ID D8T7J7_SELML Unreviewed; 496 AA.
AC D8T7J7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Calcium dependent protein kinase 34 {ECO:0000313|EMBL:EFJ07310.1};
GN Name=CPK34 {ECO:0000313|EMBL:EFJ07310.1};
GN ORFNames=SELMODRAFT_450099 {ECO:0000313|EMBL:EFJ07310.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ07310.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; GL377686; EFJ07310.1; -; Genomic_DNA.
DR RefSeq; XP_002991556.1; XM_002991510.1.
DR AlphaFoldDB; D8T7J7; -.
DR EnsemblPlants; EFJ07310; EFJ07310; SELMODRAFT_450099.
DR GeneID; 9631929; -.
DR Gramene; EFJ07310; EFJ07310; SELMODRAFT_450099.
DR KEGG; smo:SELMODRAFT_450099; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; D8T7J7; -.
DR OMA; PWIKEMC; -.
DR OrthoDB; 655312at2759; -.
DR Proteomes; UP000001514; 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; 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: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; 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; 3.
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 3: Inferred from homology;
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:EFJ07310.1};
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:UP000001514};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..293
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 336..371
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 372..407
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 408..441
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 442..477
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 477..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 496 AA; 55130 MW; 5F519FA9F3BEBCE8 CRC64;
MGNCLGGGDE KKQSARQALV ANVLGQPHKD IKQQYTIGRE LGRGQFGVTY LCTDKKSAQQ
FAVKTISKRK LMNKDDVDDV KREVQIMKHL TGKDNIVELY STFEDKSTVY LVMELCQGGE
LFDRIVSKGH YTEKAASAVC RTIVKVVHTC HSHGVIHRDL KPENFLLANK REDAPVKATD
FGLSVFFRSG QVFREIVGSA YYVAPEVLKK SYGPEADVWS AGVILYVLLA GVPPFWAETE
QGIFEAVLRG HLDLNGSPWP TISASAKDLV RKMLKPNPRE RLSAADVLQH PWIKEDGDAP
DKLIDGEVLS RMKNFSAMNK LKKVALKIIS ESLSEEEIIK LKDMFKQMDT DNSGTITFEE
LKAGLAKQGS NMIDAEIRQL MEAADVDGNG TIDYLEFIQA SMHLNKMDRG DHLHAAFQNI
DTDGSGYITM EELEAALVKH GLGVEDAKDI IKEVDTDNDG RINYDEFCAM MLKRNSPPAG
AGHRRSINDL PVGIKK
//
