ID M3V3P9_9ACTN Unreviewed; 898 AA.
AC M3V3P9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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:GAC83917.1};
GN ORFNames=GP2_016_00510 {ECO:0000313|EMBL:GAC83917.1};
OS Gordonia paraffinivorans NBRC 108238.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223543 {ECO:0000313|EMBL:GAC83917.1, ECO:0000313|Proteomes:UP000035021};
RN [1] {ECO:0000313|EMBL:GAC83917.1, ECO:0000313|Proteomes:UP000035021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108238 {ECO:0000313|EMBL:GAC83917.1,
RC ECO:0000313|Proteomes:UP000035021};
RA Isaki-Nakamura S., 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 paraffinivorans NBRC 108238.";
RL Submitted (FEB-2013) 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:GAC83917.1}.
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DR EMBL; BAOQ01000016; GAC83917.1; -; Genomic_DNA.
DR AlphaFoldDB; M3V3P9; -.
DR STRING; 1223543.GP2_016_00510; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG3118; Bacteria.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000035021; 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:GAC83917.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:GAC83917.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 262..511
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 97962 MW; 1B49793A65739656 CRC64;
MEHTPDPTDH EPLDPAGRRD PAQTEEVGTQ RVSLADLMGD DEAGTERHTT DRNHPDSSGD
DGRPEEGTTD EVVEVGTQKA DLSALVDDDE PGDDQPGGDR PHDDQPHDDG RGEDELTTQP
RTTDPAVGTQ RAAPAFTVGT PGREPADART DKVLRPPPPA PPVDSGPLGR RLVPRRRPPV
HERRLGGGLV EMPKIQDIEP ADAVIDDPVI AESKRFCWRC GKPVGRSEGE GQGPPSGDCP
NCGARYSFVP GLAPGTLVAD QYEIAGAIAH GGLGWIYLAI DRNVSDRPVV LKGLLNSSDS
EAQRVAVAER QFLASVNHPG IVKIYNFVEH VADNGDRFGY IVMEYIGGQT LKQITSGDAG
KSLLSVEQAL AYMLEVLQAV GYLHSVGLVY NDVKPENIMV SSDEVKLIDL GAVSPINGYG
HLYGTPGFQA PEIVKTGPQV ATDIYSVGRT LAVLTVPVEM RGGRYVDGLP SPEDTPVFRD
NPSFYLLLQR ATAPDPADRF ASAEEMSTQV LNVLRETVAV HTGVPRPALS TVFTPQRSTF
GTDLMLAPVD GFFDPDQAAF YDPVDIANAL PLPLVDPLDP AAGLLTSAAL SDPRQTLDTI
KTARAERFAS LFNGRPSDNE HPSLEIDLAE ARAHLQLDDV DTALSLLREV RVHHGDSWRV
EWYMGICALM NDEPELAYER FDEVLQAMPG EVAPKLAVAG TAELIGRWLA DEKESKNADA
KIDRLYDVAQ HHYHDLWLTD HSIVTAAFGL ARLAVAAGDY EGAVRPLDEV PPTSRHFNTA
RLTAIMALVH GRPTSQVTRE QIVQAARRLE QIPDTEPRKP RMLLIVLGTA LGWIVDHPEE
VDSEKEPSTI LGFPFTEYGI RVGTEKSLRR LARQTRTNRE HRFMLVDLAN YVRPNTLF
//