DR STRING; 3988.B9SDM2; -.
DR GeneID; 8259786; -.
DR KEGG; rcu:8259786; -.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; B9SDM2; -.
DR OrthoDB; 655312at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24349:SF295; CALCIUM-DEPENDENT PROTEIN KINASE 25; 1.
DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EEF38301.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EEF38301.1}.
FT DOMAIN 177..435
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 478..513
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 514..549
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 550..585
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 588..619
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 35..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 641 AA; 72059 MW; 1A4B970FB6B3C080 CRC64;
MGNNCVGSRA SQSIWWLTHP TDCFLSHHHA KKEAIKGLPY NKQEQESTTS QPQNTPPEQM
KIAKEEIKQA ALPASSAPPK QEANQKPALP SQPKEEIKQA PLPPKPKDET VQSEVNGIIR
NQRGEIKSTR QVSVKEEKKP AVPPRPRKPH NVKRLYSAGL LAESVLRTKT GHLKEYYNLG
RKLGHGQFGT TFLCVEKGTG KEYACKSIAK RKLSTIDDVE DVRREIQIMH HLSGNPNVIS
IKGAYEDAVA VHVVMELCAG GELFDRIIKR GHYTERKAAQ LTRTIVGVVE ACHSLGVMHR
DLKPENFLFV NNQEDSPLKA IDFGLSVFFK PGEIFTDVVG SPYYVAPEVL KKRYGPEADV
WSAGVMVYIL LSGVPPFWAE TEQEIFEEVL HGQLDFTSDP WPHISESAKD LVRRMLVRDP
RKRITAHEVL CHPWVRDDGV APDKPLDPAV LSRMKQFSAM NKLKKMALRV IAENLSEEEI
AGLTEMFKMI DTDNSGQITF EELKVGLRRF GANLNESEIY DLMQAADIDN SGTIDYGEFI
AATLHLNKVE REDHLFAAFS YFDKDGSGYI TLDELQQACI EFGMEDVHLE EMIREVDQDN
DGRIDYKEFV AMMQKGNSEM GKNGLQGTSF SIGFREALQV C
//
