ID A0A0N7L6W4_PLAHL Unreviewed; 779 AA.
AC A0A0N7L6W4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Camk cdpk protein kinase {ECO:0000313|EMBL:CEG45403.1};
OS Plasmopara halstedii (Downy mildew of sunflower).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Plasmopara.
OX NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG45403.1, ECO:0000313|Proteomes:UP000054928};
RN [1] {ECO:0000313|Proteomes:UP000054928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma Rahul, Thines Marco;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CCYD01001572; CEG45403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N7L6W4; -.
DR STRING; 4781.A0A0N7L6W4; -.
DR EnsemblProtists; CEG45403; CEG45403; CEG45403.
DR OrthoDB; 47229at2759; -.
DR Proteomes; UP000054928; 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; cd17716; BRCT_microcephalin_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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:SF527; LD17393P; 1.
DR PANTHER; PTHR24349; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF12330; Haspin_kinase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
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:CEG45403.1};
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:UP000054928};
KW Transferase {ECO:0000313|EMBL:CEG45403.1}.
FT DOMAIN 67..146
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 310..565
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 710..745
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 779 AA; 87193 MW; 2E81C3A7D940C334 CRC64;
MVTTVSNSRS LAKRASRETT SASSIVTTKS TTSGVRKSRN IGPLKGVVAM VDVRVGIDAE
IDCSDIVSQK LRELGVSTVK RLTPKLTHIV LSHFTPTWKN KIAKWQASGV NVAAFAARYS
LKIVSQLWVN ACYVSKTHMD ERPFFPVGRK ISFESSPSTG NQKGLKGVIR KKAGTTPVYD
FKNCKVANGN KRKRAVSMEP MNSNVMMEKL DITIKVAKLD KHKGVSLSAK RRKTLNGPLT
QQDEDEVTVS QASGSKFESK SDHEDKGKMK MNENSRVDVE LVSSFFNRKR VVTEKTNLCM
HHKTPVGDVY RSLGELGRGA FGVVEKVEHL KTQRQYALKT VHFESGSKRH EFENEMRILR
VLHHPNIVRM LETFEDEHHF YIIMELCSGG TLLDQVKARN KELCEEKAKD IIRSLASVIQ
YLHSRNICHR DLKLENILVE NLEQGGHIKL CDFGASTLFK SGASMREVLG SVVYMAPEVL
EGNYKESCDM WSLGVIMYML LSNKAPFHGN TEDKLIESIF SGNVSYEHNV WATVSLEAKA
LLRKLLNTTP EDRFTAAQVL QHPWIKSSEQ VVLPQVYDMI VPRIKAFCDY SPFQRAALVA
MAFCMSSQRV ALHAAVYNEL NVAHNGDLKL QELHLAPALL RYQLNLDQIF SVLDQQNENG
INLLEFIAAT IGPEDAADEE LLLSTFHILD RSHCGAITKE NLKTLLGQHF TLTECREMIR
KADADKDGKV NFEDFIKLMK LSTDLCGTCT QIFASPACIS NTSDHGSSYI SNARSVAND
//
