ID W0I1Y4_9EURY Unreviewed; 256 AA.
AC W0I1Y4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=TES1_0668 {ECO:0000313|EMBL:AHF80056.1};
OS Thermococcus paralvinellae.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=582419 {ECO:0000313|EMBL:AHF80056.1, ECO:0000313|Proteomes:UP000019027};
RN [1] {ECO:0000313|EMBL:AHF80056.1, ECO:0000313|Proteomes:UP000019027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES1 {ECO:0000313|EMBL:AHF80056.1,
RC ECO:0000313|Proteomes:UP000019027};
RX PubMed=25082851; DOI=10.1099/ijs.0.066100-0;
RA Hensley S.A., Jung J.H., Park C.S., Holden J.F.;
RT "Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov.
RT of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.";
RL Int. J. Syst. Evol. Microbiol. 64:3655-3659(2014).
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; CP006965; AHF80056.1; -; Genomic_DNA.
DR RefSeq; WP_042680253.1; NZ_CP006965.1.
DR AlphaFoldDB; W0I1Y4; -.
DR STRING; 582419.TES1_0668; -.
DR GeneID; 24907532; -.
DR KEGG; ths:TES1_0668; -.
DR HOGENOM; CLU_018693_3_3_2; -.
DR OrthoDB; 31344at2157; -.
DR Proteomes; UP000019027; 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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR008266; Tyr_kinase_AS.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 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:AHF80056.1};
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:AHF80056.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..256
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 256 AA; 30372 MW; B8334CEDE710D369 CRC64;
MDRLDREIAE ILGLDERREK DSELFKVFSE VFDKTTVETL SYFHRRGKIE QLLGVISTGK
EANVFAGVDS RGNKIAVKIY RTYTTEFRRI WEYLAADPRI GYLPKDIRKL VFVWTRREFK
NLQRAMKYAV RAPEPIAFRN NILIMEFIGD ENPAPRLKDV EKVLEKRDFE ELYEFSMNAI
ERLWKRGDMV HGDLSEYNIL IWEKPVIIDW SQATVKRNRM SLTLLYRDLR NIINYFGRKG
VAVDDLEEKF KELTGD
//
