ID   Q9ZNB6_STRCH            Unreviewed;       487 AA.
AC   Q9ZNB6;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Eukaryotic-type protein kinase {ECO:0000313|EMBL:BAA34340.1};
GN   Name=pkaE {ECO:0000313|EMBL:BAA34340.1};
OS   Streptomyces coelicolor.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=1902 {ECO:0000313|EMBL:BAA34340.1};
RN   [1] {ECO:0000313|EMBL:BAA34340.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A3 {ECO:0000313|EMBL:BAA34340.1};
RX   PubMed=10627033;
RA   Ogawara H., Aoyagi N., Watanabe M., Urabe H.;
RT   "Sequence and evolutionary analyses of eukaryotic-type protein kinases from
RT   Streptomyces coelicolor A3(2).";
RL   Microbiology 145:3343-3352(1999).
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; AB018799; BAA34340.1; -; Genomic_DNA.
DR   PIR; T42076; T42076.
DR   RefSeq; NP_627320.1; NC_003888.3.
DR   AlphaFoldDB; Q9ZNB6; -.
DR   OMA; NVMVKQD; -.
DR   PhylomeDB; Q9ZNB6; -.
DR   BRENDA; 2.7.11.1; 5998.
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; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 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:BAA34340.1};
KW   Transferase {ECO:0000313|EMBL:BAA34340.1}.
FT   DOMAIN          1..253
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          273..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..297
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  53321 MW;  56F91372AF9EBE3F CRC64;
     MGQVWTAYDR RLDRRVAVKL LRPDKVAGAE ADELRRRFVR ECRITAQVDH PGLVTVHDAG
     SEGEELFLVM QYVDGADLSD HLAEHDPYPW QWAVAVAAQL CAVLSAVHAV PIVHRDLKPR
     NVMVKQDGTV TVLDLGVASV MDADTTRLTH TGTPIGSPAY MAPEQAMGGA VGPYTDLYAL
     GVLLHELLSG DVPFAGSTAL GVLHRHLYEP PLPVRRIRPE VPEALEALVL RLLAKDPQHR
     PDSAQEVYEH LALLLPALGV PTGGPLDPTR PFVRPHAPWP DRARTPAPQP APVPPAAEAA
     KPDVARAVDD VKRLLGEGRI TQAVDVLGAI LPAAAEQHGE RSPVVRTLRR QYAATLMDDG
     QYRRALPELR RLADERAAEA GQADPQCLRH RYDAAQCLEQ LGEPAAALAE YRALLPYYEN
     QYVAGDPDLA HDVRRRIGHL LLALGDRAAA HDTLARLLHD VERVHGPGHP LAADIRRTLQ
     WLGRMHG
//