ID Q8MMZ6_CRYPV Unreviewed; 965 AA.
AC Q8MMZ6;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00024113};
GN ORFNames=CPATCC_003876 {ECO:0000313|EMBL:QOY39825.1};
OS Cryptosporidium parvum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=5807 {ECO:0000313|EMBL:AAM20902.1};
RN [1] {ECO:0000313|EMBL:AAM20902.1}
RP NUCLEOTIDE SEQUENCE.
RA Donald R.Gk., Liberator P.A.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAM20902.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11834729; DOI=10.1074/jbc.M108393200;
RA Gurnett A., Liberator P.A., Dulski P., Salowe S.P., Donald R.G.K.,
RA Anderson J.W., Wiltsie J., Diaz-Saldana C.A., Harris G., Chang B.,
RA Darkin-Rattray S.J., Nare B., Crumley T., Blum P., Misura A., Tamas T.,
RA Sardana M., Yuan J., Biftu T., Schmatz D.;
RT "Purification and molecular characterization of cGMP-dependent protein
RT kinase from Apicomplexan parasites. A novel chemotherapeutic target.";
RL J. Biol. Chem. 277:15913-15922(2002).
RN [3] {ECO:0000313|EMBL:QOY39825.1, ECO:0000313|Proteomes:UP000593906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOWA-ATCC {ECO:0000313|EMBL:QOY39825.1,
RC ECO:0000313|Proteomes:UP000593906};
RA Baptista R.P., Li Y., Sateriale A., Ansell B., Jex A., Sanders M.,
RA Brooks K., Tracey A., Berriman M., Striepen B., Cotton J.A.,
RA Kissinger J.C.;
RT "Consistent, comparative and evidence-based genome assembly and annotation
RT for Cryptosporidium parvum, C. hominis and C. tyzzeri.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AF413571; AAM20902.1; -; Genomic_DNA.
DR EMBL; CP044415; QOY39825.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8MMZ6; -.
DR SMR; Q8MMZ6; -.
DR VEuPathDB; CryptoDB:cgd8_750; -.
DR VEuPathDB; CryptoDB:CPATCC_0000790; -.
DR OMA; ESCLADC; -.
DR BRENDA; 2.7.11.12; 1728.
DR Proteomes; UP000593906; Chromosome 8.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 3.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF153; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 4.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW Kinase {ECO:0000313|EMBL:AAM20902.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 109..224
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 227..336
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 499..598
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 622..879
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 965 AA; 109031 MW; D995BFFD9C70C50C CRC64;
MAFLTKLKTS KFSSGVKAAK ETTYEELSKE ENDEIEYPEE KMVVFRDRQK ANIQSRIGGL
SKNMSNISNA GGGMEDDYEQ NMVISHLKDR EKTEEDIKTI SKALAGNVVG ASLNESEIAT
LVSSMHYYEY EVGEVVIEQG ASGFYFFVIS TGSFGVEING NRVNTMSEGT AFGELALIHN
TPRSATILVI EKGGLWGLGR STFRDTLRLI SSRNYEENRA FIESLSIFSG LTDKQKSLLS
EALVREIFVK DQVIIREKEI GNVLYMIKSG IVGVFVEDKY IRSLNEGDAF GERSLMFDEP
RSATVIANAT TECLTLNRGI LTQILGNLGQ VLSKNLIQQS LQNSPIFKQF TKNQMQILLD
KISIKTFQKD VILSTAETKA LNMRAFVILE GEVQVSLPSN WLSRRASSLT SMVIDKSIGS
VNNYSLSDYI NVNLGRGDYF GDDFVFHPKI PFVCKIEMKS ETKIGVITSS MLSECFGDEN
VDVGLEINRK RDAIKSCFVF QYVSEQQLSL LVKSLRLVKF TSGEKIVVQG DKGTAFFILQ
SGEVAVYRNN KFIRYLGKND YFGERALLYD ELRSATIEAA TPEVHLWTVD KEAFLKIVEP
PMRRYLDERI KLQETRVQMS DLKILQTIGK GTFGVVYMVE NIKSGNKYAL KKISKSRILA
LNMQAHVKLE RSILALNDHP FIIKLVRTFK DSENIYLLTE LIPGGELYDA LQRIGLLTRY
QAQFYIGSII LALEYLHERS IVYRDLKPEN ILLDSQGYIK LIDFGCAKKI AGRSYTLAGT
PHYMAPEVIL GKGYNLSCDA WAIGICLYEF LCGCLPFGND AVDHLEIFKD ILTSKLVFPR
HLNDVDTVNI IKRLLCRVPE VRMGCSATGY KEIKDNVFFK DFNFDRLLGR SYVAPLVRKY
RVFAKNTENE NIVENITEVS QNEEALSPNT HNIKSKQKIS FNASKNHSVS TRGNKMDEYD
WDIEF
//
