CDPK_SOYBN
ID CDPK_SOYBN Reviewed; 508 AA.
AC P28583;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Calcium-dependent protein kinase SK5;
DE Short=CDPK;
DE EC=2.7.11.1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Williams;
RX PubMed=1852075; DOI=10.1126/science.1852075;
RA Harper J.F., Sussman M.R., Schaller G.E., Putnam-Evans C., Charbonneau H.,
RA Harmon A.C.;
RT "A calcium-dependent protein kinase with a regulatory domain similar to
RT calmodulin.";
RL Science 252:951-954(1991).
RN [2]
RP STRUCTURE BY NMR OF 329-508 IN COMPLEX WITH CALCIUM ION.
RX PubMed=15155727; DOI=10.1074/jbc.m311520200;
RA Weljie A.M., Vogel H.J.;
RT "Unexpected structure of the Ca(2+)-regulatory region from soybean calcium-
RT dependent protein kinase-alpha.";
RL J. Biol. Chem. 279:35494-35502(2004).
CC -!- FUNCTION: May play a role in signal transduction pathways that involve
CC calcium as a second messenger.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Activated by calcium. Autophosphorylation may play
CC an important role in the regulation of the kinase activity (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found throughout the plant.
CC -!- DOMAIN: There are 3 contiguous domains conserved in the CDPK subfamily:
CC a kinase domain, an autoinhibitory (junction) domain and a calmodulin-
CC like domain. The autoinhibitory domain (298-328) inactivates kinase
CC activity under calcium-free conditions (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M64987; AAB00806.1; -; mRNA.
DR PIR; A43713; A43713.
DR RefSeq; NP_001238517.2; NM_001251588.2.
DR PDB; 1S6I; NMR; -; A=329-508.
DR PDB; 1S6J; NMR; -; A=329-402.
DR PDBsum; 1S6I; -.
DR PDBsum; 1S6J; -.
DR AlphaFoldDB; P28583; -.
DR BMRB; P28583; -.
DR SMR; P28583; -.
DR STRING; 3847.GLYMA08G00840.1; -.
DR iPTMnet; P28583; -.
DR PRIDE; P28583; -.
DR EnsemblPlants; KRH41022; KRH41022; GLYMA_08G005600.
DR GeneID; 547825; -.
DR Gramene; KRH41022; KRH41022; GLYMA_08G005600.
DR KEGG; gmx:547825; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; P28583; -.
DR OMA; YWEETEM; -.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.1; 2483.
DR EvolutionaryTrace; P28583; -.
DR Proteomes; UP000008827; Chromosome 8.
DR Genevisible; P28583; GM.
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-KW.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP00561; -.
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 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; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..508
FT /note="Calcium-dependent protein kinase SK5"
FT /id="PRO_0000085833"
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 335..370
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 371..406
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 407..442
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 443..476
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 298..328
FT /note="Autoinhibitory domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 348
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 359
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1S6I"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:1S6I"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:1S6I"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:1S6I"
FT TURN 435..440
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:1S6I"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:1S6I"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1S6I"
SQ SEQUENCE 508 AA; 57169 MW; AFCEDC51224192E4 CRC64;
MAAKSSSSST TTNVVTLKAA WVLPQRTQNI REVYEVGRKL GQGQFGTTFE CTRRASGGKF
ACKSIPKRKL LCKEDYEDVW REIQIMHHLS EHANVVRIEG TYEDSTAVHL VMELCEGGEL
FDRIVQKGHY SERQAARLIK TIVEVVEACH SLGVMHRDLK PENFLFDTID EDAKLKATDF
GLSVFYKPGE SFCDVVGSPY YVAPEVLRKL YGPESDVWSA GVILYILLSG VPPFWAESEP
GIFRQILLGK LDFHSEPWPS ISDSAKDLIR KMLDQNPKTR LTAHEVLRHP WIVDDNIAPD
KPLDSAVLSR LKQFSAMNKL KKMALRVIAE RLSEEEIGGL KELFKMIDTD NSGTITFDEL
KDGLKRVGSE LMESEIKDLM DAADIDKSGT IDYGEFIAAT VHLNKLEREE NLVSAFSYFD
KDGSGYITLD EIQQACKDFG LDDIHIDDMI KEIDQDNDGQ IDYGEFAAMM RKGNGGIGRR
TMRKTLNLRD ALGLVDNGSN QVIEGYFK
