ID A0A1Q2HZ75_9CORY Unreviewed; 837 AA.
AC A0A1Q2HZ75;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Serine/threonine-protein kinase PknG {ECO:0000313|EMBL:AQQ16133.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:AQQ16133.1};
GN Name=pknG {ECO:0000313|EMBL:AQQ16133.1};
GN ORFNames=CGLAU_10995 {ECO:0000313|EMBL:AQQ16133.1};
OS Corynebacterium glaucum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=187491 {ECO:0000313|EMBL:AQQ16133.1, ECO:0000313|Proteomes:UP000217209};
RN [1] {ECO:0000313|EMBL:AQQ16133.1, ECO:0000313|Proteomes:UP000217209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 30827 {ECO:0000313|EMBL:AQQ16133.1,
RC ECO:0000313|Proteomes:UP000217209};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CP019688; AQQ16133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2HZ75; -.
DR KEGG; cgv:CGLAU_10995; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000217209; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
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 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:AQQ16133.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217209};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:AQQ16133.1}.
FT DOMAIN 184..429
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 92285 MW; 5A279A69D1060E79 CRC64;
MAIERGTSED RGPDSGPDPT EAVLYDPFVD DDDDADDDDA DDDDAGDDGG FSQEEPDTEA
VAFDPFAEDD DEAVDEDDED SGISDAAYAE LGDMAGLLKD LEKLRRGGGR EETSQRSRLQ
ALDTFRERRG TRRASRMVAD GMVELPWVQP AEPKEALHDP TAAVVQKGIP APALHPGDVV
AGQYEILGVI AHGGMGWIYL AQDHYVAGRV VVLKGLHSTD NPDEAAAAAA EREFLADITH
PGIVKIFNFI DDPRVPGGFI VMEYVGGPSL REARKAAPGH LLEPDIAIAY ILEVLPALGY
LHSRGVVYND LKPDNIIVTE DQVKLIDLGA VSGIGAFGFI YGTRGFQAPE VATEGPTIES
DIYTVGRTLA ALIIDLPTSD GVYDPGIPTP STEPMFRRYI SLYRVIARCC HKDPALRFHS
AKALELQLLG VLRELIAVRD GKTYPAQHSL FSPQRTTFGT KHLVFRTDQL IDGITRTVEI
TPQEVVAALP SPLINRHDVG AAMLQGSSYA EPQETLETLR QAMRTPQYKE SMEIPFAVVR
TMLDLGLTSQ ARSWLGSLDE KYGENWRFFW YFGVVNLLLG DFAQAQRDFS RVLGILPGEA
APKLAIAAVD ELLLQQAGLR EEQLLDDDLA RACAGIRTSL DDIPSRVFQD LVAAGVLDDE
WSMVADNPAM LRFHAMRLYS LVWLANPTTV SSAFGLARQL MNEGEVELAV AALDRVPQSS
RHHRMAQLTA ILCLVAQDLT EARIRRAARR LEEIPSTEPR FLQVKIFVLR AALTFLRQNR
VYGAASHKPL FEYPFNVRGL RRGLAITLRE QARVAPYPRH RYALVDMANK VRPATWF
//