CDPK6_PLABA
ID CDPK6_PLABA Reviewed; 1482 AA.
AC A0A509ALV6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Calcium-dependent protein kinase 6 {ECO:0000303|PubMed:18005753};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P62344};
GN Name=CDPK6 {ECO:0000303|PubMed:18005753};
GN ORFNames=PB001122.01.0 {ECO:0000303|PubMed:18005753},
GN PBANKA_0925500 {ECO:0000312|EMBL:VUC55795.1};
OS Plasmodium berghei (strain Anka).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN [1] {ECO:0000312|Proteomes:UP000074855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA Janse C.J.;
RT "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT expression.";
RL BMC Biol. 12:86-86(2014).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18005753; DOI=10.1016/j.chom.2007.10.002;
RA Coppi A., Tewari R., Bishop J.R., Bennett B.L., Lawrence R., Esko J.D.,
RA Billker O., Sinnis P.;
RT "Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites
RT to stop migrating and productively invade host cells.";
RL Cell Host Microbe 2:316-327(2007).
CC -!- FUNCTION: Calcium-dependent protein kinase which acts as a sensor and
CC effector of intracellular Ca(2+) levels (By similarity). In
CC sporozoites, probably involved in the secretion of the cysteine
CC protease that cleaves circumsporozoite protein CSP, thereby exposing
CC CSP TSR domain, which binds with high affinity to highly sulfated
CC heparan sulfate proteoglycans (HSPGs), resulting in productive invasion
CC of the host hepatocytes (PubMed:18005753).
CC {ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:18005753}.
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:0000250|UniProtKB:P62344};
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:0000250|UniProtKB:P62344};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P62344};
CC -!- ACTIVITY REGULATION: Activated by calcium.
CC {ECO:0000250|UniProtKB:P62344}.
CC -!- DOMAIN: The EF-hand domains 1, 4 and 6 appear to lack a functional
CC calcium binding site. {ECO:0000305}.
CC -!- DOMAIN: It is unclear if CDPK6 has the junction domain (J domain) found
CC in other CDPKs. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Sporozoites display enhanced migratory activity
CC and are less infective for host hepatocytes (PubMed:18005753). Severe
CC decrease in circumsporozoite protein CSP proteolytic cleavage upon
CC sporozoite contact with host hepatocytes (PubMed:18005753).
CC {ECO:0000269|PubMed:18005753}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000305}.
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; LK023124; VUC55795.1; -; Genomic_DNA.
DR SMR; A0A509ALV6; -.
DR STRING; 5823.A0A509ALV6; -.
DR VEuPathDB; PlasmoDB:PBANKA_0925500; -.
DR OMA; VTPFYIK; -.
DR Proteomes; UP000074855; Chromosome 9.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1482
FT /note="Calcium-dependent protein kinase 6"
FT /id="PRO_0000455604"
FT DOMAIN 931..966
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 972..1007
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1043..1295
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1338..1373
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1376..1406
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1407..1442
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 1468..1482
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 250..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 989
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 991
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 996
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1049..1057
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1072
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1424
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 1482 AA; 177394 MW; C797EA7BA9227221 CRC64;
MVLELLKNNY ERNDEHYYNE KVENNTSKHK KKKKKKKKHI LVEESEKYDR NIDSENNEEA
YNAYELIKTK PNNIYEEKYD FSFQNLDKKC LREKNNMRES YRNSKDIIQY GTNENDIFTE
DMLENDNFDD DSFVEDDTMD YKTYNSYTKP EFNLFSKYST ESKKKNIMNN KKHSKIEDFY
KKYKNNSEYS KQANEHDASI IQFLNNNKKS VDCGKMKDIN FKKNDSQNYS ESNKYKNEFF
KNYNYDNKYT NNYAHDNNQD SNSYYYADEN EPKDNHEEDN DTGDTYADNE EDEDNRDDND
DYSQYNQCEV ESDTNQIRPN EKRYNESIKH INDSNLKINK ELLLKRETYT KRDNIFYIKK
DIIPYKKEHN NNRFSLYDSS KNNNEHNNNY EIKFMNYKKD SEKEGEQWLK NIKKEKDEEF
LKKYMYENAL KKTHSSKDLQ FNRLDDEKNI LHHDINVDNK MVRLDKYERS NIRDMRNKTN
KCNMLRHDTA EFNKIRRKDE INNYSEYANK CLAGNIYEED DSYILKRNEL GHKELKVIDN
PILNINPDDK KKPNIKSFLD KIKYRKNNEL FLKNEHEKYV GIQETNKKDK IKMKFADILH
TKNFSNFFHR GKNSIAKSLS PNNDKKNTSF NNEVFNLNIL GKNDKNSDYK QYNINCSPYD
HENTSFHPSV REETKYYENK ESRKRLDYNC DEDNYIENSI QRYHENNIDY NSINIERTIN
LREDIKYNEF LNKPDKINSE NFSNNFNDNK QKSLKNDDSN KIRDTNKLYY HDHLENTMRS
NYIQKEYTEK ISDILESNSN NMRKFINKMD YYTKKYEQNL YKNDEDIYTK ENKFPDSRKE
FYNKSDSPMK VTDGIKDSQY ENYNRIKYKL KMKQEKQDKE DETDINIDKK LSRKMIENNK
LKEENESNDE LIVTPFYIKS KIDKVLKNSE IFERSARATF KQFDVKNKNF LHFSEIESLI
QKLCYNLELP PVDKKILSIV YKDYDSSKNN CMNYMDFRQM YWDLLKQIKK KYYPTKNFKI
KRNCIISRKK LQGYDYSSIY NYLSFKKILG CGAFGEVHLV EDNICKLYKV VKILKKKKMK
NIKVNEEINV LIYLDHPNII KIFDVYESVN CTYIVMELCE GGELMNKIKK PQIFSETYIK
NIMFQILCAI AYMHSNNIAH KDLKPENILF KTDGYDTLKI IDFGLAELIN KSEGISKTAA
GTVLYMAPEV FKKKFTIKCD IWSAGVIMYF LFTKSLPFTG NTYEEVKQNI FNSEPDYQFL
KLKMSKPALH LLKLMLEKDY SRRPMAAVLL HHPWFQGYFD PIDILPSTLN NIKSYMKHSN
IRNVIVNIMA HELCVINNHV KYINDIFLKI DSNHNGSLSH REIYNVLSNA GVKKWDINRI
IQALDVNDKG CITYTEFIAG CYRWKNIDST FLKAAFNKID KDEDGYISKS DLATLVHDNG
VNNKDIENFF ISVHSIKKNI TKDKKINKIS FEDFKDYMLS TF
