ID   Q0RSN5_FRAAA            Unreviewed;       740 AA.
AC   Q0RSN5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027};
DE            EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027};
GN   OrderedLocusNames=FRAAL0753 {ECO:0000313|EMBL:CAJ59423.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59423.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ59423.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45986 / CECT 9034 / ACN14a
RC   {ECO:0000313|Proteomes:UP000000657};
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; CT573213; CAJ59423.1; -; Genomic_DNA.
DR   RefSeq; WP_011601993.1; NC_008278.1.
DR   AlphaFoldDB; Q0RSN5; -.
DR   STRING; 326424.FRAAL0753; -.
DR   KEGG; fal:FRAAL0753; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_018811_0_0_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; IPR036116; FN3_sf.
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:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PROSITE-ProRule:PRU00159};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}.
FT   DOMAIN          15..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          298..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..368
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..427
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10027"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   740 AA;  77298 MW;  A858CC10F2DB5C72 CRC64;
     MAAVPVGNRV VAGRYRLVAR LGAGAMGTVW RAFDSVLETE AALKEIEFAG GVAGAERADR
     VERALREARH AAKLRGHPHV VTILDVVLEH GLPWIVMELV PSRSLFEVVR DDGPLPGAEV
     ARIGIAMLDA LVAARDHGIV HRDVKPSNVL IGTDGRVVLT DFGIATGDGD PTLTVTGVLG
     TPLYMAPERL DNRPATFEAD LFSLGGTLYY AVEGHPPFER DSFGAMLAAI LLHPPAPTRR
     AGALGPVLDG LLAKDPAQRL TPARARELLE QAARSRPQPG VGRVDALSWH LRYSAPPGGG
     SAAPGRFTGS LPEAPAAPGS LRAASPTGAG GPPGGVDDCD EATRVAGRTS HQPPPGLPPT
     RFPEPPDTPG VAGPRATSAV APDPGDAEAL PRPTEPAMPT EPAMAAEPAM PTEPAMAAEP
     AMPTKPAIGT GPAMPAEPAM DRPAAPAELT AVEQDGAVLL RWAPSVTPGA SYRVSRVLAD
     PSAPNGRRER SLGITTGTEL FDAGAPRGVP HWHEVVAMVT GAAGRLRSTP VRTPTRTLLP
     PVTALRASMS DNAVALSWRP MPERDEVMIE RTFAETSPLS GAKRRFRGTA GYFLDEDTAP
     GAVYRYRVWV AGSDSSDALA PSGAAEVVVR VVARPRPVLD LEARTTLGGT VLRWTTVPGA
     IVRIYATEAP EQAGLAGTGP FGPADHEVGV GSLEGRARLV GESRRGRLVD RQATDTVVYT
     PITIAEDRAV IGAAVSHSEL
//