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Database: UniProt
Entry: A0A1G9A1H9_9EURY
LinkDB: A0A1G9A1H9_9EURY
Original site: A0A1G9A1H9_9EURY 
ID   A0A1G9A1H9_9EURY        Unreviewed;       303 AA.
AC   A0A1G9A1H9;
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=SAMN05216226_1482 {ECO:0000313|EMBL:SDK21206.1};
OS   Halovenus aranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halovenus.
OX   NCBI_TaxID=890420 {ECO:0000313|EMBL:SDK21206.1, ECO:0000313|Proteomes:UP000198856};
RN   [1] {ECO:0000313|EMBL:SDK21206.1, ECO:0000313|Proteomes:UP000198856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M10015 {ECO:0000313|EMBL:SDK21206.1,
RC   ECO:0000313|Proteomes:UP000198856};
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; FNFC01000048; SDK21206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9A1H9; -.
DR   STRING; 890420.SAMN05216226_1482; -.
DR   OrthoDB; 50101at2157; -.
DR   Proteomes; UP000198856; 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; IPR000719; Prot_kinase_dom.
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.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDK21206.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198856};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:SDK21206.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          94..303
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   303 AA;  34916 MW;  B88AF6E989E28906 CRC64;
     MVRNVADEMA DLEAEDFYLL SGIEHGMRFS EYVNREKLPE FSRLTAEDVE YRLDRCERRG
     LVERKTIQYE GFRLTFEGYD ALALHTFAER ETVEGMGSSL GVGKESDVYE VQSYQPFALK
     FHREGYTEFR EVNREREYTA DREHVSWMYT ARKAAENEYG ALEALYPDVS VPRPVDHNRH
     AIVMERLDGV ELERAALESQ QVVPIMELIL SEMATAYEAG YVHADMSEYN LFVDTDGITI
     FDWPQAVPAA HENSDDLLGR DVENVVGYFQ RKYPGKVDVV DTDSIADAII DGSFERVDEY
     MED
//
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