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Database: UniProt
Entry: C6X7L2_METGS
LinkDB: C6X7L2_METGS
Original site: C6X7L2_METGS 
ID   C6X7L2_METGS            Unreviewed;       295 AA.
AC   C6X7L2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Msip34_0005 {ECO:0000313|EMBL:ACT49254.1};
OS   Methylovorus glucosotrophus (strain SIP3-4).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylovorus.
OX   NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49254.1, ECO:0000313|Proteomes:UP000002743};
RN   [1] {ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT   "Complete sequence of chromosome of Methylovorus sp. SIP3-4.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACT49254.1, ECO:0000313|Proteomes:UP000002743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT49254.1,
RC   ECO:0000313|Proteomes:UP000002743};
RX   PubMed=21622745; DOI=10.1128/JB.00404-11;
RA   Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA   Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA   Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT   "Genomes of three methylotrophs from a single niche uncover genetic and
RT   metabolic divergence of Methylophilaceae.";
RL   J. Bacteriol. 193:3757-3764(2011).
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}.
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DR   EMBL; CP001674; ACT49254.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6X7L2; -.
DR   STRING; 582744.Msip34_0005; -.
DR   KEGG; mei:Msip34_0005; -.
DR   eggNOG; COG1718; Bacteria.
DR   HOGENOM; CLU_047558_0_0_4; -.
DR   Proteomes; UP000002743; Chromosome.
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; IPR000687; RIO_kinase.
DR   InterPro; IPR018935; RIO_kinase_CS.
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; PS01245; RIO1; 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   Reference proteome {ECO:0000313|Proteomes:UP000002743};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..235
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          274..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  32709 MW;  9E88845FB6550225 CRC64;
     MMGPMKPPKR LEPLIEDGLI DEVLRQLMSG KEATVYVVRC GDDVRCAKVY KEADKRSFRQ
     SVDYTEGRKV KSSRQARAMG KGSRYGRKLQ EEAWQSAEVD ALYRLAAAGV RVPQPYNFYE
     GVLLMELVTD AAGHAAPRLN DVEFTEQEAL QHHQSLLVDV IRMLNAGIVH GDLSEFNILL
     GIDGPVIIDL PQAVNAAGNN HASSMLERDV DNLAAYFGRF APSLLGTQYG KEIWSLYAHG
     DLSTESSLSG QVAPDAIPVD LKSVLRVIDD VRKEEEKKQA RATETPAHKI RPQHS
//
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