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Database: UniProt
Entry: A0A0M4CJI1_9CORY
LinkDB: A0A0M4CJI1_9CORY
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ID   A0A0M4CJI1_9CORY        Unreviewed;       653 AA.
AC   A0A0M4CJI1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknB {ECO:0000313|EMBL:ALC04522.1};
GN   ORFNames=CDES_00175 {ECO:0000313|EMBL:ALC04522.1};
OS   Corynebacterium deserti GIMN1.010.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=931089 {ECO:0000313|EMBL:ALC04522.1, ECO:0000313|Proteomes:UP000068067};
RN   [1] {ECO:0000313|EMBL:ALC04522.1, ECO:0000313|Proteomes:UP000068067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMN1.010 {ECO:0000313|EMBL:ALC04522.1,
RC   ECO:0000313|Proteomes:UP000068067};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium deserti GIMN1.010 (=DSM
RT   45689), isolated from desert sand in western China.";
RL   Submitted (AUG-2014) 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; CP009220; ALC04522.1; -; Genomic_DNA.
DR   RefSeq; WP_053543739.1; NZ_CP009220.1.
DR   AlphaFoldDB; A0A0M4CJI1; -.
DR   STRING; 931089.CDES_00175; -.
DR   KEGG; cdx:CDES_00175; -.
DR   PATRIC; fig|931089.4.peg.31; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000068067; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 4.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.30.10.20; -; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR005543; PASTA_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   NCBIfam; NF033483; PknB_PASTA_kin; 1.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF03793; PASTA; 4.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00740; PASTA; 3.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51178; PASTA; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ALC04522.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:ALC04522.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          370..436
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          437..505
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          506..570
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   653 AA;  69093 MW;  F18865B6BAC0F655 CRC64;
     MTFVIADRYE LGGNIGSGGM SEVFAATDTL IGREVAVKML RIDLAKDINF RERFRREAKN
     SGKLSHPAIV AVFDTGEVDR DGISVPYIVM ERVHGRNLRD IVTEDGVFTP TEAARTLIPV
     CEALQASHDA GIIHRDVKPA NIMITNTGGV KVMDFGIARA VDDSTSAMTQ TSAVIGTAQY
     LSPEQARGKP ADARSDIYAT GCVMYELVTG KPPFEGESPF AVAYQHVQED PTPPSDFIAD
     LTPTAAINVD AVILTAMAKH PADRYQTAAE MASDLGRLSR NAVSHAARAH VEAEEKEPET
     LLSTRAATTV DPAAAPDARL APAAPIAAPI AAREKKRGSR GLIALTIVLA LGVVGVAGAF
     TYDYLSNSST SSTHAIPNVE GFPQAEAISQ LEAAGFTVNV ATEASADIQE GLVIRTSPSV
     GSEVRDGATV TITVSTGREM VNIPDVSGMT LEEAARTLED LGLVLDPSIR EEYSDTVSTG
     QVIEQNPPAG QEVVVGSSVS LTVSSGVENI RVPTATGMNW SQAEQNLTSL GFTPSVTYVD
     SEHPEGEVLT VSNEGTEMPK GSVITVEVSN GMLINAPDLA RLNQQQAIDA LRAAGWTAPD
     QSLIVGEPIA TVALVDQGRI GFQSPSANAL FRKDAQVTVR FFEFNIEALV QNP
//
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