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Database: UniProt
Entry: R7WRP3_9NOCA
LinkDB: R7WRP3_9NOCA
Original site: R7WRP3_9NOCA 
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
//
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