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Database: UniProt
Entry: A0A024TKJ9_9STRA
LinkDB: A0A024TKJ9_9STRA
Original site: A0A024TKJ9_9STRA 
ID   A0A024TKJ9_9STRA        Unreviewed;       516 AA.
AC   A0A024TKJ9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=CAMK/CAMK1 protein kinase, variant 1 {ECO:0000313|EMBL:ETV94675.1};
GN   ORFNames=H310_11660 {ECO:0000313|EMBL:ETV94675.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV94675.1};
RN   [1] {ECO:0000313|EMBL:ETV94675.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETV94675.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) 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; KI913984; ETV94675.1; -; Genomic_DNA.
DR   RefSeq; XP_008876619.1; XM_008878397.1.
DR   AlphaFoldDB; A0A024TKJ9; -.
DR   EnsemblFungi; H310_11660-t26_6; H310_11660-t26_6-p1; H310_11660.
DR   EnsemblProtists; ETV94675; ETV94675; H310_11660.
DR   GeneID; 20088710; -.
DR   VEuPathDB; FungiDB:H310_11660; -.
DR   OrthoDB; 49147at2759; -.
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; 2.
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; PTHR24347:SF446; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24347; 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; 3.
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:0000313|EMBL:ETV94675.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:ETV94675.1}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..516
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001534386"
FT   DOMAIN          44..299
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          361..396
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          397..432
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          436..471
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          473..508
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   516 AA;  57520 MW;  73BD93DF93AD6E2E CRC64;
     MRSGWRRVLT AIPLLAATSP WNTAWSEAHT PKPRQRTKSI SDKYEVGKVI GSGGFAVVKL
     AKDRTTGVEV AAKFFDMKTA STAEIEAEID MLRWIGTHAN IVSLRDVVYE PTDIIMIMDL
     VRGGELFDYI VSQGSITEAD ASRMLREVCL ALQHLHQRGV CHRDLKPENL LLTEVSPDAD
     IKIADFGQSL RLPAGSKLTE SPAGGTIVYW APEIIKRAPQ DCAVDMWAFG VLVRLYSSPP
     CAYHADRHRR SCTLPSLPGV SNSWYNSLSD EAKDLLSHLL TVDPEKRFTA ADALSHPWMN
     PRFRRRLSRR YRDGLSGRLQ AYRRLQQLRA NIVTVLLSQK LHKSPSGKHV VAPHTTDLET
     LNQDVYKEVF ALFDEDQSGA ISKHELANVL RALGQQYTPA EIDDIMKAAD VDGDGGISLT
     EFTTLVNSSL IQVEQWNDAD LHAAFEIFDV NHDGFISADE LAYVMNVLDK TPISPAELHD
     LIQSIDENGD GKIDYKEFST LMQAWLVEGR GQTKGK
//
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