ID B6ADZ8_CRYMR Unreviewed; 903 AA.
AC B6ADZ8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=CMU_009310 {ECO:0000313|EMBL:EEA06439.1};
OS Cryptosporidium muris (strain RN66).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN [1] {ECO:0000313|EMBL:EEA06439.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA06439.1,
RC ECO:0000313|Proteomes:UP000001460};
RA Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA da Silva J.;
RL Submitted (JUN-2008) 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}.
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DR EMBL; DS989729; EEA06439.1; -; Genomic_DNA.
DR RefSeq; XP_002140788.1; XM_002140752.1.
DR AlphaFoldDB; B6ADZ8; -.
DR STRING; 441375.B6ADZ8; -.
DR EnsemblProtists; EEA06439; EEA06439; CMU_009310.
DR GeneID; 6995951; -.
DR VEuPathDB; CryptoDB:CMU_009310; -.
DR eggNOG; KOG0032; Eukaryota.
DR OrthoDB; 655312at2759; -.
DR Proteomes; UP000001460; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; PTHR24349:SF569; MAP KINASE-ACTIVATED PROTEIN KINASE 2; 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; 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; 4.
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:EEA06439.1};
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:UP000001460};
KW Transferase {ECO:0000313|EMBL:EEA06439.1}.
FT DOMAIN 418..673
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 753..788
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 789..824
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 825..860
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 868..903
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 107..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 903 AA; 102693 MW; 42B5EE9FB982D1E1 CRC64;
MTSKILVRYE SGLDTYENNS NIFTPCSQEC FTFETAEEED PTIFDLNSHE LNGLVTSIKK
NFEEDVPSSQ CFSKDKNNVS NFEESGTLNK DRYMMTSVRP DSKVCNKGVN KGQSSQNIKY
PSCKGLNTQQ RNRLDQNRSS DLGSYTMEVS QHQNITDNST NYNVNSIQFS DVIPGINNKD
NQRCCRDCNY EGYNNQVNNI KNNFSKAGNQ PSIHGAHNYH EIPEISKIEY ITETSSLTSL
EDSNMEGIYE NSCDKTALYS IYNNEDVNKE MTCQACKYSH DCYQRSPEAY NYPNLDAMYV
GSKVQVSSDI NNLDLHAKSS TLDNSVEKSY FCAENEHYKV LCREYCDLVN YMYCNYNLIS
KPCINSKVNS NSASPLSCKE RKSPLSSKRS SECPLKEGKF RRDGLIPACK GSIYIDYIID
MKSIGKGTYG SVCCGVNRLT GVVRAIKSIP LAKVKAMDRF MKEINIMKNL DHPNIVKLYE
TYQDHKNIYL VLEFCSGGEL FDRIIQQGNF DEAYAAYLMR QILSAIFYCH EHGIVHRDLK
PENFLFLNNQ NNAPLKIIDF GLATKFNKNN TTLTTRAGTP YYVAPEVLSG EYDQQCDLWS
LGVILYILLC GYPPFYGSSD NIILQKVKTG HFIFKDKDWK DISPLAKDLI CKLLTYNPKG
RICARDALKH PWITHFTRNN YKIPLYCLIN ETQLEGNETD KECNQGFSSL NSYRTGTCIS
SGINILSNFR NFHQYNRFKK VALTVIAQQM TESQISNLKE AFFALDANGD GTLTPQEIIL
GLQKSGIKEL PSDLIQILQD IDSDGSGSID YTEFIAATLD SRQCFQEDIC WAAFRVFDLD
GNGKITASEI MNVIGCHHVR HALHLQSYIM STIEDMIREV DVNGDGEIDF EEFLEMFRRC
EKV
//
