ID A0D862_PARTE Unreviewed; 456 AA.
AC A0D862;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Chromosome undetermined scaffold_40, whole genome shotgun sequence {ECO:0000313|EMBL:CAK79229.1};
GN ORFNames=GSPATT00014196001 {ECO:0000313|EMBL:CAK79229.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK79229.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK79229.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK79229.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000256|ARBA:ARBA00024334}.
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DR EMBL; CT868319; CAK79229.1; -; Genomic_DNA.
DR RefSeq; XP_001446626.1; XM_001446589.1.
DR AlphaFoldDB; A0D862; -.
DR EnsemblProtists; CAK79229; CAK79229; GSPATT00014196001.
DR GeneID; 5032411; -.
DR KEGG; ptm:GSPATT00014196001; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_37_3_1; -.
DR InParanoid; A0D862; -.
DR OMA; EVEIMRC; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.
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:SF263; CALCIUM-DEPENDENT PROTEIN KINASE 1; 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; 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 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:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Myristate {ECO:0000256|ARBA:ARBA00022707};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304}.
FT DOMAIN 10..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 313..348
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 350..385
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 386..421
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 422..456
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 456 AA; 52768 MW; 99DC6C04B4A8B779 CRC64;
MTINLVYDQR QCQGVLGVGA FSQVRKVTHR KTRAIRAMKV ISKSRLSTTE LQQNFINEIN
VYKQLDHPHI LKLYEFYQDE KNFYIIIELC TGGELFDKII EKGSFSEKEA SYVMKQIMSA
VLYAHNQNIV HRDLKPENVL LDITSQGNYN VKVVDWGTAK IFSPNQQINE KFGTLYYMAP
EVLKRNYNEK CDIWSCGVIL YILLSGMPPF GGKTDLEIQK SITYGKYTLD SDVWNSVSAH
AKDLVSQMLQ YDVQKRLSAK QVLEHPFLQL QHQEKVDKQI VQCRLKNLVN FRAEQKLQQA
TLMFIGTTMI SKEEKNQLMQ AFKEMDQNGD GILTKEEILE TYKKYMDDET ACQEVQKIMD
LVDMDGSGTI DYTEFIIATM DRKKAVQKEK LKEAFQIFDK DGNGFISEQE IKDVLGPSIT
GIDEKYWMNM IKEIDKNGDG QISYEEFCAM MMKIIQ
//
