ID U3LNN3_9TRYP Unreviewed; 507 AA.
AC U3LNN3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
OS Paratrypanosoma confusum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Paratrypanosoma.
OX NCBI_TaxID=1470209 {ECO:0000313|EMBL:AGG11489.1};
RN [1] {ECO:0000313|EMBL:AGG11489.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CUL13 {ECO:0000313|EMBL:AGG11489.1};
RX PubMed=24012313; DOI=10.1016/j.cub.2013.07.045;
RA Flegontov P., Votypka J., Skalicky T., Logacheva M.D., Penin A.A.,
RA Tanifuji G., Onodera N.T., Kondrashov A.S., Volf P., Archibald J.M.,
RA Lukes J.;
RT "Paratrypanosoma is a novel early-branching trypanosomatid.";
RL Curr. Biol. 23:1787-1793(2013).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KC534720; AGG11489.1; -; Genomic_DNA.
DR AlphaFoldDB; U3LNN3; -.
DR VEuPathDB; TriTrypDB:PCON_0025820; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF01163; RIO1; 1.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..295
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 322..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 507
FT /evidence="ECO:0000313|EMBL:AGG11489.1"
SQ SEQUENCE 507 AA; 57205 MW; A627574BD59E09F6 CRC64;
MVKLDVSLIR FLEPEDFRVL TALEMTMRNH EVAPTALVER IAQLPHGGCR KRLNNLLRHK
IIHHENTMYD GYSMKYAAYD FLALHTLSKR GTVVGVGSRI GCGKESDIIH VEDENGNECV
MKLQRLGRCS FRSVTRNRDY KGGGRTRRGE SWFYLSRLAA QKEYAFMQIL YENGFPVPKP
IDQNRHSIVM EYVTSTLLNN ITEMDQAAKV YERCIALIVR LAEHGLIHGD FNEFNLLITD
DYQVIMLDFP QMVSTDHRNA VELFNRDVRN ISNFFQRRFR LTKILEPELT RDVTRKGHLD
REALASGSFT HRQQQELEQM MERARVDEED EEDEEDEEEE HGVAAGNQAT VTVGNSFVSL
NGTDGNAPDG SVAADSADVG EHGGATVAGK RVSWDPSVAE HGEAGSRSGD EGDSSGRSSG
SDEEAEGDDA AGEGLRSHGH RVREYNPNLT SDGTVNLHHI RTRVRQSLRH NDNREFSRTL
HRNTQKGRHK RKIQRQLKGA GGGGFFD
//
