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Database: UniProt
Entry: A0A2M9E6I0_9GAMM
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ID   A0A2M9E6I0_9GAMM        Unreviewed;       285 AA.
AC   A0A2M9E6I0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=CO641_07845 {ECO:0000313|EMBL:PJJ99452.1};
OS   Xanthomonadaceae bacterium NML91-0213.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae.
OX   NCBI_TaxID=2032582 {ECO:0000313|EMBL:PJJ99452.1, ECO:0000313|Proteomes:UP000229012};
RN   [1] {ECO:0000313|EMBL:PJJ99452.1, ECO:0000313|Proteomes:UP000229012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML91-0213 {ECO:0000313|EMBL:PJJ99452.1,
RC   ECO:0000313|Proteomes:UP000229012};
RA   Bernier A.-M., Bernard K.;
RT   "Zoonotically transmitted species of Xanthomonadaceae : Genome sequencing
RT   and assembly.";
RL   Submitted (SEP-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:PJJ99452.1}.
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DR   EMBL; NWQL01000002; PJJ99452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9E6I0; -.
DR   OrthoDB; 9795258at2; -.
DR   Proteomes; UP000229012; 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   CDD; cd05145; RIO1_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR048148; Prot_kin_PA4780.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR000687; RIO_kinase.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   NCBIfam; NF041645; prot_kin_PA4780; 1.
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.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PJJ99452.1};
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          5..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          60..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31689 MW;  BB246502A61AE1F4 CRC64;
     MKTPASLLTL LEEGVIDEVI RPLKSGKEAA VYVVRSGDDV RCAKVYKDMA HRSFQKRVQY
     QEGRKSRGSR EARAVATGSR YGRRQQEAEW KNAEVDALYQ LREAGVRVPE PHGFFHGVLV
     MELVTDDAGF SAPRLGEVEL TPEQAREFHA VLVRQVVRML CCGLIHGDLS AYNVLVGPDG
     PVVIDFPQVV SAAGNNAART MLLRDVNNLT ATLGRWAPEL LDTWYGEEMW ALFEAGTLQP
     DTELSGQFTF DESTIDLDGV RDAINDAREL ALIRQQGRDA QDDDD
//
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