ID A0A1U7NZ48_9DEIO Unreviewed; 294 AA.
AC A0A1U7NZ48;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=BOO71_0006616 {ECO:0000313|EMBL:OLV18189.1};
OS Deinococcus marmoris.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV18189.1, ECO:0000313|Proteomes:UP000186607};
RN [1] {ECO:0000313|EMBL:OLV18189.1, ECO:0000313|Proteomes:UP000186607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV18189.1,
RC ECO:0000313|Proteomes:UP000186607};
RA Kim J.H., Oh H.-M.;
RT "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL Submitted (JAN-2017) 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:OLV18189.1}.
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; MSTI01000074; OLV18189.1; -; Genomic_DNA.
DR RefSeq; WP_075832368.1; NZ_MSTI01000074.1.
DR AlphaFoldDB; A0A1U7NZ48; -.
DR STRING; 249408.BOO71_0006616; -.
DR OrthoDB; 9795258at2; -.
DR Proteomes; UP000186607; Unassembled WGS sequence.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..280
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
SQ SEQUENCE 294 AA; 33115 MW; F03B7DAFFE5B5B3E CRC64;
MNARWLDTEL EGADITPERR SKFKKKKLLG RRRLDGLTAE DPERIADDTI RRLIDTGHIT
EIVAELKSGK EATAYVARGP RGSVLVKLYR EMEARSFKND AVYREGNVIL DARAERAIQG
RTRKGLEMLQ ADWVCAEYAH LWTLWQAGLN VPEPLVGPNV KVCAATVPAV LMRLIGTEDE
VAPRLSEARL TPIEAQSAWK QAVHGLADML RLGYAHGDYS TYNLLWWENT VIIIDFPQLT
TRQNPNFQQL LGRDAQSLAT SFRKHGIQTD GDATLREVQR LARGKGPEPR IVLP
//
