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
//