ID I1XHB5_METNJ Unreviewed; 290 AA.
AC I1XHB5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=Q7A_942 {ECO:0000313|EMBL:AFI83784.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI83784.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI83784.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI83784.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
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; CP003390; AFI83784.1; -; Genomic_DNA.
DR AlphaFoldDB; I1XHB5; -.
DR STRING; 754476.Q7A_942; -.
DR KEGG; mej:Q7A_942; -.
DR PATRIC; fig|754476.3.peg.929; -.
DR eggNOG; COG1718; Bacteria.
DR HOGENOM; CLU_047558_0_0_6; -.
DR Proteomes; UP000009144; 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 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, ECO:0000313|EMBL:AFI83784.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AFI83784.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..242
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 32756 MW; B467406642DA59AB CRC64;
MSDKTRIMKI PKQIQPLVDD GLVDEVISRL MSGKEADVYV VKCGDEIRCA KVYKDAIKRS
FKKAVQYQEG RKVRNSRRGR AMEKGSKFGR QQQEETWQNA EVDALYLLAS AGVRVPQPYD
CLNGVLLMEL ITDEDGDVAP RLNDVSMSAE QAIEDHLMVM HSVKKMLCAG LVHGDLSEFN
VLVDAHGPVI IDLPQAVNAV ANNNAQAMLT RDVQNMTRYY AQFAPELRNT HFEKEIWSLF
ENGELLPDTE LTGQFEEDAQ AADVDGVMLE IKAILAEEQQ RQLWLRDKDD
//
