ID   Q0RIK4_FRAAA            Unreviewed;      1826 AA.
AC   Q0RIK4;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   SubName: Full=Putative two component sensor serine/threonine kinase {ECO:0000313|EMBL:CAJ62664.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:CAJ62664.1};
GN   OrderedLocusNames=FRAAL4022 {ECO:0000313|EMBL:CAJ62664.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ62664.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ62664.1, 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; CAJ62664.1; -; Genomic_DNA.
DR   RefSeq; WP_011605153.1; NC_008278.1.
DR   STRING; 326424.FRAAL4022; -.
DR   KEGG; fal:FRAAL4022; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3706; Bacteria.
DR   eggNOG; COG3899; Bacteria.
DR   HOGENOM; CLU_240134_0_0_11; -.
DR   OrthoDB; 5521237at2; -.
DR   Proteomes; UP000000657; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   PANTHER; PTHR45138:SF9; DIGUANYLATE CYCLASE DGCM-RELATED; 1.
DR   PANTHER; PTHR45138; REGULATORY COMPONENTS OF SENSORY TRANSDUCTION SYSTEM; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CAJ62664.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Transferase {ECO:0000313|EMBL:CAJ62664.1}.
FT   DOMAIN          9..265
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1694..1826
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   REGION          364..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1367..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..383
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1367..1394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1826 AA;  195786 MW;  D02D2C63C508B58C CRC64;
     MVQVEIPGVL IREELGRGAY SVVYRAEREG RNYAVKVPLR AVARDESVVR AFAREATILA
     CINHPNIARV RAAGHTADHP FLIMDMIEGE SLKARIAEGP LGIAEATRVA LDVASALSEA
     HRRGLVHQDV KPANIMIGPD GKATLLDFGL MTRAGGPPTD RAVGTVLFGA PEQTGMLRRP
     VEPRSDLYAL GAVLHTCLAG SPPFQAGDTA ELLRLHAVAT PRPLTQVRAD VPAELAAVVT
     RLLAKDPDDR FPSALDVVAA LTPLAPGVAG LARPPVDQAA AAGAGDPDLL VRGRHVGRRH
     ERALLRQAWA RCLTAQRRTP GERCTAGERS TAGQRWTVGE RGVVTVVGEA GAGKTLLIQD
     LLAAPGPAAT PPGTPPGPAD GPADGPAEAP GAGPVVLRGR CAANGSAPLA LLHDLIDGYL
     RGLASLPEPR RRELLARMVS AAGPDAALLA RVHPLFARAW DVDRPAREPE AGEPRLRAAA
     AGFLSRLAIR SHGLVIWVDD AHWLGPADRQ ILEDLTASTD PAPLLLVNAT RDPRLRVAAG
     SATSWDITLG PLDEHEVAEV IRDYLGEITD HAFARDVAVR SSGNPLAVAE YVRAVIDAGL
     VRPDWGRFVL DRTGLDSLPL PEEVLDLIRH RVHALSPTAA AVLGVAAVIG RGFDLALLTA
     ASGQSSAAIS MATAEAQARQ LAARGRDGTW SFVHDCVHEA LLSTMSPWER IIAHRRVVEA
     LDTVGPRGDG ASGDGASGDG HLYELARHAI AGRIAPQRRF RLASAAAAAA LATPAPYEAV
     ALYRAAQAAA DEAGVEPDAA FEEGFALASA RTLAPADART HFTRALRTQT DPRRRARALL
     ELAGVEFAEF RTAAALDYVH RGLAEIGRGL PANPAAMAAV SVGRWAAGMA CRRPWTGFGA
     ARGECRELHE IRCRLYEIGI LSEWISGRIG PMLAFMMSAV HPSQRLGSGE EYVRSHGCFV
     LVAADFRRAR VVERGVSRLR ELVADSDDPV LRAEAYLYTS AALLFAGRNV AGERDSEDTF
     RRAHRWIETF FFTSSYSILV RSLALRGHDR EAWASCETRP HGDRVQADLA ILRARLARTL
     RYPPVPHPGL GALDDESEVE RIRRYLICSD VAELEVEDDD FGPTFDAAVE MGDAVVQPSW
     RVPRFFRKFW ITRARGRLEQ ARAAPPGPVR ARRHRTAHAA LREARRAADY PPFAADLQVL
     RAVDRQLAGD HAGALDLVDA AERAARTLDL PRVRFDALLE RARCLRALDE PDRATTEAEL
     AATVAARYGW IGREHRVYRE FELTERGLSF AEASGAASPA TASRDRRRLD AVLQVSAAAG
     RETTPQAVAT VALDEIISIL GADRALLLLP DPADREGDSG RLRLYAERHA DQSDERAADG
     EPGGGRDGGP REGSDEPPRG IAMTVVERVQ AEQRPLVVTG TDEGAALGSQ SAVQYGLRSI
     LAAPVPIDGG RSGVIYVDSR VAKGLFNSDD ARILITLAKQ VGLSLNMAEA ARLQAVVAAE
     RRQRDLAETM RNVTLQATST LNTREILGRV LTAAGPVLPF DVAWVLTRVG GTVRISSTHG
     EVADGLVGTE LRPAPGGPIA RAFDHGEVLA TADAMALPGG GRGARSWLAA PVPLRESIEM
     VVVLASRTPD CYSETRIQIA QTIIDQVVIG YQNAWLFEKV QRLAATDQLT GLASRRHFLE
     RADHLYAAQA AAGRPVCAAM VDIDHFKRVN DAYGHLVGDE VLTEVARRIR RAFRDDDLIG
     RIGGEEFAVL MSGPVTTAES LGQRLRNALA RDPIDTSAGP LDIRLSVGLT ARSPADGSLR
     DLLARADAAL YEAKHGGRDR VAVQLR
//