ID R7WRP3_9NOCA Unreviewed; 790 AA.
AC R7WRP3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=Rrhod_0662 {ECO:0000313|EMBL:EOM77988.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM77988.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM77988.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM77988.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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:EOM77988.1}.
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DR EMBL; APMY01000020; EOM77988.1; -; Genomic_DNA.
DR AlphaFoldDB; R7WRP3; -.
DR PATRIC; fig|1273125.3.peg.639; -.
DR eggNOG; COG0515; Bacteria.
DR Proteomes; UP000013525; 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 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EOM77988.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 161..426
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 85140 MW; BAC330F6CEF008A2 CRC64;
MTRDRETPDE NRSEEDDAAG TGSAELASTQ AGAYVPTQAA AGPQLSVPTQ AAGLAPTQAA
ETRTPSGPRG SGRSSRPRSR GRRELHLAGG LVDVPVPTPP DPTDAVMKDP RVPEHKRWCW
RCGKPVGRGR PGPQSGVCAY CGTPFDFRPA LRPGDLVGGQ YEVMGCLAYG GLGWVYLGID
RNVSDRWVVL KGLLHSGDAE AQAVAMSERE FLAEVTHPGI VQIFNFVEHP TQDGAPIGYI
VMEYVGGTSL RDVLGQCTPP ARIPVEQAIG YVLGVVPALS YLHSMGLVYN DLKPENIMVT
DESIVLIDLG AVSQIGSYGY LYGTPGYQAP EIVRTGSTPA TDIYTVGRTL AVLVLKMPMK
HGKYLPGLPE SAPLLAEHPS LRLFLERAID ENPANRFASI DEMAEQLTGV LRGILAQQTG
EEHPGLSTVF SRSRTTFGTD VVVAPTDVYV DGIRRDTRLD VAEVTRALPV PLIDPTDPNA
RLLTATILSE PQQTLDAIAQ VRAEGLEHAA DEADPARAHD AREAELLSRE LTVAEAKAHI
DLGEPGAALE LLAGLEAELG RHWRTDWFTA TASLAQGDLP TAAERFEAVR RAMPGELAPK
LALAATAELT LQHGKGDDPD SLRELAERAY GAVWRTDQTV VSAAFGYARA LTARPDVPAA
VRALDRIPTT SRFYTIGRMT AIVTLLSGRR IADIGEPSLR EAARRVTVLP MQERRRLQLE
TVVLGTALDW ILTGNRPAHP GSILGVAFTE NGLRSGVENC LRSLARLTDD RVHRYQLVDL
ANGVRPRSML
//