ID K6X9G1_9ACTN Unreviewed; 903 AA.
AC K6X9G1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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 Name=pknG {ECO:0000313|EMBL:GAC02717.1};
GN ORFNames=GONAM_60_00010 {ECO:0000313|EMBL:GAC02717.1};
OS Gordonia namibiensis NBRC 108229.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1208314 {ECO:0000313|EMBL:GAC02717.1, ECO:0000313|Proteomes:UP000035058};
RN [1] {ECO:0000313|EMBL:GAC02717.1, ECO:0000313|Proteomes:UP000035058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108229 {ECO:0000313|EMBL:GAC02717.1,
RC ECO:0000313|Proteomes:UP000035058};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia namibiensis NBRC 108229.";
RL Submitted (AUG-2012) 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};
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:GAC02717.1}.
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DR EMBL; BAHE01000060; GAC02717.1; -; Genomic_DNA.
DR RefSeq; WP_006868846.1; NZ_BAHE01000060.1.
DR AlphaFoldDB; K6X9G1; -.
DR Proteomes; UP000035058; Unassembled WGS sequence.
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:GAC02717.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:GAC02717.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 267..516
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 97975 MW; 98EF6F18083B3371 CRC64;
MPMDYAGEPS HADPHGPEGH DVPTPDTPEE VGTQRVSLAD LMGDDEADTD RHATDAHAAD
DHTTDAEAQS SQNPAENATD DHTTDVRSSD EGTTDQVVEV GTQKADLDAL MAGADDTADD
DTTRPRAVAD SDVGTQAAAP AFTVGIAPPD RFDGRTDRVV RTRATPEPDS GPLGRRLVPR
RRPPVHERRL GSGLVEMPKI TDIEPEDAVI DDPVIAESKR FCWRCGKPVG RLEGEGEGPP
TGDCANCGAR YSFVPGLAQG TLVADQYEIA GAIAHGGLGW IYLAIDRNVS DRPVVLKGLL
NSSDSEAQRV AVAERQFLAS VNHPGIVKIY NFVEHISDDG ERFGYIVMEY IGGQTLKQIT
SGDPEKSLLS VEQGLAYILE VLLAVGYLHS VGLVYNDVKP ENIMVGSDEV KLIDLGAVSP
INGYGHLYGT PGFQAPEIVK TGPQVATDIY SVGRTLAVLT VPMEMRNGRY VDGLPAPDET
AVFRDNPSFY LLLQRATAPD PADRFASAEE MSTQVLNVLR ETVAVHTGVP RPSLSTVFTP
QRSTFGTDLM LAPVDGFFDP DQAAFYDPVD IATALPLPLV NPLDPAASLL TSAALSDPRQ
TLDSINTARA EGFASLFGGR PVKNAHPSLE IDLAEARAHL QLDDVDTALA LLRDVREHHG
DSWRVEWYMG ICALMNDEPE LAYERFDEVL GAMPGEVAPK LAVAGTAELI GRWLADENGS
GKSAEKISRL YDVAQHHYHD LWLTDHSIVT AAFGLARLAV AAGDYDGAIR PLDEVPATSR
HFNTARATAI IALVHGRPTS QVTRNQIVEA ARRLEQIPDT EPRKSRMLLI VLGTALGWIH
DNPEEEDSDK EPSTLLGFPF TEYGIRTGTE RSLRQLARQT RNNREHRFML VDLANYVRPN
TLF
//