ID A0A1Q9EGX0_SYMMI Unreviewed; 1157 AA.
AC A0A1Q9EGX0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=CPK2 {ECO:0000313|EMBL:OLQ06686.1};
GN ORFNames=AK812_SmicGene10014 {ECO:0000313|EMBL:OLQ06686.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ06686.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ06686.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ06686.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000256|ARBA:ARBA00024334}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLQ06686.1}.
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DR EMBL; LSRX01000155; OLQ06686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9EGX0; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 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:SF569; MAP KINASE-ACTIVATED PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 3.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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:0000313|EMBL:OLQ06686.1};
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:UP000186817};
KW Transferase {ECO:0000313|EMBL:OLQ06686.1}.
FT DOMAIN 721..976
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1020..1055
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1121..1156
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 549..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 751
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1157 AA; 128670 MW; 1576D67E3D6CA882 CRC64;
MGRLLEYKRQ HAAGNAPVGI CNRLHDAWPA EILVSHDLDE VETRLQAIIN TERQKRRQSA
LSACRQRMRQ CGKAATRWLH DRSQVLPPSV SRVNAQGVKH VSSSVSESLE MIRAYWERIW
HRSGTPRTCG SAEHGGTCSG RGTKHRFRPK SCLNRPSAIP KARQGLTSAL RRRCRISRLA
FGKTVLGVFG NGSMPSVVMP ELALRNLDSL GCPRAFSAVL WWVWPHQLRW LQPGQVILPQ
PSLVTASVSQ GPQGCPAAPL ALCVLLATSA ATAHENSCQM HQTIFVDDRA AVVYAVCDAV
AYSRAWADES ARLGLEENWD KFHVVSRSMS HLLAGAGLET ADEAEVLGTV FSSNPQKDTV
GVEALSEDHG LVDRLARLPL SPTLRESLYR SRVASRLTWG LWFRTWMIAR ERSLTRAPEG
LKGNWHGTDG RQTCVANARR SYTLRERAMT KLRPWTKVTQ RGHMGNAANG PLAVASDYWS
CRCTQKKDPQ SNSQSGITGE ADAADLDLED HDKIAIADPS RFAKYSAVEN VDEPSPRLHA
NTLKAVYVTK EPVLPDDKER FPERPPDTTP SARTKHSSWA RSTMRYSVGS EFTASSLSGG
TLGSEKHLNS AMASPRHAQP AVDLAVCSTD TDVGNSRGHA KRRPHKALSQ HGRHTESHDG
TEVSPCSRHH DGAESSPYVY HRKASRHLHQ FVRLTDTMGI VPSAALGIVI NNHGNVSDFY
KLDAKPLGEG SFGAVFYATL RVTKASRAIK KIPKEKMREK LVTLKTEVQL LKLVDHPHIV
MLHEIFEDND DVHLVMSLCR GGHLQAYVMR YGRLKEQPAV AAMRQLFRAV SYLHRRFICH
RDLKSENLML LHDEPFTGSS RNTLKVTDFG LATLFQPGVP LTSTAGTPSH MAPEVYAKKY
NLACDLWSCG VILFFVVSRL MPFDANEKGS KRFKFNLNVH PWDLIHQDCI NLVTVLLDKS
VHKRATAAAA LQHPWIVNNT PRVEDVVIQP NVLARLKRYR KHNRFKRACF NVAASFLKES
ERATSDCLFQ FLDSSGDGRI SYEEMAKLVG EKDAREIFGA PDPADNTYKP FAYTEFLAAT
FDRKQSLTTA VCKTAFAAFD RNSDGTISMA ELTSGRLLGA LTVEEISETL KQLDKNGDQA
IDFQEFMAVM KDDEEGG
//
