ID A0A074Z821_9TREM Unreviewed; 1024 AA.
AC A0A074Z821;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012428};
DE EC=2.7.11.12 {ECO:0000256|ARBA:ARBA00012428};
GN ORFNames=T265_08731 {ECO:0000313|EMBL:KER23356.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER23356.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER23356.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) 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=2.7.11.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000962};
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=2.7.11.12; Evidence={ECO:0000256|ARBA:ARBA00000555};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000256|ARBA:ARBA00006352}.
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DR EMBL; KL596852; KER23356.1; -; Genomic_DNA.
DR RefSeq; XP_009172880.1; XM_009174616.1.
DR AlphaFoldDB; A0A074Z821; -.
DR STRING; 6198.A0A074Z821; -.
DR GeneID; 20322910; -.
DR KEGG; ovi:T265_08731; -.
DR CTD; 20322910; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
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; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR035014; STKc_cGK.
DR PANTHER; PTHR24353:SF147; CGMP-DEPENDENT SERINE_THREONIN PROTEIN KINASE-RELATED; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 472..587
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 590..671
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 714..973
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 974..1024
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 992..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 115410 MW; 210014DDB721D9B9 CRC64;
MSTDNLKQLV EKQTAEIAAL KSELLARDTR IADLTGLLDK YQSVFSRQTN QMNLISDGLG
GGTTPSIKPR KRGIGISAEP EDASKIMTHE LKRYPKPNED DLQSALSPTE FELLDTKAKE
VKSAQGKQCK DRQIREFEKL LSTTRCSSNT AEKNRPLSEE ERCLLEKGLN FAVSKGVIRA
EEIVPSVESV FQKLPSMEAE KLRVLLVTVL KSQQPGVPNI APAERRALNT LKNVDSIVIT
KADKGKATVV MNKSDYLHKV RQHIADGPYR QSSNGKITSI MSSKSKVEVG KYLRSEINHL
GQGKWYQLYP KSAIQPRLYG LPKIHKEGVF ISPIVDGIGS PPYQLARYLA GILKPLAGKS
PTHIQVAGLQ MEPDEVLASF DVNSMYTNVP RADAVEVARR LLLADTMLKE RTQLSVDEIV
EGIKVCLNLS HFVSDSVVYT QEQGLAMGSP ISPILANIVR KIIKQAIMEN DFLNHLAQDQ
LNNLIDCMYL IAHRAGETLI NEGDFGDLVY VLFDGVLEIW KDGVKVRDVN RCTVLGELAV
LYNCERTATV KAATACRLWA IDRKSFQTIL RKKNIQRLQS RLAFLRSVPT FHDLPDTTLS
QMADQLTEVR YAPNEYVIRQ GARGDNFYIV CQGQVHVTVQ EVEKSGEINT STKPKFIRTL
GRGEWFGEMA LKGSYNALIG DLEALQRHYA DLKIRQVSKL EDRTRFSHVL LENLKTIGTM
GVGGFGRVEL VKLNDSDGQS FALKKMKKNH IVRTKQQEHV INEKTILLEV NSEFIVKLWK
TFRDSKYVYL LMEPCLGGEL WTLLRDQFFF NETTTQFYVA CVVEALDYLH SLNIIFRDLK
PENLILDNEG YCKLTDFGFA KRVPSGSKTW TFCGTPEYMA PEVILNKGHD SAVDFWSLGI
LIYELLTGLP PFDSPDAMRT YNLILKGLDA VGFPPKVTGN AQNLIRKLCR DSSVERFGYG
KGGIREVEKH VWFEGFDWKG LQKRVLEPPY RRQVDSQQDL RNFDKCPEDK GEPPDELSGW
DANF
//
