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Database: UniProt
Entry: A0A143Q4Y5_9NOCA
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ID   A0A143Q4Y5_9NOCA        Unreviewed;       785 AA.
AC   A0A143Q4Y5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknG {ECO:0000313|EMBL:AMY17512.1};
GN   ORFNames=A3Q40_00097 {ECO:0000313|EMBL:AMY17512.1};
OS   Rhodococcus sp. PBTS 1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY17512.1, ECO:0000313|Proteomes:UP000076180};
RN   [1] {ECO:0000313|EMBL:AMY17512.1, ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY17512.1,
RC   ECO:0000313|Proteomes:UP000076180};
RX   PubMed=27284129;
RA   Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL   Genome Announc. 4:0-0(2016).
RN   [2] {ECO:0000313|Proteomes:UP000076180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA   Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT   "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT   Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL   Submitted (APR-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; CP015219; AMY17512.1; -; Genomic_DNA.
DR   RefSeq; WP_068099335.1; NZ_CP015219.1.
DR   AlphaFoldDB; A0A143Q4Y5; -.
DR   STRING; 1653478.A3Q40_00097; -.
DR   KEGG; rhu:A3Q40_00097; -.
DR   PATRIC; fig|1653478.3.peg.99; -.
DR   Proteomes; UP000076180; 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-EC.
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   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:AMY17512.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076180};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMY17512.1}.
FT   DOMAIN          160..445
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   785 AA;  85015 MW;  14ACFBB5B5844F27 CRC64;
     MTRVEGEGEA AETRAAAPDF EGTRAAAPDF EGTRAAAPDF EGTRAAVPDF EGTRAAAPDT
     DSSRRTTAPR PSRRVRTGSR RRLGGGLVEL PRIPEVDPAT AIMSDPRVPE SKRFCWKCAA
     PVGRSVDGRP ANPTGDCTRC GTHFDFAPLL DPGEMVAGQY EVQGCIAHGG LGWIYLAIDR
     NVSDRWVVLK GLLHFGNAEA HAVAMAERQF LAEVTHPGIV KIYNFVEHPR KAPAGSTSGD
     PADTTGYIVM EYVGGRTLRQ IMTDDPSRTK LPVEQAIAYL LEVMPAMAYL HSIGLAYNDL
     KPENIMVSQD QIKLIDLGAV SPLEGYGYLY GTAGYQAPEI VRTGPTVASE IYTVGRTLAV
     LTLDIASEKG RYVDGLPDDA PVLQEYEFYD RLLRRAVHLD PSARFRSADE LASQLSGILR
     EILSQQTGKT HPGLSTVFSP QRTTFGTDEQ VAVTDVYIDG RHRVARLDPR DVVAALPVPL
     IDTSDPSAQL IAAAVHSEPH QTLDSLRLAR ENGVDRVVGD EALGSVEAVL TEARAYLDLG
     EGDAAAEVLA RLDAVTGNWR VDWHRGTAAL LGRSFVDAAR RFDAVLSAVP GEIAPKLAMA
     ATAELLAQQT GDEDHDTWCA TAETMYTSVW RTDRTIVSAA FGVARRMTER GAVLDAIFTL
     DQVPPTSRHY SMARMTSVLT LLSGPVEDMT EGALAEAARR IEALPAREPR ALQLRTVVLG
     TALDWMESGR EPETSRRILG VPFTRDGLRT GAESALRALA RTARSRSHRF ALVDLANAVR
     PQSLL
//
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