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Database: UniProt
Entry: A0A0L7K7K2_PLAFX
LinkDB: A0A0L7K7K2_PLAFX
Original site: A0A0L7K7K2_PLAFX 
ID   A0A0L7K7K2_PLAFX        Unreviewed;       957 AA.
AC   A0A0L7K7K2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=PFHG_01018 {ECO:0000313|EMBL:KOB59262.1};
OS   Plasmodium falciparum (isolate HB3).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=137071 {ECO:0000313|EMBL:KOB59262.1, ECO:0000313|Proteomes:UP000054289};
RN   [1] {ECO:0000313|EMBL:KOB59262.1, ECO:0000313|Proteomes:UP000054289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB3 {ECO:0000313|EMBL:KOB59262.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA   Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA   Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "Annotation of Plasmodium falciparum HB3.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Kodira C., Zeng Q., Oleary S., Yandava C., Alvarado L., Wirth D.,
RA   Volkman S., Hartl D.;
RT   "The genome sequence of the Plasmodium falciparum HB3.";
RL   Submitted (MAR-2006) 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; CH671933; KOB59262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7K7K2; -.
DR   EnsemblProtists; KOB59262; KOB59262; PFHG_01018.
DR   OMA; QWSEKEF; -.
DR   Proteomes; UP000054289; 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; SSF141571; Pentapeptide repeat-like; 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:UP000054289};
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          745..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        881..895
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..957
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  113610 MW;  3E0B1DF11B1F6A6C 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 VDINRVIMLK
     GYNVEGYNVE GYNVEGYNVE GYNVEGHNVE GHNVEGYNVE GYNVEGYNVE GYNVEGYNVE
     GYNVEGHNVE GHNVEGHNVE GYDDTNTIDD KTSHLLPQKD FSKLLDVPDA GFYENVEILP
     LKVLFDFIVS SSLPDDIVYF IENDKKKISL NPYEIIYLQI FGLIKNTTPI PKLNLKKIQK
     NRIYFEKLKR ATCYYVTKFT NEKKKKLEKY SKKHSQKYAH KDEVEEQVFL SSWIPSYLNE
     IKDIRTIEKD LKLLKKGKSI VNNFISNQNN DHKYQNNTKE EDPKNKKKEQ NKEQNKEQNK
     EQKEIYNKNE VHIDSHIFYE ERNQMDVNKI NDTLHISNEH SFEENIKQYD HEYKETHQEE
     IIIEQDKNEE NEIMSNSNTL LNIIQTNSCD HLSNSVDSDT SNIDDESDSC EQNEDEENYS
     SVHEQEEVKF KGIIPDGITR KEWCKLVKEQ NREKRKHKIP KYQKKKKKKK THIKKKK
//
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