ID A0A0N8KRC9_9EURY Unreviewed; 160 AA.
AC A0A0N8KRC9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=MPEBLZ_00813 {ECO:0000313|EMBL:KPQ44586.1};
OS Candidatus Methanoperedens sp. BLZ1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ44586.1, ECO:0000313|Proteomes:UP000050360};
RN [1] {ECO:0000313|EMBL:KPQ44586.1, ECO:0000313|Proteomes:UP000050360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA Welte C.U.;
RT "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT oxidation of methane by Methanoperedens-like archaea.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPQ44586.1}.
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DR EMBL; LKCM01000070; KPQ44586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8KRC9; -.
DR Proteomes; UP000050360; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR PANTHER; PTHR45852; SER/THR-PROTEIN KINASE RIO2; 1.
DR PANTHER; PTHR45852:SF1; SERINE_THREONINE-PROTEIN KINASE RIO2; 1.
DR Pfam; PF01163; RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KPQ44586.1};
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:KPQ44586.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..160
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 160 AA; 18722 MW; 5BECEFAC40F8FE2B CRC64;
MSFRHVRTKR ETIGERRHLS WLYAARLAAK KEYDALVALY PKVSVPEPID HNRHGIVMSK
ATGQQLAHTR LDEPDWYLDE ILRQVKNAYG LGIIHCDLSE FNIFVNPAGC EIIDWPQFIK
PTHPNAKELL RRDIDNVLSY FNRKYRIKRD IGEIINNIIT
//
