ID Q0RHQ2_FRAAA Unreviewed; 780 AA.
AC Q0RHQ2;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN OrderedLocusNames=FRAAL4330 {ECO:0000313|EMBL:CAJ62972.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ62972.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ62972.1, 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; CAJ62972.1; -; Genomic_DNA.
DR RefSeq; WP_011605455.1; NC_008278.1.
DR AlphaFoldDB; Q0RHQ2; -.
DR STRING; 326424.FRAAL4330; -.
DR KEGG; fal:FRAAL4330; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OMA; PREWRVD; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031634; PknG_rubred.
DR InterPro; IPR031636; PknG_TPR.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24363:SF0; SERINE/THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF16919; PknG_rubred; 1.
DR Pfam; PF16918; PknG_TPR; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CAJ62972.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:CAJ62972.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ62972.1}.
FT DOMAIN 166..431
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 82813 MW; 8852AEEC9BB18204 CRC64;
MAEDDATLPD GDHHEDRSDP PGDGRTGGAA GSARWLEPTE PTRARFTGSP RPGDDDGDED
GRERAVGVGA VPVPRTISSP RRGPAPGVPR DPLRLPRRIG PPPGATPPLL EAPSVPVGLR
ECAGCGAPVA RPGQSGTVAL EGTCGGCGHR YSFTVKLRPG ERVGRYTVHG VIAHGGLGWV
YAATDDNLGG DDVQAWVVLK GLLDAANPEA RRIAEGERRI LTTVSHPAIV KILDYVTHEG
EDYIVMEYVP GISLTGLADT GPPGPDGRPA PPPPADVLRY LLRVLPALGH LHRMGLVYCD
FKPDNVMVTA SGVKLIDLGG ARRLDDMVSG YLSTPGYRAP ELDDDGERPG GVARAAPSVT
TDTFAVARTL ARLVLGRFPG FVDAYRHVLP PRRAHPPLRE FESLDRLLRR ATATDPQRRF
QSVTELADEL VGVLYEIVAR TEGPVPPLAS RWFDAAGHPT GETGPTGPPA AWEVLPDLRV
DQDDPRAPAL TAGPEEDPAA LAARLAAIVP VTTEVRLALA RARIRAGQLG EAARALDAAA
AAAPREWRVD WYRGLAALVA RRPGQAAAAF DRVYSQVPGE LAPRLALATA LADVATTAGS
ARERQAARER AGELFDVVGA IDPGVTSAAF GLARCRTDPT GKIDAYQRVP RSSSAYTASR
ARMIGVLVAR VPGTDSPATG SAALLRAAAL LADPLLDLGE RRRAELRRDI FTAALTLVPA
GHPPPGSPRP PTLLGRPMVE RELRFGLAET YREMARLTPD RASRVRLVDQ ANHARPRTLT
//