ID A0A0A1E1F1_STRER Unreviewed; 565 AA.
AC A0A0A1E1F1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
GN Name=riok-3 {ECO:0000313|EMBL:AIY22524.1};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|EMBL:AIY22524.1};
RN [1] {ECO:0000313|EMBL:AIY22524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UPD {ECO:0000313|EMBL:AIY22524.1};
RA Yuan W., Liu Y., Lok J.B., Stolzfus J.D., Gasser R.B., Lei W., Fang R.,
RA Zhao J., Hu M.;
RT "Exploring features and function of Ss-riok-3, an enigmatic kinase gene
RT from Strongyloides stercoralis.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SSTP_0000897800.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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 ECO:0000256|PIRNR:PIRNR038146};
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 ECO:0000256|PIRNR:PIRNR038146};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR038146};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC ECO:0000256|PIRNR:PIRNR038146}.
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DR EMBL; KM434338; AIY22524.1; -; Genomic_DNA.
DR WBParaSite; SSTP_0000897800.1; SSTP_0000897800.1; SSTP_0000897800.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05145; RIO1_like; 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 InterPro; IPR017406; Ser/Thr_kinase_Rio3.
DR PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF01163; RIO1; 1.
DR PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 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:0000256|PIRNR:PIRNR038146};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR038146};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR038146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038146}.
FT DOMAIN 286..516
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 32..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 65566 MW; 59092A54E22D6242 CRC64;
MMDLEEIDSD LAGALEEEEL KLALEMQKKW DLQKNEDSSP SSCPWKKNIP PSTTKLSDIM
SEEIANKINT EKDDCINVVS ETPATVTLPN VVEEEMDPDL KLALELQKQF DAEVSLDDTD
FEEAKKLQKI FDEEVAQIYD KDHSLDISEA KKLQHEWDME VLNKESPKSI TFGMTRYKFS
HDDEIDDYEA LLDEYDEEDI KEKSWLKKYE KKDNFIGDND NVKNDCNFTT KHDTELSKIR
NADKTMNFAI GMNIGDCSDE KISNKVFNKL RQYSKDEIKR HFKIKDKAEK STYEQGMDED
ARLIIFKLIQ RKELDTVEGI VASGKESIVL HAKKEDWNFA IKVYKKTLSE FKNRNEYVKD
DFRFKNPRHV LKVWSLKEFL NLRRLKKAQI NAPEPLYVKK NVLVMRMIGE DKPALKLKDV
VFQDEESKEL AYQKVENIIC EMYKNCKLVH GDLSEFNLLY NKGIIYVIDV SQAMDLSHPN
SLVFLLRDIE NILNFFNTTG TPNLPSSGIV FEKVTGIPID PTKSVAVQVE QFEADNRNIH
LRDDKAKPCN AEVRAMDEDE CNNRL
//
