ID A0A127NUZ1_9CORY Unreviewed; 827 AA.
AC A0A127NUZ1;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Putative serine/threonine-protein kinase pknG {ECO:0000313|EMBL:AMO89432.1};
GN ORFNames=WM42_1713 {ECO:0000313|EMBL:AMO89432.1};
OS Corynebacterium simulans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=146827 {ECO:0000313|EMBL:AMO89432.1, ECO:0000313|Proteomes:UP000074804};
RN [1] {ECO:0000313|EMBL:AMO89432.1, ECO:0000313|Proteomes:UP000074804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PES1 {ECO:0000313|EMBL:AMO89432.1,
RC ECO:0000313|Proteomes:UP000074804};
RX PubMed=26861018;
RG NISC Comparative Sequencing Program;
RA Tsai Y.C., Conlan S., Deming C., Segre J.A., Kong H.H., Korlach J., Oh J.;
RT "Resolving the Complexity of Human Skin Metagenomes Using Single-Molecule
RT Sequencing.";
RL MBio 7:e01948-15(2016).
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; CP014634; AMO89432.1; -; Genomic_DNA.
DR RefSeq; WP_062037034.1; NZ_CP014634.1.
DR AlphaFoldDB; A0A127NUZ1; -.
DR STRING; 146827.WM42_1713; -.
DR KEGG; csp:WM42_1713; -.
DR PATRIC; fig|146827.5.peg.1689; -.
DR Proteomes; UP000074804; Chromosome.
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 PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AMO89432.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:AMO89432.1}.
FT DOMAIN 180..461
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 91404 MW; 80F6078B6759D4FD CRC64;
MSPTQGHNFS EDELDHLEPE KLEEPNERAD DQATAAVMHT ASSAASASAA HDATQAVPFD
PFADEEGTSA VAFDPFADED GADADSDFND PDNIGALIAE LGQLRDRRKQ EDASQRSRRA
AIDTFRQRRA AKRTDREVAD GMARLPFIVP RNPTEALIDP VKEKVAPPQL SPGDIVAGQY
EILGVIAHGG LGWIYLANDH FVSGRIVVLK GMQAEKSSDE TATAEVEREF LADITHPGIV
KIFNFIDDPR VDGGFIVMEY VGGPSLKQRR NDQADHLFPV DTAIAYILEL LPALDYLHAR
GVVYNDLKPS NIIITEDQVK LIDLGAVSGI GAFGHIYGTK GFQAPEIAKD GPSVASDIYT
IGRTLACLTF HLPQEDGVYL PGLPSPADEP LLRRYLSFYR LLLRATDPDP AKRFQSVSQL
RNQLFGVLRE VIALRDGVQH PSQHSLFSPQ RTTFGTKHLV FRTDQLIDGI DRTVRITASE
VVSALPAPLV DRSDVGAALL QGASYTEPQE ALETLRQAMQ APEYEESAEI PLGVVRSMID
LGYTGQAREW LASIEDKLGN DWRFQWYSGV AVLLLDEYRA AQVHFANVLN LLPGEPAPKL
AIAAINELIL QQLGYNEVSL IDPAIARACA NLTTSLDELP NELFTDDRGI WDHVTDDPAH
LRFNSMRLYG IVWATYPTTV SSAFGLARQM RSEQQVELAV ATLDRVPNAS RHYRMARLTT
ILQLVLHDLS ESRIRRAARR LEEIPQNEPR FLQVKAAVIS AGLNFLRDCD LDAAASPNDL
FEFAFTQRGL RYGLADTLRA LARQAPFARH RYALVDLANQ VRPVTNF
//