ID A0A164I0C6_9NOCA Unreviewed; 776 AA.
AC A0A164I0C6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=A2J03_10845 {ECO:0000313|EMBL:KZF00398.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF00398.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF00398.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF00398.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZF00398.1}.
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DR EMBL; LVCV01000598; KZF00398.1; -; Genomic_DNA.
DR RefSeq; WP_068379989.1; NZ_LVCV01000598.1.
DR AlphaFoldDB; A0A164I0C6; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000077673; 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; 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:KZF00398.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077673};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:KZF00398.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 152..431
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 84495 MW; 62252264C074B082 CRC64;
MSTRDSDTPT GPTTAPSQQT QAVDRTQAVD RTQAVDRTQA VARTQATAAT PVRSSRTSGR
TRSSRSHRTD TRRRLGAGLV EIPRVDPVDP ATAVMSDPTV PARKRFCWKC NSPVGRNAEG
EPDNPSGICP HCGARFDFTP LLEPGDLVVG QYEVQGCIAH GGLGWVYLAI DRNVSDRWVV
LKGLLHFGDD EAHAVAVAER QFLAEVAHPG VVKIYNFVEQ LRSDGTKIGF IVMEYVGGQS
LREILSAQGD TSARMPVEQA IAYVLEVLPA LAYLHSIGLV YNDLKPENIM VTDDQIKLID
LGAVAGIEDY GYLYGTAGYQ APEIVETGPT VASDIYTAGR TLAVLTLDMP STKGKYDAGI
PSEEDHELLR KYPSFKRLLL RATNPDPTQR FSSAEVLASQ ATGVLREILA LQTGTERPGL
STAFSPPRTT FGTEESVGRT DTYVDGKIRG DRISAREVVS ALPVPLVDPL DPSAPLLAAA
VHSAPQQTLD SLAHARRNGI ERFADGSPGG LEITLAEVKA HIDLGDTGTA ESVLKQVRTD
GPDPWRVEWY AGLIGLLKNE FNDASNHFEK VLDAMPGELA PKIALAASAE LIMEGTLRLD
TDEREKWRAC AESYYLSVWR TNRAVVSSAF GLARQMMYRS DPAAAVEVLD QVPISSRHYA
VARMTSVLTL LMDRPSPDLE EEDFREAARR VAMLPGREPR ALQMRTLVLA MAMDWVRSGH
AVEAEREPIL GAPFTETGLR TGTEAGLRAL ARNATDRAHR YTLVDLANAI RPQSLF
//