ID   Q2JF75_FRACC            Unreviewed;       695 AA.
AC   Q2JF75;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ABD10067.1};
GN   OrderedLocusNames=Francci3_0683 {ECO:0000313|EMBL:ABD10067.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD10067.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD10067.1, 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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP000249; ABD10067.1; -; Genomic_DNA.
DR   RefSeq; WP_011435136.1; NZ_JENI01000002.1.
DR   AlphaFoldDB; Q2JF75; -.
DR   STRING; 106370.Francci3_0683; -.
DR   KEGG; fra:Francci3_0683; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 3218230at2; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.40.1000.10; Mog1/PsbP, alpha/beta/alpha sandwich; 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; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 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}; Kinase {ECO:0000313|EMBL:ABD10067.1};
KW   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:0000313|EMBL:ABD10067.1};
KW   Transferase {ECO:0000313|EMBL:ABD10067.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        475..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          282..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   695 AA;  73631 MW;  5104087E2D02414E CRC64;
     MAGESPDNPG SARAVTLVGG RYRLDGVIGR GGFGVVHRAT DELLQRVVAV KEVRLPLGEN
     ADERGLTRER VLREARAAGR LHHPGAVAVL DVIDDGELPW IIMEYVDGRS LATIINDRGP
     LPVEETCRIG ISLAYALEAA HRLGVVHRDV KPSNVLVTAD GRARLTDFGI AVSQGDPRLT
     STGMVMGSPA YLPPERARGD AGSAAGDRWG LGATLFTTVE GYPPFTGGDP ISVLAALVQG
     RRQPFRLAGP LIPVIDDLMA PHEASRPPLT VVRRRLREIV ERDAVRRPSR PSRPTRPRSS
     TRTTSPAARA IPTTPAESAT EAVPSGDVTG FPETEVRSET SAVSGISAVP APVAALTTPD
     TETRQDTETR QEATPSRTPR SRPTGPLERM HSIDRMRALG GIPARARLIG RGHGNGLTGG
     DVELANLFAT AAPASPPSTA RLRPAPDGPA GIEPAGIGPA EDPPRDPGAG DRRRVTIAVA
     TLVALVAAAI IGIVIVVTGG PDDRSRDTSA NQTGGISSPT GAGGSALADP AAARDPVARE
     TTPVTGPPGW VSYVDPTAGW SVAYPSDWQR REGPGGPGNV DFVDPATRSF LRVGSVRQAN
     TSAIGDWQRN EAGFRQSVRD YRQIRLAPSD GGDGTNQADW EFGYRGSDGV MVHVLNRGAI
     RNGHGYALYW HTREDLWLQD QPLMRQLFAT FRPGP
//