ID W4J1U5_PLAFP Unreviewed; 1886 AA.
AC W4J1U5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=PFUGPA_02043 {ECO:0000313|EMBL:ETW55999.1};
OS Plasmodium falciparum (isolate Palo Alto / Uganda).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW55999.1, ECO:0000313|Proteomes:UP000019103};
RN [1] {ECO:0000313|EMBL:ETW55999.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW55999.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW55999.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW55999.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KI927329; ETW55999.1; -; Genomic_DNA.
DR EnsemblProtists; ETW55999; ETW55999; PFUGPA_02043.
DR OMA; HNENFAG; -.
DR Proteomes; UP000019103; Unassembled WGS sequence.
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:UP000019103};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..459
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 721..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1886 AA; 223146 MW; C0D65CA279411A3B CRC64;
MEQYENYEEI KVLSNDVQTS IIQGEKLTNK FRNRGLTRDK RATINSVLDN RTLIILRKLK
ENVYNDIYGV ISSGKEAYVF NAIKYINDEE LNSLKNIFIK HLEKYKNNIN IKINNNENMI
YNQMENIHDQ CSDVHNYMSQ DSERDINNYE QSEDTHFYNN DKYYNGFFNK NKNNKGDQSG
DDTNNDIYND IYNDIYDDLY NDIYNDIYND DDEKQNFSKR EDTVLEEKNK SNNTYEQTFD
IIKEMNDISF YDNKKSQISH IINILDKTKE KKGIALATKV YNTSILVFKK RSQYIEGEFR
FRNAYTKNTN PRKMVKQWAE KEFRNLRRIL ICGLRCPYPL VLRSNVIVMS MIGYIDNACP
KMKDLNFDIL KWKELYIECI CILRFLFFNC KLVHADFSEY NLLYFCNHIY IIDVSQSMEH
DHPYSLEFLK RDCLNITNFF KKKIGTIVQQ TQPTNLYTQR NEQNVENKTN VDINRVQTNY
TNEHVEGYNV EGYNVEGYNV EGYNVEGYNV EGYNVEGHNV EGHNVEGHNV EGHNVEGYDD
TNTIDDKTSH LLPQKDFSKL LDVPDAGFYE NVEILPLKVL FDFIVSSSLP DDIVYFIEND
KKKISLNPYE IIYLQIFGLI KNTTPIPKLN LKKIQKNRIY FEKLKRATCY YVTKFTNEKK
KKLEKYSKKH SQKYAHKDEV EEQVFLSSWI PSYLNEIKDI RTIEKDLKLL KKGKSIVNNF
ISNQNNDHKY QNNTKEEDPK NKKKEQNKEQ NKEQKEIYNK NEVHIDSHIF YEERNQMDVN
KINDTLHISN EHSFEENIKQ YDHEYKETHQ EEIIIEQDKN EENEIMSNSN TLLNIIQTNS
CDHLSNSVDS DTSNIDDESD SCEQNEDEEN YSSVHEQEEV KFKGIIPDGI TRKEWCKLFP
ISNSKGICYR QRTTECVKEN NGITKFFLKD LIKESSLKNN EDVTKKDIED KEKKNVQQNE
KNQSFNVSYT WETDTISGLR FINVLNKKDK KKLGFQCIYC RDRQLFKKKS SVLYHMVTFN
HGLKNSVIDE LKVHIHNSCN IYVYINERTS DDRLNFINNF NTEKQITIEK ENIVEKNVTK
DYNLIKLEIE FVSTMNLLTF EELKELFLFF FPEQVMSIDE NIIKENIIEK FLLNINSLSE
NYSRIIEKEY HVPDYSKDLN LITLSEYLNN LRNVKLEKKT NFYCEESVDS ELAINETITS
QNKEREEKKM CANQEKNIVE TSSENILSKD ITEEQKVYIS EENRNDKINE EDQVHIKSVE
KKDNAAVVEA KNMNNLVIEQ NIEKVIVEEK KKRKRKEKIN IDENKHILIN INDYNILRHD
DQLFISLTTN KNKPQKEKTI IGKENFFIIN NNISNDEMNK QDNNNENINT TSTSNINDNN
STKSNNNKSN FHNIYNSASS NNYYEHVKNV NGSYNSNIHT NSNNNNLLQK INAEQYMIID
NNNNNNYYND DENKKKHPMN ILLNLNNKEK KKRSRNEGSK ETKMNVSKKV RNMKNKNNLD
IHFLYEKTNE NNVDNQNKNE HLYEQKLINY ESIIGIDDIT ENNDLKEEHN SISSIPNYNI
ISTTSNTCDM QEEFYNNMNI NINRCLYKQT ITNKNNKDDN NNNNNDNNND NNNNDNNNNI
NVEETKEQGN MKNSYNTKNN EEDTNILNNI HILNNIHNDN KIQRILQIHV DDDLKDNKKN
ISEKNVEESV LACSQNKSVK MVNYKDKNMI DKSRNKSVIK KKEINNKNIL KNITKINTLN
SNTKGRKKKA NIIETQKDNI LKKNLKKNYS YKITIDKEKK KIINYNKRNN RRKNIIKTTS
SINNYYKNQH IDNIINKKKN IKLYKKKNKQ TNIIHKKCYK KVNEHICTSS IKEIKQLCNL
SNENIIPHNE NLSCTRSYRL SRYIKT
//
