ID   Q2J973_FRACC            Unreviewed;       730 AA.
AC   Q2J973;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Francci3_2811 {ECO:0000313|EMBL:ABD12169.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD12169.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD12169.1, ECO:0000313|Proteomes:UP000001937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3
RC   {ECO:0000313|Proteomes:UP000001937};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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};
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DR   EMBL; CP000249; ABD12169.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2J973; -.
DR   STRING; 106370.Francci3_2811; -.
DR   KEGG; fra:Francci3_2811; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG4783; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   PhylomeDB; Q2J973; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR031634; PknG_rubred.
DR   InterPro; IPR031636; PknG_TPR.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF16919; PknG_rubred; 1.
DR   Pfam; PF16918; PknG_TPR; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABD12169.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:ABD12169.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          104..369
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   730 AA;  78321 MW;  8BF3D356E399E72E CRC64;
     MNLPAPRVTA LPRRFPAPGA HRDPLRLPHL VGPPPGSTPP LLDAPSVPTG LRECAGCGAP
     VARPGHDEQD EQDESVALEG SCAGCGHRYS FTVKLRPGER VGRYTVHGVI AHGGLGWVYA
     ATDDNLGGDG VRAWVVLKGL LDAANPEARR IAEGERRILT TVSHPGIVKI LDYVTHHGED
     YIVMEYVPGV SLAGLAEVGV AGPDGRSAPP SAADVIRYLL RVLPALGHLH RLGLVYCDLK
     PENVMVTAED VKLIDLGGAR RLDDRVSGYL STPGYRAPEL DDDGERPAGI ARTAPTVTTD
     IFAVARTLAR LVLGRFPGFL GAYRHALPPR RAHAPLRDFE SLDRLLRRAT ATDPDQRFQS
     TTELADELVG VLYEIVARTE GPVPPLASRW FDAVGHPTGE AGPAGTPAWW EVLPDLRIDQ
     DDPWAPGLTA GSDEEPASLA TRLAAIVPRT TEVRLSLARA QIRAGQLHEA AGTLDDAAVE
     QPREWRVDWY RGLHALVGGR PAVAAAAFDR VYSRVPGELA PRLALATALA DVATTADTAD
     TADTADTAPE RDAARHRAAA LFDVVSTIDP STTSAAFGLA RCRTDPTDKI DAYLRVPPSS
     AAYTASRIRM IGVLVGLAAR PDRAASGSAA LHRAATILAD PRLDLGERRR AELHRDLFTA
     ALALVMTYPA AYPAADAPRP PTLLSRVMVE RDLRFGLAET YREMARLAGD RASRVRLVDQ
     ANRIRPRTLL
//