ID A0A1G8NGU7_9NOCA Unreviewed; 779 AA.
AC A0A1G8NGU7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=SAMN05444695_11148 {ECO:0000313|EMBL:SDI78730.1};
OS Rhodococcus triatomae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=300028 {ECO:0000313|EMBL:SDI78730.1, ECO:0000313|Proteomes:UP000183263};
RN [1] {ECO:0000313|EMBL:SDI78730.1, ECO:0000313|Proteomes:UP000183263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44892 {ECO:0000313|EMBL:SDI78730.1,
RC ECO:0000313|Proteomes:UP000183263};
RA de Groot N.N.;
RL Submitted (OCT-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; FNDN01000011; SDI78730.1; -; Genomic_DNA.
DR RefSeq; WP_072738982.1; NZ_FNDN01000011.1.
DR AlphaFoldDB; A0A1G8NGU7; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000183263; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 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:SDI78730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183263};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 779 AA; 85523 MW; FD62B6C58084C546 CRC64;
MTDPNTPERD RGDDETTRRA APPDEETTRR TAPPAPDEAP DDLPDTAAVQ RSEPSRGSRT
GNSGTGRSVR SRLSRSGGRM RLGGGLVEVP AVRTVDPAAA VMADPQVPER KRFCWKCTRP
VGRKSASTRS AEYGQCPHCG ATFDFRPLLR RGDLVAGQYE VQGCIAYGGL GWIYLAIDHN
VSDRWVVLKG LLHFGDAEAQ AVAVAERQFL AEVAHPNIVK IYNFVEHPRP DGTPMGYIVM
EYVGGTSLRD VLSAQPDDHR LPVDQAIGYV LEILPALGYL HSIGLVYNDL KPENVMVTED
SLELIDLGAV AGIEDYGYLY GTPGYQAPEI IKTGPTPATD IYTVGRTLAV LTLDMPVDKG
KLRSGLPTPE EAPLLAEHEF FHRLLLRATD PDPKQRFESA EEMAGQATGV LREIVAGRTG
RERPGLSTVF SRPRNTFGTD ELVEQTDVYV DGRVRDPTLD PRSVAQGLPV LLVDPGDPHA
RLLAATVQAE PRQTLDSIAH ARESGIERQS GEGRVALSRE LTFAEVVAHL DLGDPETARN
LLDRLERDIG SHWRIDWYAG LTMLTEAQYE PAFSHFEAAL TAAPGEAAPK LALAVTADLI
VQHWDSSDQR QWRDFAERYY RTVWLTDHGM VSAAFGLARQ LTARSDLDGA VTVLDQVPAS
SRHYSMARMT AVLTRLSGAL VDLDEAAMRE SARRVSLLAA EESRALQMRT LVLGTALDWM
RCGNRPSDDS PILGVPFTEE GLRRGVEKCL RALARGAQER THRYALVDMA NAIRPRSLF
//