ID   Q2JF76_FRACC            Unreviewed;       674 AA.
AC   Q2JF76;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABD10066.1};
GN   OrderedLocusNames=Francci3_0682 {ECO:0000313|EMBL:ABD10066.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD10066.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD10066.1, 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; ABD10066.1; -; Genomic_DNA.
DR   RefSeq; WP_011435135.1; NZ_LRTJ01000019.1.
DR   AlphaFoldDB; Q2JF76; -.
DR   STRING; 106370.Francci3_0682; -.
DR   KEGG; fra:Francci3_0682; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 9762169at2; -.
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; 1.10.510.10; 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; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
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   Kinase {ECO:0000313|EMBL:ABD10066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABD10066.1};
KW   Transferase {ECO:0000313|EMBL:ABD10066.1}.
FT   DOMAIN          24..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          289..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..580
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..644
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  69207 MW;  CEE771E6F36EEAC8 CRC64;
     MAKSASVPPD TSRHGTPRYV AQRYRLDTPI GRGGAGVVWR GEDELLQRPV AIKEILVPMA
     GAQNERDAIR ARVLREARAL ARLHSPAIVS VYDVVEEHQR HWIIMELVDA DSLGDVIRNQ
     GPLPFDQVAA IGLALTDALA AAHSAGVLHR DVKPGNVLLG RDGRVRLTDF GIAATEGDVT
     LTGTGALVGS PAYIAPERVR GSSGTPASDL WGLGATLYSA VEGQPPFEGP ETYAVLTAVV
     EGRRRAFRLA GPLRNLLSDL MDRPAEERPD VTEIRRRLIP IARNANPVPA SVMHARPRTD
     EETDASSVDV GLENLDDPAE PAAGAGPAAD SRSGSSGGVA GTAGVQAGEA ASAAVGDQGA
     VPGPANRPAS AAAPPVPADR DVTVDPLLNP LGGAAVAAAG AAGSRTGRRE PDRAGPSNRV
     IPPDRTTPQN RAAPPGRTRP DPDHDAPTSI GLNSVAGPSV DDDVTRIGAV TPVSATSDLD
     LFDDDNHAAG LLPLGEARRR AEPARHDGHG RGPGDPQRRR QRTIAVVAGA AMLVMGAAIA
     LTVGLTSGGS TPGPNDVTAQ QTTPPPIATI ASSPPAVTSR SAASEVVAPD SPRYTPRPRP
     SSSATPTTTP TTETPTPTPQ PSTQVQTSPP PTQTPPPRVT PSPSRTAPAS PGGTTPPVVS
     TTAPAPTGTT TFVP
//