ID A7X9K6_PHYPA Unreviewed; 549 AA.
AC A7X9K6; A9SN27; E1C9R2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Calcium-dependent protein kinase {ECO:0000313|EMBL:ABV22549.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:ABV22549.1};
GN Name=CPK1 {ECO:0000313|EMBL:ABV22549.1};
GN ORFNames=PHYPA_005537 {ECO:0000313|EMBL:PNR58542.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:ABV22549.1};
RN [1] {ECO:0000313|EMBL:ABV22549.1}
RP NUCLEOTIDE SEQUENCE.
RA Hrabak E.M., Chervincky K.M.;
RT "Calcium-dependent protein kinase genes from Physcomitrella patens.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNR58542.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32944916.CDS.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [3] {ECO:0000313|EMBL:PNR58542.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32944916.CDS.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [4] {ECO:0000313|EnsemblPlants:PAC:32944916.CDS.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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DR EMBL; EU050658; ABV22549.1; -; Genomic_DNA.
DR EMBL; ABEU02000003; PNR58542.1; -; Genomic_DNA.
DR RefSeq; XP_001767768.1; XM_001767716.1.
DR AlphaFoldDB; A7X9K6; -.
DR STRING; 3218.A7X9K6; -.
DR PaxDb; 3218-PP1S96_216V6-3; -.
DR EnsemblPlants; Pp3c3_37890V3.1; PAC:32944916.CDS.1; Pp3c3_37890.
DR EnsemblPlants; Pp3c3_37890V3.2; PAC:32944917.CDS.1; Pp3c3_37890.
DR EnsemblPlants; Pp3c3_37890V3.4; PAC:32944918.CDS.1; Pp3c3_37890.
DR EnsemblPlants; Pp3c3_37890V3.5; PAC:32944919.CDS.1; Pp3c3_37890.
DR Gramene; Pp3c3_37890V3.1; PAC:32944916.CDS.1; Pp3c3_37890.
DR Gramene; Pp3c3_37890V3.2; PAC:32944917.CDS.1; Pp3c3_37890.
DR Gramene; Pp3c3_37890V3.4; PAC:32944918.CDS.1; Pp3c3_37890.
DR Gramene; Pp3c3_37890V3.5; PAC:32944919.CDS.1; Pp3c3_37890.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_3_1; -.
DR InParanoid; A7X9K6; -.
DR OMA; TEREDHF; -.
DR OrthoDB; 655312at2759; -.
DR Proteomes; UP000006727; Chromosome 3.
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; 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; IPR000261; EH_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:SF353; CALCIUM-DEPENDENT PROTEIN KINASE 17; 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; SM00027; EH; 1.
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:ABV22549.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABV22549.1}.
FT DOMAIN 93..351
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 394..429
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 430..465
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 466..501
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 504..536
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 549 AA; 60578 MW; D95FB1ADB5F6A2B2 CRC64;
MGNTSSRGSR KSTRQVNQGV GSQDTREKND SVNPKTRQGG SVGANNYGGK PSSGAQAGER
STSAPAALPR PKPASRSVSG VLGKPLSDIR QSYILGRELG RGQFGVTYLC TDKMTNEAYA
CKSIAKRKLT SKEDIEDVKR EVQIMHHLSG TPNIVVLKDV FEDKHSVHLV MELCAGGELF
DRIIAKGHYS ERAAADMCRV IVNVVHRCHS LGVFHRDLKP ENFLLASKAE DAPLKATDFG
LSTFFKPGDV FQDIVGSAYY VAPEVLKRSY GPEADVWSAG VIVYILLCGV PPFWAETEQG
IFDAVLKGHI DFENDPWPKI SNGAKDLVRK MLNPNVKIRL TAQQVLNHPW MKEDGDAPDV
PLDNAVLTRL KNFSAANKMK KLALKVIAES LSEEEIVGLR EMFKSIDTDN SGTVTFEELK
EGLLKQGSKL NESDIRKLME AADVDGNGKI DFNEFISATM HMNKTEKEDH LWAAFMHFDT
DNSGYITIDE LQEAMEKNGM GDPETIQEII SEVDTDNDGR IDYDEFVAMM RKGNPGAENG
GTVNKPRHR
//
