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Database: UniProt
Entry: A0A1H6HNZ0_9EURY
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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}.
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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
//
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