ID A0A078AY37_STYLE Unreviewed; 1334 AA.
AC A0A078AY37;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Protein kinase domain containing protein {ECO:0000313|EMBL:CDW86127.1};
GN Name=Contig9738.g10419 {ECO:0000313|EMBL:CDW86127.1};
GN ORFNames=STYLEM_15218 {ECO:0000313|EMBL:CDW86127.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW86127.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW86127.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW86127.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CCKQ01014372; CDW86127.1; -; Genomic_DNA.
DR EnsemblProtists; CDW86127; CDW86127; STYLEM_15218.
DR InParanoid; A0A078AY37; -.
DR OMA; WIMNGES; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
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 CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 1.20.5.340; -; 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; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13499; EF-hand_7; 1.
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 SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
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|PIRSR:PIRSR630616-
KW 2}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CDW86127.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630616-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Transferase {ECO:0000313|EMBL:CDW86127.1}.
FT DOMAIN 32..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 339..374
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 414..449
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 452..487
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1196..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 638..735
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 908..1076
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1196..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-1"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 158..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT BINDING 174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-2"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR630616-3"
SQ SEQUENCE 1334 AA; 155103 MW; AD2E0381221D3AA4 CRC64;
MQTQKKLKDK FKLKISKSIF VHECKGQIKS KYRVLENIGK GTYGQVKKVL HKATGELRAM
KIIKKGQVND EFMSILMNEI EILKQLDHPK IVRIFEFYQD RENFFLITEL IQDGDLSNLV
KKQKKFDEKQ TITIIKQLLL AIVYCHTKKI AHRDLKPENL ILEDKEKLQV KLIDFGTSIR
FDLNKMDYRI GTPHYMAPEV ITKAYDEKCD IWSIGVIAYY LLAGIHPFRG KNQNDIFKEI
KEYKLSFGGQ EWREISTEAK LFIKRLMSLN PKDRPRPEEA LLDQWIMNGE SSYPKKKQVI
ERNNLVISKM IRNTNQIKIE KKLQQAILSY FANYMNSDEN KRIIEEIYFA FDSNNDGIID
QKELELALLA HYDGNSDLAH IKTMEFLEKL DLNENGDIEY SEFMITSIES QQIMHGDIIQ
EMFEVFDLNQ SGEISSVELR KVLGNNLRKG EIEDNEWDEI VNEIDSNGNG YITFEDFKTT
IMNLFKRDDP RSKLSRLVDF QDVSQAKAGI NRQLTANDKV NPDFNIIEQH HDPNGNIVDT
FLEAKIDISR LDDIFSFTYS FDKLQAILKV LIQQQRAHSD HINSLYKQTA LMDKFRQDQK
QIKDNIKSLG EKLNNHDDSL FNINNNVSNI KINLDDTSTS LENTKRDQDN QLERIEKLEN
DQILMKDDYE TNIQGVKEEL VSVKDNYLSK KQHEEKNQEM KKELSNDIKS NEDELKKLQT
RVKELENSVP TMRIDVDANI TQIKDMMEKI GQIDTSVDKH RSDISLHTRN LDDNMGLIKE
LQRKLQEKVG CDIFDKEINY LKSLLTHLRN KQQDDQKFMQ EEKTKNTREI GSKEFNLLRE
IEEKLPMIED KLKQLMDAML KIPRIEDFLL KLSSQLKELN VSEIMQKLKE LQEHKLDKDQ
FEKFVHQFLD LEAKMKDLQK MISILDQKGA GPDNSDGIMS LIQKQELLIK KISDLEKEVV
ELKRNSKAGN TISINEPANS QEINDLKEQI YNMKKEMDLM KQGFGKSIKD LEKQVKFKVD
NNQLNQLEKV LMDQLNEQMN ILNNKIDDLK KLKAQIAKLE AALKKLQDYI MEQLALLQSM
NHGNSNGEEE DAMFSKRPLL GYSCASCDKD ILNLSGRPAD FHPWSKMPQR DPTDRISRVG
QGFSRMLQQV KPEMIDKLKR GKMMNQTMQN FLQTEGSVDE TMNEDQSIEA ANRSGLIKPI
SSQSQQRLGK IQNKTQLGKT QPINSKQIGA NPGSQTERSH PNDHLKLFSD TPQFKKNLIK
NIQHEQKLMS EIVSPLRERA SKIQFNERQL EMSNTNGDIQ YSTSDIQVLT QHPTSKSTSK
LPPVLRSKTP QKKQ
//
