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Database: UniProt
Entry: A0A024JTR1_9MYCO
LinkDB: A0A024JTR1_9MYCO
Original site: A0A024JTR1_9MYCO 
ID   A0A024JTR1_9MYCO        Unreviewed;       755 AA.
AC   A0A024JTR1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=BN973_01067 {ECO:0000313|EMBL:CDO86722.1};
OS   Mycobacterium triplex.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO86722.1};
RN   [1] {ECO:0000313|EMBL:CDO86722.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86722.1};
RX   PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA   Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT   "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL   Genome Announc. Announc.2:e00499-e00414(2014).
RN   [2] {ECO:0000313|EMBL:CDO86722.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO86722.1};
RA   Urmite Genomes U.;
RL   Submitted (APR-2014) 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; HG964446; CDO86722.1; -; Genomic_DNA.
DR   RefSeq; WP_036466398.1; NZ_LQPY01000021.1.
DR   AlphaFoldDB; A0A024JTR1; -.
DR   STRING; 47839.BN973_01067; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_011707_0_0_11; -.
DR   OrthoDB; 137117at2; -.
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:CDO86722.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:CDO86722.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          155..427
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  82291 MW;  CB52CDC03CFAC3B5 CRC64;
     MTEAEHDADA EDTDPGTQPP DAQTGATTGR AHATQALFRP EWDDDDDDLP HLTLGGVDTE
     PQDRMTVATR VLPPTRQLGG GLVEIPRIRD IDPLEALMTN PVVPEHKRFC WNCGKPVGRS
     TSEGKGESEG KCPSCGSPYS FLPQLNPGDI VANQYEVKGC IAHGGLGWVY LAVDHNVNDR
     PVVLKGLVHS GDAEAQAIAM AERQFLAEVV HPQIVQIFNF VEHTDRHGDP VGYIVMEYIG
     GQSLKRGKKD PRLPVAEAIA YLLEILPALS YLHSIGLVYN DLKPENIMLT EEQLKLIDLG
     AVSRVNSFGY LYGTPGYQAP EIVRTGPTIA TDIYTVGRTL AALTLNLRTR NGRYVDGLPE
     DDPVLSTYDS FGRLLRRAID PDPRRRFGSA EEISAQLTGV LREVVAQDSG VPRPGLSTLF
     SPSRSTFGVD LSVAHTDVYL DGQVHSEKLT AREIVTALSV PLVDPTDVAS PVLQATVLSQ
     PVQTLDSLRA ARHGSLAAEG IDVSESVELP LMEVRALLDL GDVAKATRKL DDLAERVGWR
     WRLVWFRAVA ELLTGDYDSA IKHFTEVLDT FPGELAPKLA LAATGELAGH VDVDKFYKTV
     WRTNDGVISA AFGLARSLSA EGDRIGAVRT LDEVPATSRH FTTARLTSAV TLLSGRSTSE
     ITEEQIRDAA RRVEALPPTE PRVLQIRALV LGGAMDWLET NTASTNHILG FPFTQHGLRL
     GVEASLRSLA RVAPTQRHRY TLVDMANRVR PTSTF
//
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