ID W8P532_9EURY Unreviewed; 258 AA.
AC W8P532;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BD01_0951 {ECO:0000313|EMBL:AHL22570.1};
OS Thermococcus nautili.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=195522 {ECO:0000313|EMBL:AHL22570.1, ECO:0000313|Proteomes:UP000019434};
RN [1] {ECO:0000313|EMBL:AHL22570.1, ECO:0000313|Proteomes:UP000019434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30-1 {ECO:0000313|EMBL:AHL22570.1,
RC ECO:0000313|Proteomes:UP000019434};
RA Oberto J., Gaudin M., Cossu M., Gorlas A., Slesarev A., Marguet E.,
RA Forterre P.;
RT "Genome Sequence of an Hyperthermophilic Archaeon, Thermococcus nautili 30-
RT 1, producing viral vesicles.";
RL Submitted (FEB-2014) 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}.
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DR EMBL; CP007264; AHL22570.1; -; Genomic_DNA.
DR RefSeq; WP_042690580.1; NZ_OX281345.1.
DR AlphaFoldDB; W8P532; -.
DR STRING; 195522.BD01_0951; -.
DR GeneID; 82171372; -.
DR KEGG; tnu:BD01_0951; -.
DR eggNOG; arCOG01180; Archaea.
DR HOGENOM; CLU_018693_3_3_2; -.
DR OrthoDB; 31344at2157; -.
DR Proteomes; UP000019434; Chromosome.
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; 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 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:AHL22570.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AHL22570.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..257
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 258 AA; 30748 MW; 988187A54736DCE3 CRC64;
MREEAIEREV EEILGLRDKR EKDSELYKIA NEVFDRTTKE TLAYLHRRGK IEELYGVIST
GKEANVFAGV DAEGNKIAVK IYRTYTTEFR RIWEYLAADP RIGYLPKDMR KLVFVWTRRE
FKNLQRAIKY AVRVPEPVIF RNNVLVMEFI GDEMPAPRLK DVERELERSD FEELYDYLIG
VIERLWKRGD MVHGDLSEYN VLLWDGPVVI DWSQATVRRN RMSVELLKRD LRNVTSYFAR
KGVEVEDYEV KLRELIER
//
