CCAMK_PEA
ID CCAMK_PEA Reviewed; 527 AA.
AC Q6RET6; Q6RET4; Q703H2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase;
DE EC=2.7.11.17;
DE AltName: Full=Ps-SYM9;
DE AltName: Full=PsCCaMK;
DE Flags: Fragment;
GN Name=SYM9;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-24 AND GLY-202.
RC STRAIN=cv. Frisson;
RX PubMed=14963335; DOI=10.1126/science.1093038;
RA Levy J., Bres C., Geurts R., Chalhoub B., Kulikova O., Duc G.,
RA Journet E.-P., Ane J.-M., Lauber E., Bisseling T., Denarie J.,
RA Rosenberg C., Debelle F.;
RT "A putative Ca2+ and calmodulin-dependent protein kinase required for
RT bacterial and fungal symbioses.";
RL Science 303:1361-1364(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-465.
RC TISSUE=Root;
RX PubMed=15070781; DOI=10.1073/pnas.0400595101;
RA Mitra R.M., Gleason C.A., Edwards A., Hadfield J., Downie J.A.,
RA Oldroyd G.E.D., Long S.R.;
RT "A Ca2+/calmodulin-dependent protein kinase required for symbiotic nodule
RT development: gene identification by transcript-based cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4701-4705(2004).
CC -!- FUNCTION: Protein kinase that recognizes the calcium spiking induced by
CC Nod factors and translates this signal to components controlling
CC nodulation and mycorrhizal infection responses.
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=2.7.11.17;
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=2.7.11.17;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS55542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS55543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS55544.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY502067; AAS55542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY502069; AAS55544.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY502068; AAS55543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ621916; CAF21911.1; -; mRNA.
DR AlphaFoldDB; Q6RET6; -.
DR SMR; Q6RET6; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0009877; P:nodulation; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calmodulin-binding; Coiled coil; Kinase; Membrane;
KW Metal-binding; Nodulation; Nucleotide-binding; Phosphoprotein; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..>527
FT /note="Calcium and calcium/calmodulin-dependent
FT serine/threonine-protein kinase"
FT /id="PRO_0000085700"
FT TRANSMEM 239..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 12..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 408..443
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 444..479
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 486..521
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..350
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COILED 358..379
FT /evidence="ECO:0000255"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 432
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 468
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 499
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 501
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 503
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 279
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MUTAGEN 24
FT /note="S->F: In DK22; loss of nodulation and mycorrhizal
FT infection."
FT /evidence="ECO:0000269|PubMed:14963335"
FT MUTAGEN 202
FT /note="G->R: In DK9; loss of nodulation and mycorrhizal
FT infection."
FT /evidence="ECO:0000269|PubMed:14963335"
FT NON_TER 527
SQ SEQUENCE 527 AA; 59227 MW; 55662E42C62EF462 CRC64;
MEYGTRKLSD VYEVSEILGR GGFSVVRKGT RKSNNDDEKS QSQSKSQSQS QVAIKTLRRL
GTSNNLPRKK DGGENSTETM MKFPTMRQVS VSDALLTNEI LVMRRIVENV SPHPNVIDLY
DVYEDTNGVH LVLELCSGGE LFDRIVAQDK YSETEASTVV HQIVAGLEAI HRANIIHRDL
KPENCLFLDV GKDSSLKIMD FGLSSVEEFT DPVVGLFGSI DYVSPEALSQ GKITTKSDMW
SLGVILYILL SGYPPFIAQN NRQKQQMILN GNFSFYEKTW KGISQSAKNL ISSLLTVDPA
KRPSAQELLS DPWVKGEKAK DDQMDPEIVS RLQRFNARRK LRAAAIASVW SSTIFLRTKK
LKSLVGSYDL KEDEIENLRM HFKKICADRD NATLCEFEEV LKAMKMPSLI PFAARIFDLF
DNNRDGTVDM REILCGFSSL KNSKGEDALR LCFQMYDTDR SGCITKEEVA SMLRALPYDC
LPTDITEPGK LDEIFDLMDA NSDGKVTFDE FKAAMQRDSS LQDVVLS
