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Database: UniProt
Entry: A0A1X1USG0_9MYCO
LinkDB: A0A1X1USG0_9MYCO
Original site: A0A1X1USG0_9MYCO 
ID   A0A1X1USG0_9MYCO        Unreviewed;       752 AA.
AC   A0A1X1USG0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Serine/threonine-protein kinase PknG {ECO:0000256|ARBA:ARBA00014676};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AWC06_16880 {ECO:0000313|EMBL:ORV59782.1};
OS   Mycobacterium fragae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1260918 {ECO:0000313|EMBL:ORV59782.1, ECO:0000313|Proteomes:UP000194000};
RN   [1] {ECO:0000313|EMBL:ORV59782.1, ECO:0000313|Proteomes:UP000194000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45731 {ECO:0000313|EMBL:ORV59782.1,
RC   ECO:0000313|Proteomes:UP000194000};
RA   Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA   Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA   Olivier J., Enrico T., Nicola S.;
RT   "The new phylogeny of the genus Mycobacterium.";
RL   Submitted (JAN-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};
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:ORV59782.1}.
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DR   EMBL; LQOW01000024; ORV59782.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1USG0; -.
DR   STRING; 1260918.AWC06_16880; -.
DR   OrthoDB; 137117at2; -.
DR   Proteomes; UP000194000; 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:ORV59782.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194000};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:ORV59782.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          153..424
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        20..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   752 AA;  82134 MW;  5601C06F60E00AD3 CRC64;
     MGDSVNKPEP DEAGPGTQPV DESPDSSSAR RPVTTQAVFR PHFDDDEDSD DIAARTADTE
     PRERVTTAAR APVRRLGGGL VEIPRVPDID PLEALMPSPV VPESKRFCWN CGRPVGRSSP
     DGKALSEGWC PYCGSPYSFL PQLSPGDVVA GQYEIKGCIA HGGLGWVYLA FDRNVNDRPV
     VLKGLVHSGD AEAQAIAMAE RQFLAEVVHP SIVQIFNFVE HTDRHGEPVG YIVMEYVGGR
     SLKRGKGDKL PVAEAIAYVL EILPALGYLH SIGLVYNDLK PENIMLTEEQ LKLIDLGAVS
     RINSFGYLYG TPGYQAPEIV RTGPTVATDI YTVGRTLAAL TLNMRTRGGR YVDGLPEDDP
     VLSTYDSFGR LLRRAIDPDP RRRFASAEEM SGQLSGVLRE VVAQDTGIRR PGLSTIFSRS
     RSTFGVDMLV AHTDVYLDGQ VHAEKLTAKE IVTALQVPLV DPADVAAPLL QATVLSEPVQ
     TLDSLRAFRH GALDSDDIDL SESVELPLME VRALLDMGDV AKATRKLDDL ADRVGWRWRL
     VWYRAVSELL TGDYDSATKH FNEVLDTFPG ELAPKMALAA TAELAGSSDE HKYYETVWKT
     DDGVISAAFG LARAQSVEGD REGAVRTLDE VPASSRHFTT ARLTSAVTLL SGRSASEITE
     EQIRDAARRV EALPPTEPRV LQIRALVLGS AMDWLQDHEA STNHILGYPF TEHGLRLGVE
     ASLRGLARVA PTQAHRYTLV DMANRVRPTS TF
//
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