CCAMK_MEDTR
ID CCAMK_MEDTR Reviewed; 523 AA.
AC Q6RET7; G7L6Z2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3;
DE EC=2.7.11.17;
DE AltName: Full=CCaMK DMI3;
DE AltName: Full=MtCCaMK;
DE AltName: Full=Protein DOES NOT MAKE INFECTIONS 3 {ECO:0000303|PubMed:17722695};
GN Name=CCAMK {ECO:0000303|PubMed:14963335};
GN Synonyms=DMI3 {ECO:0000303|PubMed:17722695};
GN OrderedLocusNames=MTR_8g043970 {ECO:0000312|EMBL:AET02600.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Jemalong A17;
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], FUNCTION, AND IDENTIFICATION.
RC STRAIN=cv. Jemalong A17;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [5]
RP INTERACTION WITH IPD3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17722695; DOI=10.1094/mpmi-20-8-0912;
RA Messinese E., Mun J.H., Yeun L.H., Jayaraman D., Rouge P., Barre A.,
RA Lougnon G., Schornack S., Bono J.J., Cook D.R., Ane J.M.;
RT "A novel nuclear protein interacts with the symbiotic DMI3 calcium- and
RT calmodulin-dependent protein kinase of Medicago truncatula.";
RL Mol. Plant Microbe Interact. 20:912-921(2007).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Jemalong A17;
RX PubMed=22874912; DOI=10.1242/dev.081620;
RA Rival P., de Billy F., Bono J.-J., Gough C., Rosenberg C., Bensmihen S.;
RT "Epidermal and cortical roles of NFP and DMI3 in coordinating early steps
RT of nodulation in Medicago truncatula.";
RL Development 139:3383-3391(2012).
RN [7]
RP REVIEW.
RX PubMed=23221781; DOI=10.4161/psb.22999;
RA Rival P., Bono J.-J., Gough C., Bensmihen S., Rosenberg C.;
RT "Cell autonomous and non-cell autonomous control of rhizobial and
RT mycorrhizal infection in Medicago truncatula.";
RL Plant Signal. Behav. 8:E22999-E22999(2013).
CC -!- FUNCTION: During nodulation, plays a central role in bacterial
CC infection and contributes to nodule organogenesis (PubMed:22874912).
CC Protein kinase that recognizes the calcium spiking induced by Nod
CC factors and translates this signal to components controlling nodulation
CC and mycorrhizal infection responses. May phosphorylate the NSP1 protein
CC (PubMed:14963335, PubMed:15070781). Required in epidermal and cortical
CC cells to promote infection thread (IT) formation in root hairs
CC (PubMed:22874912). {ECO:0000269|PubMed:14963335,
CC ECO:0000269|PubMed:15070781, ECO:0000269|PubMed:22874912}.
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 -!- SUBUNIT: Interacts with IPD3. {ECO:0000269|PubMed:17722695}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17722695}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots (PubMed:17722695,
CC PubMed:22874912). Expressed in root hairs and nodules (PubMed:17722695,
CC PubMed:22874912). Expressed at low levels in flowers. Not detected in
CC leaves or stems (PubMed:22874912). {ECO:0000269|PubMed:17722695,
CC ECO:0000269|PubMed:22874912}.
CC -!- DEVELOPMENTAL STAGE: In non inoculated roots, present at low levels in
CC both epidermis and cortex. Levels increase two days after inoculation
CC with Sinorhizobium meliloti, especially in root hair cells. During
CC infection, mostly expressed in cortical cells where infection thread
CC (IT) progresses and in underlying layers. Detected in the whole cortex
CC of young nodules. In mature nodules, localized in the infection zone.
CC {ECO:0000269|PubMed:22874912}.
CC -!- INDUCTION: Small up-regulation in nodules.
CC {ECO:0000269|PubMed:14963335}.
CC -!- PTM: Autophosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; AY502066; AAS55541.1; -; Genomic_DNA.
DR EMBL; AY496049; AAS75146.1; -; mRNA.
DR EMBL; CM001224; AET02600.1; -; Genomic_DNA.
DR RefSeq; XP_003628124.1; XM_003628076.2.
DR AlphaFoldDB; Q6RET7; -.
DR SMR; Q6RET7; -.
DR STRING; 3880.AET02600; -.
DR EnsemblPlants; AET02600; AET02600; MTR_8g043970.
DR GeneID; 11405240; -.
DR Gramene; AET02600; AET02600; MTR_8g043970.
DR KEGG; mtr:MTR_8g043970; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR OMA; KQQMIMA; -.
DR OrthoDB; 330091at2759; -.
DR BRENDA; 2.7.11.17; 3201.
DR Proteomes; UP000002051; Chromosome 8.
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:0009877; P:nodulation; IMP:UniProtKB.
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 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; 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; 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 ATP-binding; Calcium; Calmodulin-binding; Kinase; Metal-binding;
KW Nodulation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..523
FT /note="Calcium and calcium/calmodulin-dependent
FT serine/threonine-protein kinase DMI-3"
FT /id="PRO_0000085699"
FT DOMAIN 12..306
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 400..435
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 436..471
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 478..513
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 329..342
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q43531"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0AAR7"
SQ SEQUENCE 523 AA; 58637 MW; C53517F0A97BE67D CRC64;
MGYGTRKLSD EYEVSEILGR GGFSVVRKGT KKSSIEEEKS QSQVAIKTLR RLGASNNPSG
LPRKKDIGEK STIGFPTMRQ VSVSDTLLTN EILVMRRIVE NVSPHPNVID LYDVYEDTNG
VHLVLELCSG GELFDRIVAQ DKYSETEAAT VVHQIASGLE AVHRANIVHR DLKPENCLFL
DVRKDSPLKI MDFGLSSVEE FTDPVVGLFG SIDYVSPEAL SQGKITTKSD MWSLGVILYI
LLSGYPPFIA QNNRQKQQMI MNGNFSFYEK TWKGISQPAK NLISSLLTVD PSKRPSALEL
LSDPWVKGEK AKDVQMDPEI VSRLQSFNAR RKLRAAAIAS VWSSTIFLRT KKLKSLVGSY
DLKEEEIENL RMHFKKICAD RDNATLSEFE EVLKAMNMLS LIPFASRIFD LFDNNRDGTV
DMREILCGFS SLKNSKGEDA LRLCFQMYDT DRSGCISKEE VASMLRALPY DCLPTDITEP
GKLDEIFDLM DANNDGKVTF DEFKAAMQRD SSLQDVVLSS IRP
