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Database: UniProt
Entry: A0A1I2TND8_9CORY
LinkDB: A0A1I2TND8_9CORY
Original site: A0A1I2TND8_9CORY 
ID   A0A1I2TND8_9CORY        Unreviewed;       962 AA.
AC   A0A1I2TND8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Serine/threonine-protein kinase PknG {ECO:0000313|EMBL:SFG63831.1};
GN   ORFNames=SAMN05660282_01488 {ECO:0000313|EMBL:SFG63831.1};
OS   Corynebacterium spheniscorum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=185761 {ECO:0000313|EMBL:SFG63831.1, ECO:0000313|Proteomes:UP000199065};
RN   [1] {ECO:0000313|EMBL:SFG63831.1, ECO:0000313|Proteomes:UP000199065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J11, PG 39 {ECO:0000313|Proteomes:UP000199065};
RA   de Groot N.N.;
RL   Submitted (OCT-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};
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DR   EMBL; FOPJ01000008; SFG63831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2TND8; -.
DR   STRING; 185761.SAMN05660282_01488; -.
DR   Proteomes; UP000199065; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; 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; 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:SFG63831.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199065};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:SFG63831.1}.
FT   DOMAIN          315..596
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  103857 MW;  B3A60DDB3D5D085B CRC64;
     MSPRADHDAA PWPGDEDFPT GSSAHSPGDQ SSSANPGTEA VLFDPFAEDD DEDDIDVMAL
     LAADNFGLGP SNTDEELTPK AGPQKRPDLE DLDEILAGLP LPQPTISGAS TAGISQAGPA
     LHGEESEPSQ SGAAQTLPPL GPGLKPGVSA RDARAAAQRA SMQGATKAGA ADAVGLPTAG
     TAHDFDDDAA ERPTQPGGHH QPLAQAVPGI PTASTQAGGF KTDASADTQP PGADALSRLD
     TSERSRQEAL STFRERRGAH RVGRTVADGM VHLPFVGLTQ PSAALKDPES LAKAAKDKKI
     GPPQLHRGDI VAEQYEILGV IAHGGMGWIY LANDRNVSGR LVVLKGMQSS ASAHDQGAAQ
     AEREFLADIT HPGIVKIYNF IDDPRVAGGF IVMEYVGGPS LRSRRNVLPN KVFAPDIAIA
     YILEILPALD YLHSRGVVYN DLKPDNIIIT EDQVKLIDLG AVTGIGAYGY IYGTRGFQAP
     EVATAGPSVA SDIYTIGRTL AAMTVRLPVV DGAYAMGIPS PSEEPLFRRY LSFYRLLRRA
     THEDPTQRFR DVGELQTQLF GVLREILAVR DGAQFPAQHS LFSPQRSTFG TKHLVFRTDQ
     LIDGIDRTVR ITSSEVVGAL AAPLIDRSDV GAAMLSGSSY AEPQEALETL RQAMNTEEYE
     HSAEIPLGVV RALLDLGFTA QARAWLKSLE PRLGPDWRFQ WYSGITDLLM EDYANAQKHF
     NRVLNILPGE AAPKLALAAV DELLLQQLGH HHAPLLDDET ARAASGLSSH LDELDNKHFV
     EMSESWSHIT LDPRVLRFHA MRLYGLVWAT NPTTVSSAFG LSRQLVAEGQ TEMAVAALDK
     VSQASRHHRM AQLTTILLLI SAQLTESRIR RAARRLEGIP TNEPRFLQIK IAVMSAALTF
     LRDAKVDAAA SPNDLFEFPF NQRGLRGGLA ETLRQQARQA PFARHRYALV DMANQVRPAT
     WW
//
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