ID I7MHV8_TETTS Unreviewed; 506 AA.
AC I7MHV8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 2.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:EAR89931.2};
GN ORFNames=TTHERM_00561220 {ECO:0000313|EMBL:EAR89931.2};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR89931.2, ECO:0000313|Proteomes:UP000009168};
RN [1] {ECO:0000313|Proteomes:UP000009168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(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; GG662808; EAR89931.2; -; Genomic_DNA.
DR RefSeq; XP_001010176.2; XM_001010176.2.
DR AlphaFoldDB; I7MHV8; -.
DR STRING; 312017.I7MHV8; -.
DR GeneID; 7834889; -.
DR KEGG; tet:TTHERM_00561220; -.
DR InParanoid; I7MHV8; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
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 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; 3.
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; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EAR89931.2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..252
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 362..397
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 401..436
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 437..472
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 292..345
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 506 AA; 59213 MW; 01D8083243E28C82 CRC64;
MKVSSSGQIS LVEHKISREK FILKEVQKKH ISNISQFYSD IGVVLKIDHP NILKVFQVYE
SIDKFHIVEE YCQGGSVLEF VAKKQNYNER QCAKIVQQIC SALLHSHQKA IIHQNIKSSK
ILLKYKNDDN SIKLIDLGIN LQSKDKKQSE SQLPQIQELP FLAPEQLEGR NIEVSNSWNV
GVFLYILFSG QHPFQSLDPQ KSLDQIKKGI FTFTKQCFHN CSVELKDLLS KLLTKNERKR
ISIKQCLDHE WIIQSDNSPI FDQSLTEKTF ANLKKFYSQF IDEVDYEEEQ RLNALKRQQE
EDERRRLEEE RRRLEEEMRR MEEEKERLRR LQEEEEQRMK LVQEENLKRR MLMSLVGKIP
QHYIDKLQAV FTAIDENGNG QLSLDELLTG MARFQSGANK FSEEELKDIF QKMDEDNSGE
VSQEEFIHAF AEQFSIKNKN MILQSFKQLD QDGSGIVNLE EFTYLLQNGN LPLGEVSVEQ
ILGFINDNNQ GKINYIDFFE GLQITE
//