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Database: UniProt
Entry: R4T9C6_9PSEU
LinkDB: R4T9C6_9PSEU
Original site: R4T9C6_9PSEU 
ID   R4T9C6_9PSEU            Unreviewed;       614 AA.
AC   R4T9C6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=AORI_4574 {ECO:0000313|EMBL:AGM07158.1};
OS   Amycolatopsis keratiniphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX   NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM07158.1, ECO:0000313|Proteomes:UP000013968};
RN   [1] {ECO:0000313|EMBL:AGM07158.1, ECO:0000313|Proteomes:UP000013968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM07158.1,
RC   ECO:0000313|Proteomes:UP000013968};
RX   PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA   Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA   Ding X., Zhang L., Zhao G., Zheng H.;
RT   "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT   closing.";
RL   BMC Genomics 14:289-289(2013).
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; CP003410; AGM07158.1; -; Genomic_DNA.
DR   RefSeq; WP_016334906.1; NC_021252.1.
DR   AlphaFoldDB; R4T9C6; -.
DR   KEGG; aoi:AORI_4574; -.
DR   PATRIC; fig|1156913.3.peg.4648; -.
DR   HOGENOM; CLU_428181_0_0_11; -.
DR   Proteomes; UP000013968; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
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:AGM07158.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000013968};
KW   Transferase {ECO:0000313|EMBL:AGM07158.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        315..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..264
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   614 AA;  65748 MW;  99BDDE4305ABA65B CRC64;
     MKPLRAGESR QVGPHRIIAE LGEGGMGRVV LGLAPDGRLV AVKQIHAEFA HDPGFRERFR
     REIAASRLVS GAYTAAVMDA DHEAESPWLA SIFVTGPDLR TAVDATGPLP VEAVRRLASG
     LAAALTDIHR AGLIHRDLKP SNVILSSDGL RVIDFGIARA AEEAQNLTHT GAIIGSPAFM
     SPEQAGGGPI TPATDMFSLG SILVMAATGR GPFSGASAPQ TLYDVVHTEP DLSTVPTEIR
     RIAEPCLAKD PARRPTPGQL QDFLGPVPSD TEPWPEAVHA RIRHQEAEVR SVLSLPIPAW
     QPPPRPLPVK KRRPGLPITV ALVVVAALIG TLIVVIQAIT SPPDPGIAAM PVAEALTLDR
     LRRVDTCKVL DGRYSEDLGS LEPDSNPMSP DRCTYKGPKG LYFDLRLGEP VVNGGIGTTN
     RTAEGLPLLR ASFSGGCHSL IPITDEPALY VMLYNDTNVG DKCAVADSAL TVVLARLRTH
     EVDRQDDAAG VLPLDPCALP DATVVAQTMT DVRAVTAGLR NCRWQRKDER LDVRLQRSLY
     IDADNGDPVD LGNGVTGYVT DASESSCQLS WPHRTLPDGD AEYISVWLQG YSGERACERV
     RAVAASVLNR LPKR
//
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