ID Q5CYR9_CRYPI Unreviewed; 1042 AA.
AC Q5CYR9;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=cgd7_1260 {ECO:0000313|EMBL:EAK90682.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90682.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK90682.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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:EAK90682.1}.
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DR EMBL; AAEE01000001; EAK90682.1; -; Genomic_DNA.
DR RefSeq; XP_628311.1; XM_628309.1.
DR AlphaFoldDB; Q5CYR9; -.
DR SMR; Q5CYR9; -.
DR STRING; 353152.Q5CYR9; -.
DR EnsemblProtists; EAK90682; EAK90682; cgd7_1260.
DR GeneID; 3371779; -.
DR KEGG; cpv:cgd7_1260; -.
DR InParanoid; Q5CYR9; -.
DR OMA; RECNILT; -.
DR OrthoDB; 199981at2759; -.
DR Proteomes; UP000006726; Chromosome 7.
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 Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
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 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; 2.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00054; EFh; 5.
DR SUPFAM; SSF47473; EF-hand; 2.
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.
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:EAK90682.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Transferase {ECO:0000313|EMBL:EAK90682.1}.
FT DOMAIN 282..317
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 403..773
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 819..854
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 888..923
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 950..985
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAK90682.1"
SQ SEQUENCE 1042 AA; 115540 MW; 972BEEBC97AB406D CRC64;
KMTVATSSRR NSRRSSLSSE SSLTSHTSST KPKNSYIQKN SSVSGGNGTS HNCYSHKGRS
GSGFGSSSSY ENRAYLVSGG GSCIGNNTSM GNANGSLLAP NVQLDNLPSE RVGNGSPNWA
LSADVCSLKD FKELIECKNE HAESVLRKYS GIKSVNGGRG IRQVLASIVR GSRTSKNRSS
SVDSGSCGMV SSSTSTTTSS AALVSNLNRK NTTGGDINNT RIKIEDSIDG NGTIINDNNG
SSTSNRECNI LTGQPIQKAI LTQRDIMELR GKIDKVLSTE DSFVRSALQS FQQFDFDGDG
NLTIEELLDL LTTLGEHLAL PPINRKVVAN EISIRLNSKL TVDSSASESK MLISFPFFLK
YYLSVLTTIR QKHFSSVKIN GELQQNKAIR KHLVHEDDIN DLYTFHYQLG TGTYGEVFLV
TENYTRQRRV CKIVDKVKCR RKLDEIDHEV EILKQLDHPG LVHIYEVYED RLNLYFILEF
CAGGNLFHSL QDAIQSGFRF SEFHVSRIIQ QILLAIRYLH LKRVVHKNLK PQNILLTNSF
GSGNTSVKLV DFGLAEIFSS DEINLPELTT SNVSPSHFHS PLKSLPLSSS SSSSYITQDH
IKTHNQAQPQ AQIQGHTHNT SLSSISNQNR ASEEGYLFAS VDEVTGIHKS NSSHNSSPSS
NSSLAQNLHQ EESLASYPKY LDFTAPELLK GETFSYSLDV WSVGVIMYSV ITGRHPFSGR
SRAETRHNIC FGIPAISEIT CVSNACKSLL GKLLEKNPRE RITVDEALSH DWFSISHSSY
CEVDIGMPLL AHLKVYTRQS DLRHILIHML SHQLALDTTQ INMATSVFKS LDTDNDGVLS
ISELGSGLQK LGISSRESSM IIKAMDIDGN GIISYSEFIT ACHIWRRNEI RQLKSFFMKI
DRNNQGKITR EEFKQLLKAQ KSKLLSNITK SFSSTNDVNY RTILPSSNQG VYTEWDSVLD
EIDTNRDGLI DWKEFCTFIV DYFNTSRESL RACYNNSSIS NISSTFSIDP PSVAGLSRRR
DSGICPVQEA NQHPPPHPSQ LD
//