CDPK4_PLAF7
ID CDPK4_PLAF7 Reviewed; 528 AA.
AC Q8IBS5;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Calcium-dependent protein kinase 4 {ECO:0000303|PubMed:19307175};
DE EC=2.7.11.1 {ECO:0000269|PubMed:19307175, ECO:0000269|PubMed:19666141};
DE AltName: Full=PfCDPK4 {ECO:0000303|PubMed:19307175};
GN Name=CDPK4 {ECO:0000303|PubMed:19307175}; Synonyms=CPK4;
GN ORFNames=PF3D7_0717500;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RX PubMed=12368870; DOI=10.1038/nature01111;
RA Lasonder E., Ishihama Y., Andersen J.S., Vermunt A.M.W., Pain A.,
RA Sauerwein R.W., Eling W.M.C., Hall N., Waters A.P., Stunnenberg H.G.,
RA Mann M.;
RT "Analysis of the Plasmodium falciparum proteome by high-accuracy mass
RT spectrometry.";
RL Nature 419:537-542(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 219-SER-THR-220; THR-234;
RP 350-ASN--TYR-528; 350-ASN--LYS-379; 360-LEU--TYR-528; LEU-360 AND
RP 370-SER--TYR-528.
RX PubMed=19307175; DOI=10.1074/jbc.m900656200;
RA Ranjan R., Ahmed A., Gourinath S., Sharma P.;
RT "Dissection of mechanisms involved in the regulation of Plasmodium
RT falciparum calcium-dependent protein kinase 4.";
RL J. Biol. Chem. 284:15267-15276(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, INDUCTION, AND
RP MUTAGENESIS OF LYS-99.
RX PubMed=19666141; DOI=10.1016/j.parint.2009.08.001;
RA Kato K., Sudo A., Kobayashi K., Sugi T., Tohya Y., Akashi H.;
RT "Characterization of Plasmodium falciparum calcium-dependent protein kinase
RT 4.";
RL Parasitol. Int. 58:394-400(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20466936; DOI=10.1126/science.1188191;
RA Dvorin J.D., Martyn D.C., Patel S.D., Grimley J.S., Collins C.R.,
RA Hopp C.S., Bright A.T., Westenberger S., Winzeler E., Blackman M.J.,
RA Baker D.A., Wandless T.J., Duraisingh M.T.;
RT "A plant-like kinase in Plasmodium falciparum regulates parasite egress
RT from erythrocytes.";
RL Science 328:910-912(2010).
RN [7] {ECO:0007744|PDB:4QOX, ECO:0007744|PDB:4RGJ}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 10-528.
RA Wernimont A.K., Walker J.R., Hutchinson A., Seitova A., He H., Loppnau P.,
RA Neculai M., Amani M., Lin Y.H., Ravichandran M., Arrowsmith C.H.,
RA Edwards A.M., Bountra C., Hui R., Lovato D.V.;
RT "Apo crystal structure of CDPK4 from Plasmodium falciparum,
RT PF3D7_0717500.";
RL Submitted (SEP-2014) to the PDB data bank.
CC -!- FUNCTION: Calcium-dependent protein kinase which acts as a sensor and
CC effector of intracellular Ca(2+) levels probably in part downstream of
CC cGMP-activated PKG kinase (PubMed:19307175, PubMed:19666141). Plays a
CC central role in the host erythrocytes and hepatocytes infection cycles,
CC sexual reproduction and mosquito transmission of the parasite. During
CC the liver stage, involved in sporozoite motility and thus in sporozoite
CC invasion of host hepatocytes, probably together with CDPK1 and CDPK5.
CC Involved in merosome egress from host hepatocytes, probably together
CC with CDPK5. During the asexual blood stage, involved in merozoite
CC invasion of host erythrocytes and motility by stabilizing the inner
CC membrane complex, a structure below the plasma membrane which acts as
CC an anchor for the glidosome, an acto-myosin motor. Required for cell
CC cycle progression in the male gametocyte. During male gametogenesis in
CC the mosquito gut, required to initiate the first round of DNA
CC replication, probably by facilitating the assembly of the pre-
CC replicative MCM complex, to assemble the first mitotic spindle and, at
CC the end of gametogenesis, to initiate axoneme motility, cytokinesis and
CC subsequent exflagellation. For each of these steps, may phosphorylate
CC SOC1, SOC2 and SOC3, respectively. Together with CDPK1, regulates
CC ookinete gliding in the mosquito host midgut (By similarity).
CC {ECO:0000250|UniProtKB:P62345, ECO:0000269|PubMed:19307175,
CC ECO:0000269|PubMed:19666141}.
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:0000269|PubMed:19307175, ECO:0000269|PubMed:19666141};
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:0000269|PubMed:19307175,
CC ECO:0000269|PubMed:19666141};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19666141};
CC -!- ACTIVITY REGULATION: Activated by calcium (PubMed:19307175,
CC PubMed:19666141). Upon calcium binding to the EF-hand domains, the C-
CC terminus of the junction domain (J domain) undergoes a conformational
CC change which results in the dissociation of the pseudo-substrate
CC inhibitory motif from the catalytic domain (PubMed:19307175). This, in
CC turn, may facilitate the autophosphorylation of the activation loop at
CC Thr-234, which leads to the kinase activation (PubMed:19307175).
CC Intracellular calcium increase is triggered by xanthurenic acid (XA), a
CC small mosquito molecule that induces the differentiation of specialized
CC transmission stages, the gametocytes, into male and female gametes
CC (Probable). Activated by a decrease in temperature (20 degrees Celsius)
CC and an increase in pH (7.6) occurring when the parasite is ingested by
CC in the mosquito (PubMed:19666141). {ECO:0000269|PubMed:19307175,
CC ECO:0000269|PubMed:19666141, ECO:0000305|PubMed:19666141}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8 (at 20 degrees Celsius).
CC {ECO:0000269|PubMed:19666141};
CC Temperature dependence:
CC Optimum temperature is 20-30 degrees Celsius (at pH 7.6).
CC {ECO:0000269|PubMed:19666141};
CC -!- SUBUNIT: May interact with the pre-replication MCM complex prior male
CC gametogenesis activation. {ECO:0000250|UniProtKB:P62345}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62345}. Cell
CC membrane {ECO:0000269|PubMed:19307175}; Lipid-anchor
CC {ECO:0000303|PubMed:19307175}.
CC -!- DEVELOPMENTAL STAGE: Expressed in gametocytes (at protein level).
CC {ECO:0000269|PubMed:12368870, ECO:0000269|PubMed:19307175,
CC ECO:0000269|PubMed:19666141}.
CC -!- INDUCTION: Induced by xanthurenic acid (XA) and human serum.
CC {ECO:0000269|PubMed:19666141}.
CC -!- DOMAIN: The junction domain (J domain) is composed of 2 motifs that
CC maintain the kinase inactive (PubMed:19307175). The N-terminal
CC autoinhibitory motif acts as a pseudosubstrate inhibiting the catalytic
CC domain while the C-terminal motif binds the EF-hand domains
CC (PubMed:19307175). {ECO:0000269|PubMed:19307175}.
CC -!- PTM: Myristoylated; myristoylation may target it to different
CC subcellular compartments. During male gametogenesis, myristoylation is
CC required to initiate DNA replication but not for mitotic spindle
CC assembly or axoneme activation. {ECO:0000250|UniProtKB:P62345}.
CC -!- PTM: Not palmitoylated. {ECO:0000250|UniProtKB:P62345}.
CC -!- PTM: May be autophosphorylated on Thr-234 in vitro.
CC {ECO:0000269|PubMed:19307175, ECO:0000269|PubMed:19666141}.
CC -!- DISRUPTION PHENOTYPE: Replication in host erythrocytes is normal.
CC {ECO:0000269|PubMed:20466936}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL844506; CAD50923.1; -; Genomic_DNA.
DR RefSeq; XP_001349078.1; XM_001349042.1.
DR PDB; 4QOX; X-ray; 2.75 A; A=10-528.
DR PDB; 4RGJ; X-ray; 2.30 A; A=10-528.
DR PDBsum; 4QOX; -.
DR PDBsum; 4RGJ; -.
DR AlphaFoldDB; Q8IBS5; -.
DR SMR; Q8IBS5; -.
DR BioGRID; 1209973; 2.
DR IntAct; Q8IBS5; 2.
DR STRING; 5833.PF07_0072; -.
DR BindingDB; Q8IBS5; -.
DR ChEMBL; CHEMBL2169725; -.
DR DrugBank; DB11638; Artenimol.
DR PRIDE; Q8IBS5; -.
DR EnsemblProtists; CAD50923; CAD50923; PF3D7_0717500.
DR GeneID; 2655116; -.
DR KEGG; pfa:PF3D7_0717500; -.
DR VEuPathDB; PlasmoDB:PF3D7_0717500; -.
DR HOGENOM; CLU_000288_37_4_1; -.
DR InParanoid; Q8IBS5; -.
DR OMA; LEHEWIR; -.
DR PhylomeDB; Q8IBS5; -.
DR Reactome; R-PFA-5687128; MAPK6/MAPK4 signaling.
DR Proteomes; UP000001450; Chromosome 7.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:GeneDB.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IDA:GeneDB.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0003824; F:catalytic activity; IDA:GeneDB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR CDD; cd00051; EFh; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13499; EF-hand_7; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calcium; Cell membrane; Cytoplasm;
KW Developmental protein; Differentiation; Kinase; Lipoprotein; Magnesium;
KW Membrane; Metal-binding; Myristate; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..528
FT /note="Calcium-dependent protein kinase 4"
FT /id="PRO_0000085842"
FT DOMAIN 71..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 376..411
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 427..458
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 459..494
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 496..528
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..386
FT /note="J domain"
FT /evidence="ECO:0000269|PubMed:19307175"
FT MOTIF 350..358
FT /note="J domain autoinhibitory motif"
FT /evidence="ECO:0000269|PubMed:19307175"
FT MOTIF 359..368
FT /note="J domain EF-hand interaction motif"
FT /evidence="ECO:0000269|PubMed:19307175"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 400
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 512
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 517
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P62345"
FT MUTAGEN 99
FT /note="K->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:19666141"
FT MUTAGEN 219..220
FT /note="ST->AA: No effect on catalytic activity and auto-
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 234
FT /note="T->A: Loss of catalytic activity and auto-
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 350..528
FT /note="Missing: Constitutively active."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 350..379
FT /note="Missing: Partial loss of catalytic activity. Is
FT active in absence of calcium."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 360..528
FT /note="Missing: Loss of catalytic activity in absence or in
FT presence of calcium."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 360
FT /note="L->A: Partial loss of catalytic activity in presence
FT of calcium."
FT /evidence="ECO:0000269|PubMed:19307175"
FT MUTAGEN 370..528
FT /note="Missing: No effect on catalytic activity. Is active
FT in absence of calcium."
FT /evidence="ECO:0000269|PubMed:19307175"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4RGJ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4RGJ"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4RGJ"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:4QOX"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 251..265
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 299..308
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 348..388
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 398..412
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 418..432
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 445..471
FT /evidence="ECO:0007829|PDB:4RGJ"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:4QOX"
FT HELIX 481..490
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:4RGJ"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4RGJ"
FT HELIX 515..527
FT /evidence="ECO:0007829|PDB:4RGJ"
SQ SEQUENCE 528 AA; 60780 MW; 225E3C1F3DFDA3BA CRC64;
MGQEVSSVNN TKNEHHKTNK KSLKGGNERH EMKESSVGIS KKIVENSFNN SKLRPGMFIQ
NSNVVFNEQY KGIKILGKGS FGEVILSRDK HTGHEYAIKV ISKKHVKRKT DKESLLREVE
LLKMLDHINI MKLYEFFEDN NYYYLVSDVY TGGELFDEII SRKRFYEIDA ARIIKQILSG
ITYMHKNNVV HRDLKPENIL LETKNKEDMI IKIIDFGLST HFEYSKKMKD KIGTAYYIAP
DVLHGTYDEK CDIWSCGVIL YILLSGCPPF NGSNEYDILK KVEAGKYTFD LPQFKKISDK
AKDLIKKMLM YTSAVRISAR DALEHEWIKM MTSKDNLNID IPSLELSIAN IRQFQSTQKL
AQAALLYMGS KLTTIDETKE LTKIFKKMDK NGDGQLDRNE LIIGYKELLK LKGEDTSDLD
NAAIEYEVDQ ILNSIDLDQN GYIEYSEFLT VSIDRKLLLS TERLEKAFKL FDKDGSGKIS
ANELAQLFGL SDVSSECWKT VLKEVDQNND GEIDFKEFRD MLVKLCNY
