GenomeNet

Database: UniProt
Entry: K6X9G1_9ACTN
LinkDB: K6X9G1_9ACTN
Original site: K6X9G1_9ACTN 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system