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Database: UniProt
Entry: A0A1C3PGI1_9ACTN
LinkDB: A0A1C3PGI1_9ACTN
Original site: A0A1C3PGI1_9ACTN 
ID   A0A1C3PGI1_9ACTN        Unreviewed;       849 AA.
AC   A0A1C3PGI1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=FDG2_6221 {ECO:0000313|EMBL:SBW28941.1};
OS   Candidatus Protofrankia californiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Protofrankia.
OX   NCBI_TaxID=1839754 {ECO:0000313|EMBL:SBW28941.1, ECO:0000313|Proteomes:UP000199013};
RN   [1] {ECO:0000313|Proteomes:UP000199013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wibberg D.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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; FLUV01002568; SBW28941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C3PGI1; -.
DR   Proteomes; UP000199013; Unassembled WGS sequence.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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:SBW28941.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199013};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:SBW28941.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          261..511
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   849 AA;  89598 MW;  8A60C7BD91C3E59B CRC64;
     MSTSRSGGGP LPVSGGPSND GAPCSQPGCD GTIEDGYCDV CGLLPAPAVP GQPDAGNRPV
     PNQLLRRMTA GQPSGAAASG GVARPFPAVP VGDGAPCAQP DCTGTLDEGY CDICGLAATS
     PASGQDLPER DQASIGAQAS PPAAGGRSTS AMSIGALQSS GTGPGSPRRS RRRRRSGSIP
     SRSRLGAGIV SVPDVTVLDP ASMVLADPQV PERSRHCAIC NEPVGRARSD TPGLLEGFCP
     KCRHPFSFVP KLAAGDVVGQ YEIAGCLAFG GQGWVYLARD RGVAENFWVV LKGLLNTHDP
     QATAAAIAER RFLASVDHSN IVKIFSFVEW QGSGYIVMEY VGGMSLLKLL KQRWEAAGGR
     SDPLPVTQAI AYILGILPAF GYLHRQGLVY CDFKPDNVML SGDSLKLIDL GAVHRIGDPG
     LSYATPGYRA PEVATAGPSV ASDLFTIGRS LATLLLDFRG NTTTYSYTIP PQDAHEVLAR
     HDCLHRFLLR ATATDPDARF ASADEMSDEL LGVLREIVAV EEGRPNPAPS LRFGSEAHLT
     GENPDGSVAG PPWSILPTCR PDPEDPAAAT LAALPDVEPE QLTKLLSTMS PADRTGPATP
     GTHLHLARAW MEAGQASRAQ ALLTTVANDD PYQWRTDWYR GLLALTAGDA QAARDFFDKV
     YSALPGELAP KLALALATET ADPATSARMF DVVSRTDPTF TSASFGLARV RLRAGDMRGA
     IEAWQRVPRA SAAYVYARTR IIRAMVDPAG RPGRAELAEA SGNLDVLDAD PGARADLART
     ILEVALKALE AGTLQPGDDV VVAGRPLRVR DVRSGLEQVY RDLARLTTTR PQRVAMVEAA
     NRVRPWTLV
//
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