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Database: UniProt
Entry: A3TGQ7_9MICO
LinkDB: A3TGQ7_9MICO
Original site: A3TGQ7_9MICO 
ID   A3TGQ7_9MICO            Unreviewed;       288 AA.
AC   A3TGQ7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 69.
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=JNB_07599 {ECO:0000313|EMBL:EAQ00017.1};
OS   Janibacter sp. HTCC2649.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=313589 {ECO:0000313|EMBL:EAQ00017.1, ECO:0000313|Proteomes:UP000005063};
RN   [1] {ECO:0000313|EMBL:EAQ00017.1, ECO:0000313|Proteomes:UP000005063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2649 {ECO:0000313|EMBL:EAQ00017.1,
RC   ECO:0000313|Proteomes:UP000005063};
RX   PubMed=21075932; DOI=10.1128/JB.01298-10;
RA   Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA   Vergin K.L., Giovannoni S.J.;
RT   "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL   J. Bacteriol. 193:584-585(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}.
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:EAQ00017.1}.
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DR   EMBL; AAMN01000001; EAQ00017.1; -; Genomic_DNA.
DR   RefSeq; WP_009775824.1; NZ_CH672413.1.
DR   AlphaFoldDB; A3TGQ7; -.
DR   STRING; 313589.JNB_07599; -.
DR   eggNOG; COG1718; Bacteria.
DR   HOGENOM; CLU_060067_0_0_11; -.
DR   Proteomes; UP000005063; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000005063};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..281
FT                   /note="RIO kinase"
FT                   /evidence="ECO:0000259|SMART:SM00090"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   288 AA;  32203 MW;  EA2053DC3B1ECFFA CRC64;
     MSFHDSTTES PLFATDTSPD APPEGERWSS WDGAMHGPTP RPDWVITALG AVEEDLGVLK
     TGKEADVHLI RRWLPDGSHH LALPGQSLDS LLAAKRYRGA ENRLFHRDGG YLEGRRVRKS
     REMRAMARRT EFGRSMIAGQ WAAAEFDALG RLWELGLPVP YPVQLNEAEM LMEFVGIGHT
     AAPRLVQTKP SPELLAELFE QFRQVVLTLA QEGWAHGDLS PYNVLVHDDR LVVIDWPQIV
     DVVGNPHGFE FLERDVRVMC DWFTRRGLTI DADLLFGDVA AMAAGSGW
//
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