ID   Q2JFM7_FRACC            Unreviewed;       612 AA.
AC   Q2JFM7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027};
DE            EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027};
GN   OrderedLocusNames=Francci3_0531 {ECO:0000313|EMBL:ABD09915.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD09915.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD09915.1, 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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:ARBA00048679, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CP000249; ABD09915.1; -; Genomic_DNA.
DR   RefSeq; WP_011434991.1; NC_007777.1.
DR   AlphaFoldDB; Q2JFM7; -.
DR   STRING; 106370.Francci3_0531; -.
DR   KEGG; fra:Francci3_0531; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_6_11; -.
DR   OrthoDB; 3915799at2; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:TreeGrafter.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF34; SERINE_THREONINE-PROTEIN KINASE YBDM-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001937};
KW   Serine/threonine-protein kinase {ECO:0000256|PROSITE-ProRule:PRU00159,
KW   ECO:0000313|EMBL:ABD09915.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        548..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..281
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..378
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..398
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..480
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..507
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..526
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10027"
FT   BINDING         59
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   612 AA;  65252 MW;  0170504A4ECE97B2 CRC64;
     MTERSARRVS PIGGYPAEAP HPDDPTTIGV YQVVGRLGAG GMGTVFLAQD AAEKFVAIKV
     IRSDLAADPE FRARFRDEVA AARRVAPFCT AQVLDADPDA RRPYLVTEYI DGVRLDQAVT
     ESGPLPLSTL QGVAVGVASA LTAIHRAGIV HRDLKPSNVM LSYSGPRVID FGIARTLDMT
     KGRTQTGLVL GSVGWMAPEQ MEGAALGPAV DVFAWGLLIG YAATGGHPYG HGTYLEMSEK
     ILTGQPDLRA MPPDLTPIVR SALARDPRDR PSTENLLLTL LGERGRAGDA RDAATALLDG
     TWPRGRSTAG AGAAALAGGA GAGWPDPTHV ATPYEQRRWW ENEPRPLGGD RWWNDSARDR
     PPPAGPPVPP PALAPPPAAD RAAGPRHGVP RARRRRRGGF VQYDDEADGN GHRSGFDNSG
     EGGHPPPAPD ARPRHGGQPR VDSPHAGQPY PDQAHAGRPY AGRPYAGQPY AGRAAEAAPS
     PQAPARPRPV AQQRPPSAPA GPAPAPAPRV AEARPAPRGR APAPYAESVP RPRPRRRFRL
     RIPFKRTILF VLVVLLLLSA ADQIALMVDE QRQRLWNKVV TSVKDDTHDQ LDSLWNRVRD
     TFGGSSGGSS NG
//