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Database: UniProt
Entry: A0A0N5D1R4_THECL
LinkDB: A0A0N5D1R4_THECL
Original site: A0A0N5D1R4_THECL 
ID   A0A0N5D1R4_THECL        Unreviewed;       569 AA.
AC   A0A0N5D1R4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
GN   ORFNames=TCLT_LOCUS6790 {ECO:0000313|EMBL:VDN04180.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000680101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000680101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN04180.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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         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; UYYF01004445; VDN04180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N5D1R4; -.
DR   STRING; 103827.A0A0N5D1R4; -.
DR   WBParaSite; TCLT_0000680101-mRNA-1; TCLT_0000680101-mRNA-1; TCLT_0000680101.
DR   OMA; HDPQLCA; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; 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   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:UP000276776};
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          218..454
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
SQ   SEQUENCE   569 AA;  66520 MW;  57A1B4ECB6313E1F CRC64;
     MSSGLKVKDS AWCKNEREVD EPVMSFAEIM SEELVDQLME EDARVLDPSI AQYGISSDEL
     SKCADDFELA RMLQEKFDLE YEMTVQSFKN KKTESKIQLG FKSYHSVCDS DEDCDEEISQ
     DDEDLKEIRR EIEKRNALHL GKVKDEFPSS GYVRNSLGNL ITKHDKEISE RRNSEKAMHL
     PIDFPTGNVI GEKLSNKVYN KLRSCSKADR KKNIRVKDKD EKATNEISLD KITRLVIYKF
     INAGLFDKVG NIIATGKESV VLHAMTHADG IKVLEEKHFA LKVYKMTLSE FKNRLEYVLD
     DYRFKNPRRV LRIWAEREYT NLKRMIRAGV KCPEPIRLRR HIMIMTFIGS NGVAARKLKD
     IEWRDQKTIY QAFLQAVIKM FTDCNLVHGD LSEFNMLYYE NHVYIIDVSQ AMDTSHPRAL
     FFLLRDINNV LEYFQKLNIE KLPSATEFFN DVTGLNMDPG ESLLLFPFIL MTPEQIYEKL
     NLYLLSILHD RYAPTLFQFY LLKQILMNFP NMHTYCSSRI VVDFKVEHFE KDNRSAQLRH
     DKTNPADMEL RLYDAEVSET YEDPAELYN
//
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