ID A5K0B0_PLAVS Unreviewed; 866 AA.
AC A5K0B0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PVX_124185 {ECO:0000313|EMBL:EDL47671.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL47671.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL47671.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL47671.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL47671.1}.
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DR EMBL; AAKM01000001; EDL47671.1; -; Genomic_DNA.
DR RefSeq; XP_001617398.1; XM_001617348.1.
DR AlphaFoldDB; A5K0B0; -.
DR STRING; 126793.A5K0B0; -.
DR EnsemblProtists; EDL47671; EDL47671; PVX_124185.
DR GeneID; 5476707; -.
DR KEGG; pvx:PVX_124185; -.
DR VEuPathDB; PlasmoDB:PVX_124185; -.
DR InParanoid; A5K0B0; -.
DR OMA; QWSEKEF; -.
DR PhylomeDB; A5K0B0; -.
DR Proteomes; UP000008333; Chromosome 14.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF2; SERINE_THREONINE-PROTEIN KINASE RIO1; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008333};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 54..475
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 118..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..866
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 99170 MW; 022861521E5FFD4C CRC64;
MKIRKGKVKT NERDYSYGGG FESYVYSKEV SNDVKSSLIE GEKLSNKFRN RGLTRDKRAT
VNTVLDNRTL LILKKLKDNM LNEIYGVVSS GKEAYVFNSH KYLSEEELRG VKQLLLRRRG
RDGQDSGEQD SGEQDSDGQH SDDQNGGDHH SEDHHSDDQH SDNQHSDDLH SSDLHRADRH
SDDLPGGGGA RRRVRFAHES LYKVYHLSRH FDEEGAQKRE EGEEVEEVEE GEEREEVEKG
EEMEEAQDAK DAKNAEGSAL DETYDIIDRM GEVAPEADEP NWDPFQNKKV AISFATKVYN
TSVLVFKKRS QYIEGEFRFR NAYTKNTNPR KMVKQWSEKE FRNLRRILIC GLRCPYPLVL
KSNVIVMSML GSLDSACPKM KDLILSPLKW KELYIECICI LRQLFCSCKL VHADFSEYNL
LYFYNHIYII DVSQSMEHDH PYSLEFLKRD CVNITNFFKK KIGTLQNDMH ESVGQLNGML
HGAKIDQEVS IKSTSGGRGE SASEITNGVN DTNCENGPAQ ENGQNPGDCK PSESFYSHVQ
ILPLKKLFDY IVSSSLPQDV TYFLERDKKE IHMDPSEITY LQIFGLIKNT TPIPKLNLRN
IKKNRTYFEK LKRATAYYVT KFSVQNQSHI KKHADRSQVE EQIFLSSWIP SHLNEIKDIR
TIEKDLKLLK KGKSMVSNFI SNNYHTERSK HAPKNNTSVE HNSLEGESHS DAATGAKNHI
TNGDCTVDTQ KEEIAESFTK TYAQKEDSND GDNGGDPFEQ GKETYKNGEH EGVGELSENR
SPKSLGKVAP SNNLPDAHKS NAANDENNFV NSEQEEEVKF KGIIPEGVTR KEWSKLVKEQ
NREKRKHKIP KYQKKKKKKK AHLKKK
//
