ID A0A2Z4FMG4_9DELT Unreviewed; 282 AA.
AC A0A2Z4FMG4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=DFR33_103379 {ECO:0000313|EMBL:TDP76029.1}, DN745_11965
GN {ECO:0000313|EMBL:AWV90015.1};
OS Bradymonas sediminis.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV90015.1, ECO:0000313|Proteomes:UP000249799};
RN [1] {ECO:0000313|EMBL:AWV90015.1, ECO:0000313|Proteomes:UP000249799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA350 {ECO:0000313|EMBL:AWV90015.1,
RC ECO:0000313|Proteomes:UP000249799};
RA Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT fam. nov.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TDP76029.1, ECO:0000313|Proteomes:UP000294609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28820 {ECO:0000313|EMBL:TDP76029.1,
RC ECO:0000313|Proteomes:UP000294609};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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 ---------------------------------------------------------------------------
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; CP030032; AWV90015.1; -; Genomic_DNA.
DR EMBL; SNXT01000003; TDP76029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4FMG4; -.
DR KEGG; bsed:DN745_11965; -.
DR OrthoDB; 9795258at2; -.
DR Proteomes; UP000249799; Chromosome.
DR Proteomes; UP000294609; 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, ECO:0000313|EMBL:AWV90015.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000249799};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..233
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 54..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 32026 MW; F9A3B5A203DA27B3 CRC64;
MRIPARLRPL IEYGVITEVV RPLLSGKEAQ VYLVESGGEL RAAKVYKSTQ ERSFRHRSSY
TEGRKVRNSR DRRAMGKNSR YGREQQEAAW NTAEADMIRK LHRAGVRVPK PYDFVEGVLV
MECIQGPDGG VAPRISDCPF TREEGIEVCD QIIRQIVKML CAGVVHADMS VFNVLMADDG
PVVIDFPQSV SAASNPHARK ILLRDVANIT DALRFGRAPQ ALRYGYEMWD LYENGELDEN
SVLTGKYDVR QHQVDPDILM LEMQQVEEDE ALAEMDDEDF DY
//