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Database: UniProt
Entry: L7LLJ9_9ACTN
LinkDB: L7LLJ9_9ACTN
Original site: L7LLJ9_9ACTN 
ID   L7LLJ9_9ACTN            Unreviewed;       815 AA.
AC   L7LLJ9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:GAC61616.1};
GN   ORFNames=GSI01S_19_00800 {ECO:0000313|EMBL:GAC61616.1};
OS   Gordonia sihwensis NBRC 108236.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC61616.1, ECO:0000313|Proteomes:UP000035083};
RN   [1] {ECO:0000313|EMBL:GAC61616.1, ECO:0000313|Proteomes:UP000035083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC61616.1,
RC   ECO:0000313|Proteomes:UP000035083};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL   Submitted (DEC-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:GAC61616.1}.
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DR   EMBL; BANU01000019; GAC61616.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7LLJ9; -.
DR   eggNOG; COG0515; Bacteria.
DR   Proteomes; UP000035083; 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:GAC61616.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035083};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:GAC61616.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          176..426
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  88679 MW;  65C8D34942FC9C01 CRC64;
     MMSDIKKKRN KNGDAEPVAT EATALPAETQ ASAVEPAQTE ASESVQTQAG TVPAPMGAVG
     DTAPTATVTQ STQVRRILDD IAASRRKSRK SAHVHDRRLG SELVQLPEIT DIDPADAVLA
     DPVIAPSKRK CWNCGEPVGR KSGRGKGPLS GTCWNCGSRY SFVPGLKRGT MVADQYEIAG
     AIAHGGIGWI YLAVDHNVSD RPVVLKGLLN SSDSQAQAVA IAERQFLASV NDPGIVKIFN
     FVEGVTEDGR SVGYIVMEYV GGHTLKQLTT NEDGTSSLLP IEQAMAYILE VLSAVGYLHS
     VGLVYNDVKP DNIMITSDEV KLIDLGAVSA INGTGHLYGT PGFQAPEIVQ TGPQIVTDIY
     SIGRTLAVLT VDMPMADGRY LDGLPDPRTT PLFVENPSFY FLLHRATSPD PAERFSSAEE
     MTTQVLNVLR ETVALHTGVP RPSMSTVFTP QRSTFGTELL LAPVDGFFDP KDAAIHDPAD
     IARALPVPLV DPTDPAASVL TSAALSYPRQ TLDTIRAARA DGYKALIATD DADDGDGPQH
     PSMELDLAEA RAHLELGNLD TALQLLREVA VHHGDSWRLH WYLGICSLLN AEPELAFDRF
     HEVLEAMPGE VAPKLAVAGT AELIGYWLSA EEYTSNDQMA QVERWYEIAR QNYHDLWLTD
     HSIVSAAFGL ARMILAEGRY DAAIEPLDEV PTTSRHYGTA QISAIITLVH GRPPREVTRS
     ELFEAAERFE EISWDDPRRG RLQLIILGTA LGWIDAHLDE DYPADDFLGF PFNEHGLRAG
     TERSLRELAK ATRDNRAHRF LLVDLANLIR PATLF
//
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