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Database: UniProt
Entry: A0A2Z4FMG4_9DELT
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Original site: A0A2Z4FMG4_9DELT 
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}.
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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
//
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