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Database: UniProt
Entry: D8S806_SELML
LinkDB: D8S806_SELML
Original site: D8S806_SELML 
ID   D8S806_SELML            Unreviewed;       559 AA.
AC   D8S806;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Calcium dependent protein kinase 17 {ECO:0000313|EMBL:EFJ19441.1};
GN   Name=CPK17-2_2 {ECO:0000313|EMBL:EFJ19441.1};
GN   ORFNames=SELMODRAFT_449840 {ECO:0000313|EMBL:EFJ19441.1};
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:EFJ19441.1, 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).
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DR   EMBL; GL377606; EFJ19441.1; -; Genomic_DNA.
DR   RefSeq; XP_002979552.1; XM_002979506.1.
DR   AlphaFoldDB; D8S806; -.
DR   EnsemblPlants; EFJ19441; EFJ19441; SELMODRAFT_449840.
DR   GeneID; 9634454; -.
DR   Gramene; EFJ19441; EFJ19441; SELMODRAFT_449840.
DR   KEGG; smo:SELMODRAFT_449840; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   HOGENOM; CLU_000288_37_4_1; -.
DR   InParanoid; D8S806; -.
DR   OMA; TCVAYQL; -.
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; cd00051; EFh; 1.
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   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:EFJ19441.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
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..500
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          501..536
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..58
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   559 AA;  62218 MW;  9B8D4BD6B23DDA35 CRC64;
     MGNCLGHGSR ENIHHHRRDD KNNAYDFPPK ANNAATVTAA PAQPSPPSNK NNREQPTTSP
     LPQPKPSSRH APTIHSITAN VLGKPLEDVR AMYVLGRELG RGQFGVTHLC TDRASGKTYA
     CKTIAKRKLI SKADVEDVKR EVQIMHHLRG NENIVELRGS YEDKHSVHLV MELCEGGELF
     DRIIARGHYS ERAAAALCRT IVRVVYICHS LGVMHRDLKP ENFLLADKSE SAPLKATDFG
     LSVFFKHGDK FTDLVGSAYY VAPEVLRRNY GPEADVWSAG VILYILLSGV PPFWAESEQG
     IFDAVLRGQV DFVSDPWPSI SSSAKDLVKK MLTQDVKKRV TAAEVLSHPW VREDGDAPDA
     PLDNAVLSRM KQFTAMNKLK KLALKVIAAS LSEEEITGLK EMFSSMDTDG SGTITFDELK
     VGLERLGSNL RDAEIRQIMN AADVDGNGTI DYLEFITATM QMNKMQKEDH LYSAFQFFDN
     DNSGYITMEE LEEALVKYGM GDHETMKEIL KEVDTDNDGK INYDEFVAMM TKGAAPSSEQ
     QNNRRKGQEL PVGAPRHRK
//
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