ID A0A1H6HNZ0_9EURY Unreviewed; 304 AA.
AC A0A1H6HNZ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN05192561_101210 {ECO:0000313|EMBL:SEH37539.1};
OS Halopenitus malekzadehii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halopenitus.
OX NCBI_TaxID=1267564 {ECO:0000313|EMBL:SEH37539.1, ECO:0000313|Proteomes:UP000199215};
RN [1] {ECO:0000313|EMBL:SEH37539.1, ECO:0000313|Proteomes:UP000199215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10418 {ECO:0000313|EMBL:SEH37539.1,
RC ECO:0000313|Proteomes:UP000199215};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNWU01000001; SEH37539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6HNZ0; -.
DR STRING; 1267564.SAMN05192561_101210; -.
DR OrthoDB; 50101at2157; -.
DR Proteomes; UP000199215; 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 CDD; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
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 Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEH37539.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199215};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:SEH37539.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..288
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 304 AA; 35085 MW; AA757FC5972B6407 CRC64;
MVRNIAGLMA DLEPEDFYLL SGVEQGMRFS EWVRRDKLPE YSELTAEEVD YRIDRCLDEE
LIERKTIQYE GYQLTFEGYD ALALRTFAER DTVEGIGSPL GVGKESDVYE ARSFKPLALK
FHREGYTNFR EVMKEREYTA DRQHVSWLYT ARQAAEREYE ALETLYPDVS VPRPIDWNRH
AIVMDKFEGV ELARAKLDAE QVVGVLDLVL AELTTAYEDG WVHADMSEHN VAIAESGITI
FDWPQAVPTD HENAREFLER DIDNLTRYFA RKYPHQTPDS VSISAIADAI EDGSFETVRA
FEEV
//