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Database: UniProt
Entry: A0A1X7J130_9CORY
LinkDB: A0A1X7J130_9CORY
Original site: A0A1X7J130_9CORY 
ID   A0A1X7J130_9CORY        Unreviewed;       802 AA.
AC   A0A1X7J130;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Serine/threonine-protein kinase PknG {ECO:0000313|EMBL:SMG21362.1};
GN   ORFNames=SAMN06295981_1167 {ECO:0000313|EMBL:SMG21362.1};
OS   Corynebacterium pollutisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1610489 {ECO:0000313|EMBL:SMG21362.1, ECO:0000313|Proteomes:UP000193309};
RN   [1] {ECO:0000313|EMBL:SMG21362.1, ECO:0000313|Proteomes:UP000193309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VDS {ECO:0000313|EMBL:SMG21362.1,
RC   ECO:0000313|Proteomes:UP000193309};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FXAR01000003; SMG21362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7J130; -.
DR   STRING; 1610489.SAMN06295981_1167; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000193309; 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; 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; 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:SMG21362.1};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:SMG21362.1}.
FT   DOMAIN          154..436
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  87655 MW;  0931C5DDC27DF809 CRC64;
     MTHPDFEELP EDIADEAPGT QAVHFDPFAD DDDSVDAGLD ALIADLGNLR DQHDDGATVG
     SPVGTAAMTG PDTAPTAASI RDDTSARARE LALSTFRERR GAERGGRTVA DGMVNLPFIP
     PTRPEDALQD PAAAAQKGIP APHLNPGDMV AGQYEILGVI AHGGMGWIYL ANDHFVSGRL
     VVLKGMQSEK SADEMGAAVA EREFLADITH PGIVKIYNFI DDPRVPGGFI VMEYVGGPSL
     RSRRNSRENH VLPIDLAIGY LIEVLPALDY LHSRGVVYND LKPDNIIVTE DQVKLIDLGA
     VSGIGAYGFI YGTKGFQAPE VASHGPSVAS DIYTIGRTLA ALTVHLPKDD TGAYLPGLPS
     PSTEPLFRKH LSFYRLLRRA TNEDPTQRFR DIAEMSTQLY GVLREVIAIR TGEQFPAQHS
     MFSPQRTTFG TKHLVFRTDQ LIDGIDRTVR ITSPEVVSAL PAPLIDRTDV GAGMLSGSSY
     TEPQEALETL RQAMKTPEYE QSAEIPLGVV RAMLDLGFTG QARSWLSSLE GRLGHDWRFQ
     WYSGVTALLL DDYVSAQKHF AAVLNILPGE SAPKLALAAV DELILQQLGH HHSALLPEKV
     ARAASLLSTS LDAVDPEVVD QINPTWLHVT QEPALLRFNA MGLYGLVWAT NPTTVSSAFG
     LARQLMAEGQ IEMSVAALDR VPQASRHHRM AQLTTILQLI SGTLTESRIR RAARRLEEIP
     TNEPRFLQIK IAVMSAGLNF LRDATVESAA SPNDLFEYPF TQRGLRYGLA YTLRQQARQA
     PFARHRYALV DLANQVRPVT WF
//
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