ID A0A097IIF4_9CORY Unreviewed; 842 AA.
AC A0A097IIF4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AIT61896.1};
GN ORFNames=CDOO_11975 {ECO:0000313|EMBL:AIT61896.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT61896.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT61896.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT61896.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-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};
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DR EMBL; CP006764; AIT61896.1; -; Genomic_DNA.
DR RefSeq; WP_018022771.1; NZ_CP006764.1.
DR AlphaFoldDB; A0A097IIF4; -.
DR STRING; 558173.CDOO_11975; -.
DR KEGG; cdo:CDOO_11975; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_011707_0_0_11; -.
DR OrthoDB; 137117at2; -.
DR Proteomes; UP000029914; Chromosome.
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; 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:AIT61896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029914};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000313|EMBL:AIT61896.1}; Transferase {ECO:0000313|EMBL:AIT61896.1}.
FT DOMAIN 193..474
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 93015 MW; 62D183060A4083B3 CRC64;
MSASTGKTGE DYGEEFVGTE AALFDPFADD EDFDDGENVV AEAVKYEPHA EQADHTTGSL
RRDAPDNPGT SAVAFDPFAD DDEDEDDEEL AGVGDIAGLI KDLGALRDHR TGRDGASRRE
DTAERARREA LSTFRSRHGA ERSSRPVADG MVELPFIAPA RAEDALMDPH SEAKKPGIAM
PQLNPGDIVA EQYEILGVIG HGGMGWIYLA HDHFVADRLV VLKGMQAEKT DEEMAAARAE
REFLAGITHP QIVKIFNFID DERVAGGFIV MEFVGGPSLR ARRNAQDNHL LPIDVAIGYI
LEILPALDYL HSRGVVYNDL KPDNIIVTED QVKLIDLGAV SGIGAYGYIY GTKGFQAPDV
STHGPSVATD IYTVGRTLAT LTLDMPREDG IYLPGLPSPT TDPTLRRFLS YYRLLLRATH
PDPEQRFSSL AELETQLYGV LREVIALRDG RYHPQQHSLF SPQRSTFGTK HVVFRTDQLI
DGIDRTIRMT SDEVVSAIPT PLIDRSDVGA AMLSGSSYAE PQEALETLRQ AMQTPEYEES
AEIPFGVVRA MLDLGLTSQA RAWLQSLSER LGTDWRYQWY SGVTSMFLED YQAAQSHFNQ
VLTILPGEPA PKLALAAVDE LILQTRELQN TPLLDERVAR ATPALDGNLA DLAREIFENF
PGDDLWSHVT DDPKLLRFHA MRLYGMVWAS NPTTVSSAFG LSRLLVAEGL TEMAVQALDR
VPQASRHHRM AKLTTVLMLI SDVLTESRIR RAARRLEEIP TNEPRFIQIK TAVMSAALEF
LQEAGVESAA SHNTLFDYPF TQTGLRNGIA NSLRRLARQA PSAQHRYALV DIANAVRPQT
LF
//