ID   Q2J4L1_FRACC            Unreviewed;       542 AA.
AC   Q2J4L1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=Francci3_4435 {ECO:0000313|EMBL:ABD13781.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD13781.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD13781.1, 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; ABD13781.1; -; Genomic_DNA.
DR   RefSeq; WP_011438789.1; NZ_JENI01000065.1.
DR   AlphaFoldDB; Q2J4L1; -.
DR   STRING; 106370.Francci3_4435; -.
DR   KEGG; fra:Francci3_4435; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 308915at2; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 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   Kinase {ECO:0000313|EMBL:ABD13781.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:ABD13781.1};
KW   Transferase {ECO:0000313|EMBL:ABD13781.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          29..288
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          294..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  55994 MW;  2CA38809291D59D8 CRC64;
     MNNSPGNPIS PSQPFAGAAS PNTVLDNRYR LNGRIAAGGM GEVWRGLDLT LGRPVAVKLL
     RPEYASDESF LVRFRGEARH AARLSHPGVA SVYDYGEVAT ADDYPTAYLV MELVEGEPLS
     AALHREKRLS PERTLDILGQ AADALQAAHA LGVVHRDVKP GNLLLRPDGA VKVTDFGIAR
     AVDAAPLTAT GIMMGTAYYV SPEQASGRPV TPASDVYSLG VVAYECLAGR RPFDDRNPIV
     VVMAHQQDTP PPLPTDIPYQ VRALVDSAMA KDPARRPSSA GAFARSAAGI RRSLWSPEPA
     RWPGAPDATA RHPGPGAVLP PAGAAARPPR STSRTRPPSW VAAPPPSGHT SGPGRTGASP
     DNAQAVPDGP EAMLGGPDVP ATALHSPPFG GPDTAYGGPE SAYGGSAYGT SDRGGPRDPG
     TAYHPGPPPW ARTPGGPPGP SGPDSPDDLR PGWEGRAARR HRPKAASRPA LPLPLLIILL
     ILTVVIVAFA TNRLFSGSNS ASNSATTPPR VVYPTAIGDE IVSGNAGSAI SGAGGATAGE
     YS
//