ID U6KKN7_EIMTE Unreviewed; 866 AA.
AC U6KKN7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=cGMP-dependent protein kinase {ECO:0000313|EMBL:CDJ38484.1};
GN ORFNames=ETH_00017800 {ECO:0000313|EMBL:CDJ38484.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ38484.1};
RN [1] {ECO:0000313|EMBL:CDJ38484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38484.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ38484.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ38484.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG673920; CDJ38484.1; -; Genomic_DNA.
DR RefSeq; XP_013229322.1; XM_013373868.1.
DR AlphaFoldDB; U6KKN7; -.
DR EnsemblProtists; CDJ38484; CDJ38484; ETH_00017800.
DR GeneID; 25252699; -.
DR VEuPathDB; ToxoDB:ETH2_0729000; -.
DR VEuPathDB; ToxoDB:ETH2_0742100; -.
DR VEuPathDB; ToxoDB:ETH_00017800; -.
DR OMA; WEAAFYA; -.
DR OrthoDB; 90197at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 3.
DR Gene3D; 2.60.120.10; Jelly Rolls; 4.
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 PANTHER; PTHR24353:SF37; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT PRKX; 1.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 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; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CDJ38484.1};
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 173..289
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 292..391
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 411..548
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 570..669
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 693..866
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 866 AA; 97493 MW; 651B32F10B0E60B8 CRC64;
MGACSSKAQH QTRDPEPREQ QAAQEQKSTG PSGAPNDAPA PAEAERKMSG SSATAPKGEM
PTASTGTPEQ QQQQQQQQQQ QQEQQQHPEH QQSEKQQQHG EEQQQERKPS QQQQNEEAAA
PHKHGGERKV QKAIKQQEDT QAEDARLLGH LEKREKTPSD LSLIRDSLST NLVCSSLNDA
EVEALANAVE FFTFKKGDVV TKQGESGSYF FIVHSGEFEV IVNDKVVNKI LTGQAFGEIS
LIHNSARTAT IKTLSEDAAL WGVQRQVFRE TLKQLSSRNF AENRQFLASV KFFEMLTEAQ
KNVITNALVV QSFQPGQAIV KEGEKGDVLY ILKSGKALVS IKNKEVRVLQ RGEYFGERAL
LYDEPRSATI TAEEPTVCVS IGRDLLDRVL GNLQHVLFRN IMLEALQQSK VFASFPTEQL
SRLIGSVVVK DYPENYIILD RENRTRASAS ALFSAQGVRF FFVLEGEVSV FAYKDKSSSS
SSSSSSSSSS SSAEGEMELH LIDTLKRGQA FGDEYVLSPN KPFAHCVKSN GPTKLALLTA
SALTATLGGQ DIDETLDYNN KLAITKKMYI FRYLSEQQTQ TLIKAFKTVR YTQGESIIRE
GEIGSRFFII KLGEVVILKG EKRVRTLGRH DYFGERALLH DERRSATVAA NSPEVDLWVV
DKDVFLQIVK GPMLTHLEER IRMQDTKVEF KDLNVVRVVG RGTFGTVKLV QHIPTQMRYA
LKCVSRKSVV ALNQQDHIRL EREIMAENDH PFIIRLALNQ QDHIRLEREI MAENDHPFII
RLGRGLGVGS GLAALNHQDP IRLEREIMAE SDHPFIIRLA LNQQDHIRLE REIMAENDHP
FIIRLGFRVW EWGRGWQLKV NKTTFD
//
