ID U6G7J3_EIMAC Unreviewed; 1868 AA.
AC U6G7J3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=EF hand domain-containing protein, putative {ECO:0000313|EMBL:CDI76221.1};
GN ORFNames=EAH_00016810 {ECO:0000313|EMBL:CDI76221.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI76221.1};
RN [1] {ECO:0000313|EMBL:CDI76221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76221.1};
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:CDI76221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI76221.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; HG670337; CDI76221.1; -; Genomic_DNA.
DR RefSeq; XP_013253200.1; XM_013397746.1.
DR EnsemblProtists; CDI76221; CDI76221; EAH_00016810.
DR GeneID; 25269751; -.
DR VEuPathDB; ToxoDB:EAH_00016810; -.
DR OMA; ERTMACC; -.
DR OrthoDB; 102846at2759; -.
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; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141}.
FT DOMAIN 69..98
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 99..134
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1161..1261
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1269..1463
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 139..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1838..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1868 AA; 186593 MW; BCDAD459D3A922CD CRC64;
MGGQGSRYAL AGGSNLSREN LKNYLKKFDG DEVEVLKKVY KSLALRSEAP GIDKETFLRY
FPLPGLWGER LFQKFDYKGT GSVDLEEFLI GIAVCCRGTK SDRMFVLFQV FDLNNDGYIQ
KSELIAMLSN LPNLENYISV RPPDPAAEEQ QQQQLAPFED PEEQQLLQQQ RLQQQQHQET
TWTQVSSREG LDPVEEESDS SEASSVSDFS VAPLGYPAAA AAAAAVSAAA AAAGAAAAGA
AAAGAPEAGA AAAAAGAAAG ATAGVAAAAA APPPPPHAAA AAAASSLAAR KELDSEFQAP
AAAAAAPAAA APAAAPAAAP ATAAPASAAA ESAPAASAAA TPLLTAAGCS VSVTAPELGA
QQQQQQQQQQ QQQVEGVEVE KSGEEDDRNS SLLSAADCSS KAKKNPSPVA QLLIDIEKQQ
QLGPNQQPAV DVECVADKII EECEFVEHGR LSFPEFKTWL EHHPGILSMF TACLHEEVWG
LQGNALYRSS AARGNKGVMK TGSGEFNDPK GTRNGGIRQD QFQKVRRLFT GHHGGMPLQS
RVVSAAAKET FSSLGSKLSL IGSGDRGRGP TSLPVSTAAT AAAASAAAGS AAASGAGLAS
TAGSLTPVGG DTAAATPAAA AAVNAAAAAA GSLKAAAAAA AAAAAAAGVA AATAAAGTPA
KPVAEEARAQ QQQQQQQGAA GVALQQAGGA PVAASQGELL AAAAAPAQQH IPEAARPAAT
APGPAATGQA ASSTTGVSPA AAAPAAAAPS PTAAAAAAPA AAAAAPAAAT PPAAAAGGTQ
CISLPSVSRG ATPGAKLGER IGIAAATAAA APAAAAAGAA AAAGTPAARG TAGGAAGAAA
PTAESAGAAT TPAAATPAAA APAGATGTAA AAAAAPAAAA AAESSSRNPG SMKVCDFDRS
LRPDLDVHLL LKGQPTPLHP RQQQQQHQQQ QQQGDGDAES PAYVSDCGAE LGALPSVASL
SGTLGSLIRE HAAKEAGAAA AAAAAAAGEQ DLHSCPKCHR PLLLCPSCRG RSLQLCLLQG
QVVIECSNCS NQHEAAAAAT AAAAAASTTA TLASAASGPT AAAAAAAAAA AAVAGDAAST
PHRTQEGQQQ QSETADSAAA TDSTVAAAGA SKPPPSSSSS SSSSSSSSSN SGSVARRGVY
THCWECNWDF SRSTELLSVA ETSLDGVLLK KGKHLHQWQA RFYVLIDNML YYYKKKGDAK
PRGFMFLEGC FVETIPDAGA LRPHGIAIVH PRGDSVARRV LYAQSAQEQQ QWVDALRAST
RQQSLEHFYE VHEQLGQGKF SVVYRGVHKK TGEEVAIKVI DKGKINRHEK ELLRSEMVIL
RLLNHPNVIR LKEMVDTKET LYIVMELVRG GELFDLIHAN HHLPEVHVNR YVAPEVLSLE
GYNQQADLWS VGVITYLLLR GRLPFPINKH LGSPHFHQTY PLSFDGPLWR PVSSSAKDLI
TKMLSPIPQQ RITVEEALQH IWIRNPTAVI NEANKTDPFD HINPSVQPID PHALAAADGA
STFTIPNAHN RLAQQRAQQQ QAKTAAAAAP AAVAAAAAPA AAAAAAAAPA AVRATADAHE
KDSTGAVPAD AAKVAAATAA TAATAATHGA LAAANAGSTL AQPAAAAATA AAAATDATKA
AASAAQPAAA EENSKTKQPQ AAQPQGAAAA TAAAAVAGEQ HEAPAADRHT PATAAPAAGV
AAETAATAKE TAKAAAAAAH SAAAVAQAAA AAAALHAAAT DEAFAAVQRG PSGDSVGRKP
HQPEQQQQQQ QQQQQQQQQQ QQQQQQHHVP GVAPVRGAAA ASLTTPAATG GSTPMSATAA
TTAAAAAAAA TAAALQTSTA AAATHAATPT AAAATAAATA ATAAATSTQS TAAAAATLSP
QNTKKADP
//
