ID   Q0RSE8_FRAAA            Unreviewed;       654 AA.
AC   Q0RSE8;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CAJ59515.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:CAJ59515.1};
GN   OrderedLocusNames=FRAAL0847 {ECO:0000313|EMBL:CAJ59515.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ59515.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ59515.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {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=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; CT573213; CAJ59515.1; -; Genomic_DNA.
DR   RefSeq; WP_011602081.1; NC_008278.1.
DR   AlphaFoldDB; Q0RSE8; -.
DR   STRING; 326424.FRAAL0847; -.
DR   KEGG; fal:FRAAL0847; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_419063_0_0_11; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAJ59515.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:CAJ59515.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ59515.1}.
FT   DOMAIN          64..338
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  70623 MW;  6225CE8B4013B986 CRC64;
     MTRLDPAAPA GEDLTRVESA AAQQQDVTRI EPSSAEAAAL LGRAGGRPRI TLTDGLPGDL
     GVSWQLCGRL PAGGEASLLL VRPRAQAPGG RIRLVGDAGR RWVLKLYDPE RRPDDPEQQQ
     DRRAVWAAVS SVRHDHVQTL GETGTAGRHD YEISPYWPDG SLEDAVRATV DSHGETFEPW
     QPAAIRELVR QLDSALAALH AARLVHRDVK PGNILVRCRD PLHVVLGDYG IALLIDGAGR
     FTSRLGTPRF MPPEAHVAGL VWDSPARDYW ALGMVVLELT TGVRGYRRVH DAAWTRQLAG
     SGVDVSMVVD DRVRLLCQGL LTRDQADRWG HEEISRWLAG GTPAAGPADA EQVTLSLRAR
     RFQEPAGLAA AISADPVTWA TARRRFLPVD GGHDSGEGWR QLVEWLRAVR PRTAAGWSDE
     DLAELLDHRL RRTGISADVR LLHLVRWLDP AAPPSFRGIA ITPESLRSIA YDARGMIARG
     RQGQERQLVD QLRRERVLPL LAQPVLTAAD GRVVDPGPAV AAARRRLAAV AEGWDLAART
     LPRRAHDLAP APSGWPLPTW LPEWANATGL WLAADPTAAA AELSDVLGAE TARFGPWAPR
     AWSGLMRAVG VMPPGGSASP AASTGPQRRV RATGTSSRVR VRGTATGGES GVRG
//