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Database: UniProt
Entry: G7GIN1_9ACTN
LinkDB: G7GIN1_9ACTN
Original site: G7GIN1_9ACTN 
ID   G7GIN1_9ACTN            Unreviewed;       944 AA.
AC   G7GIN1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:GAB03456.1};
GN   ORFNames=GOAMR_02_00020 {ECO:0000313|EMBL:GAB03456.1};
OS   Gordonia amarae NBRC 15530.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB03456.1, ECO:0000313|Proteomes:UP000006023};
RN   [1] {ECO:0000313|EMBL:GAB03456.1, ECO:0000313|Proteomes:UP000006023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB03456.1,
RC   ECO:0000313|Proteomes:UP000006023};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL   Submitted (NOV-2011) 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:GAB03456.1}.
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DR   EMBL; BAED01000002; GAB03456.1; -; Genomic_DNA.
DR   RefSeq; WP_005180952.1; NZ_BAED01000002.1.
DR   AlphaFoldDB; G7GIN1; -.
DR   STRING; 1075090.GOAMR_02_00020; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000006023; 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:GAB03456.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006023};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:GAB03456.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          308..562
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..113
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   944 AA;  101630 MW;  B7F4CDB7C7CEF7AF CRC64;
     MTGSPTPAHP GGTSPPDGDH TTEPNSTEPN SSESNSSDPT SATTDRVRSA DVDDGTQSVS
     RDELGLGTDA DTDEDDGDST QAAAFDPFAD DEDDEDDDEE DGDKDDGERD DGEDDDHTQA
     AAFDPFADDE DEDDGTQAAP FDPFADDDEG DGTQAAVFDP FAGDTGTGTQ GSVYNPFAGD
     TDKVPRRPPP PEPVTGYSTG STGPVSSEAI TTGSTLRLIP QNHLGVHDRR LGSGLVDLPK
     IHDIDPADAV LTGAVIPEGK RRCWRCGRPV GRTQGKHAGP LTGDCPKCGA HYSFVPGLDP
     GTLVADQYEI AGAIAHGGMG WLYLATDRNV SDRPVVLKGL LNSSDSEAQQ VALAERQFLA
     SVNHPGIVKI YNFVEHPDQF GQHIGYIVME YIGGQTLKQL MAAQKSAADS DRGLLSIEQA
     MAYVLEVLPA VGYLHSVGLV YNDVKPENIM VASDDVKLID LGAVSAINGY GHLYGTPGFQ
     APEIVRTGPQ VATDIYSIGR TLAVLTLPMP RKNGRYLDGL PSPEDSAVLT DNPSYHLLLQ
     RATAPDPADR FVSAEEMTTQ VLNVLREVVA VHTGVPRPSL STVFSPPRTT FGTELLLGPV
     DGFFDPDKAA FYDPLDIAHA LPVPLVSPAD PAAGMLTSAA LSSPRQTLDS IKVARADGFS
     SIFGTPSTDP HPSLEIDLVE ARAHLELDQV DTAMELLRKI TVHHGDSWRV RWYMGVCALR
     NGEPEIAYER FDDVLQAMPG EIAPKIAVAG TAELIGRWLA DERLASPRRI TEWTTIAAHH
     YHDLWWTNHT IITAAFGLAR LNTAAGRIAE ALEPLDEVPS TSRHYNTARA TAVLILVHGR
     KSEDITREEI TAAAARLEQI PDSEPRKARL TLIVLGTALG WIAVQDDPPT DSKVKILGYP
     FTELGLRRGT ESSLRSLARQ TRSNRDHRFM LVDLANYVRP ETLF
//
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