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Database: UniProt
Entry: A0A097IIF4_9CORY
LinkDB: A0A097IIF4_9CORY
Original site: A0A097IIF4_9CORY 
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
//
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