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Database: UniProt
Entry: A0A1X0NZG1_9TRYP
LinkDB: A0A1X0NZG1_9TRYP
Original site: A0A1X0NZG1_9TRYP 
ID   A0A1X0NZG1_9TRYP        Unreviewed;       554 AA.
AC   A0A1X0NZG1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, 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=TM35_000091270 {ECO:0000313|EMBL:ORC90077.1};
OS   Trypanosoma theileri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=67003 {ECO:0000313|EMBL:ORC90077.1, ECO:0000313|Proteomes:UP000192257};
RN   [1] {ECO:0000313|EMBL:ORC90077.1, ECO:0000313|Proteomes:UP000192257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Edinburgh {ECO:0000313|EMBL:ORC90077.1};
RA   Kelly S., Ivens A., Mott A., O'Neill E., Emms D., Macleod O., Voorheis P.,
RA   Matthews J., Matthews K., Carrington M.;
RT   "An alternative strategy for trypanosome survival in the mammalian
RT   bloodstream revealed through genome and transcriptome analysis of the
RT   ubiquitous bovine parasite Trypanosoma (Megatrypanum) theileri.";
RL   Submitted (MAR-2017) 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}.
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:ORC90077.1}.
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DR   EMBL; NBCO01000009; ORC90077.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0NZG1; -.
DR   STRING; 67003.A0A1X0NZG1; -.
DR   VEuPathDB; TriTrypDB:TM35_000091270; -.
DR   OrthoDB; 5481355at2759; -.
DR   Proteomes; UP000192257; 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   CDD; cd05147; RIO1_euk; 1.
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, ECO:0000313|EMBL:ORC90077.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192257};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          135..372
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          452..554
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..493
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  62692 MW;  39339B43EB97DA41 CRC64;
     MTEMEKDLDG LLQYMAPGST LDDIVGDSES EDEAALYDVV QGKRTTTARV VLGSATGANT
     QKEVTSLSKV QPVQHTTGHA SVLRRIRVDD FYADVSAFSG GGGGASKVNQ RVLNDLREMT
     MSNRLTSMQS SHEVDRSERA TVENVMDPRT RLILYKLVNS GQLREINGCV STGKEANVYY
     AVAGDGSDAA VKVFKTSILV FKDRDKYVAG EFRFQRYCKS NPRKMVRTWA EKEARNLNRL
     QDGGVLAPAV KLLRQHVLVM EFLGEDGWPA PRLKEVRFPS AAALDRCYLD ICCTMRKMYA
     RCRLIHGDLS EYNLLLYRGR VVVIDVSQSV ENDHPHAMDF LRRDIVNVDA FFRSKGHQKL
     FSLQDLYRFI TAPPAARGWQ RCEGPDNAEE IREYLLELRE SREKEGILPV NSEQAKIDEQ
     VFLNIAVPRS LGEIADHKAP NAEIAPFVAE MTADSQKKQK NQKHRHHDDN NNDEEEEEEE
     DDDDEDEDDE RSSNHNDGDE VVKKESGKEG AKPAPKIIAN MTKEERKEHH RAVKEANRER
     RANKKKVKAV KKKK
//
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