ID   Q0RHH0_FRAAA            Unreviewed;       654 AA.
AC   Q0RHH0;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Putative serine-threonine protein kinase {ECO:0000313|EMBL:CAJ63057.1};
DE            EC=2.7.11.1 {ECO:0000313|EMBL:CAJ63057.1};
GN   OrderedLocusNames=FRAAL4415 {ECO:0000313|EMBL:CAJ63057.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63057.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ63057.1, 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};
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; CT573213; CAJ63057.1; -; Genomic_DNA.
DR   RefSeq; WP_011605538.1; NC_008278.1.
DR   AlphaFoldDB; Q0RHH0; -.
DR   STRING; 326424.FRAAL4415; -.
DR   KEGG; fal:FRAAL4415; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   OrthoDB; 3217681at2; -.
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; 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; IPR025971; LppP/LprE.
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; PF14041; Lipoprotein_21; 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:CAJ63057.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Transferase {ECO:0000313|EMBL:CAJ63057.1}.
FT   DOMAIN          16..265
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          269..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          635..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..523
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   654 AA;  67035 MW;  69503AC7A0508BA3 CRC64;
     MLTPLTSDDP RRIGPFRLAN RIGAGGMGVV YLGFGDDGKP VAVKVPSAGL ADNPEFRSRF
     RHEVDAARRV RGSSVATVLD ADLTGERPWM ATEYVEGRSL ADAVATRGEL DDRLVHGLAI
     GLADALVAIH AAGVVHRDLK PANILLAWDG PKVIDFGIAR AGDSTSHTRT GMLIGTLVWM
     APEQLRGERA GPPADIFAWG ACVAFAAAGR PPFRGERAEA VGMQILTAEP DLDGLPPDLV
     GVVRAALEKE PARRPTASEL LRRLVGRDVR SPADSDEASE TALAQVWSLP PTPPQGAGPL
     GGARDAGYGP PGGQPQRATG GYPDPTLRDP RSAYDAPPAY GNRAGYGNQA GYGNQAGYDN
     RPGYDSRAGY DQAGYDQAGY GAAPPRAGGP GYDDRVSEPG GRRGTAPYAD QYAAGHGGAG
     RRADGGWDGA PGGGRGSGDG RRGAVIAVAV LIALLLGGGI AAAVALSSGG GGGDDNVATP
     PVGTTQDAGG TAGATATGGP APTTGAASPP SSSPTPSPTP SASPSPATLS TDDAAALVRS
     KGYEPDMSTY QEDRQLSVVI GTAPASGDTP RQLAYVFADG QFRGTDTSAP SAHVTVKSQR
     NDHEVVLRYD TYDPQDPIGS PSGHADVRFR WNGSAFSTLD PIPSNDPNAT GSRR
//