ID A0A183ICZ6_9BILA Unreviewed; 514 AA.
AC A0A183ICZ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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 ORFNames=SBAD_LOCUS1490 {ECO:0000313|EMBL:VDO94506.1};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000156101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0000156101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO94506.1, ECO:0000313|Proteomes:UP000270296}
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; UZAM01006843; VDO94506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183ICZ6; -.
DR WBParaSite; SBAD_0000156101-mRNA-1; SBAD_0000156101-mRNA-1; SBAD_0000156101.
DR Proteomes; UP000050793; Unplaced.
DR Proteomes; UP000270296; 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; 2.
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:UP000270296};
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 251..484
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 58240 MW; AFCD0313CF824E67 CRC64;
MSARATHNAW NVDETLSGCS IVNSFVDIMS EEKVRELQKE DTMNSQEPTT QPDAAKDCDK
KPMVSEDRCA DDHLLALMLQ NEYNHEHDEL LLREEKKFNG NDKVALSFEN YRPRKLVSDE
DSSEDDEDLR ESLNQKLDSF KKPSFGSHGV ILHNGKLVSK HDIVLCGRDN ASRLLEFPPD
ILTGDAVKID LQLPNRVYNS LKSHSMSQGK RRNRIHEKKD KSTTVSLLSP AVHRSSFVIP
PSDRAHLMLL QFEAYSRLEW AVDAKTRLVL YKMVNSGVLD SVSGIISTGK EAALFHALGG
TWKGKDLPKE CAIKVFKTTL NEFKNRSEYV QNDYRFRNPR KVMKVWAEKE LVNLNRLRRA
DIPCPEPIRL RNHLLLMSFI GEDGIPAPKL KEVDFDSEEL ASLYESCVAI MQKMFKDCGL
VHGDLSEFNI LYWKGDLWII DVAQAVDISH PRSLAFLARD CENITELKYD KKNPADCVLR
SVNNSAGSVD FPSEPHAETP PVIEALSDSA EVQN
//
