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Entry: A0A0B5DDT4_9ACTN
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ID   A0A0B5DDT4_9ACTN        Unreviewed;       706 AA.
AC   A0A0B5DDT4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Serine/threonine-protein kinase {ECO:0000313|EMBL:AJE41848.1, ECO:0000313|EMBL:QEV40383.1};
GN   ORFNames=BJY54_003693 {ECO:0000313|EMBL:MBB4793081.1}, CP978_19135
GN   {ECO:0000313|EMBL:QEV40383.1}, SNOD_18815
GN   {ECO:0000313|EMBL:AJE41848.1};
OS   Streptomyces nodosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE41848.1, ECO:0000313|Proteomes:UP000031526};
RN   [1] {ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA   Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT   "Sequence of the Streptomyces nodosus genome.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AJE41848.1, ECO:0000313|Proteomes:UP000031526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE41848.1,
RC   ECO:0000313|Proteomes:UP000031526};
RX   PubMed=26497174;
RA   Sweeney P., Murphy C.D., Caffrey P.;
RT   "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT   antibiotic production.";
RL   Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN   [3] {ECO:0000313|EMBL:QEV40383.1, ECO:0000313|Proteomes:UP000325763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV40383.1,
RC   ECO:0000313|Proteomes:UP000325763};
RA   Lee N., Cho B.-K.;
RT   "Streptomyces genome completion.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:MBB4793081.1, ECO:0000313|Proteomes:UP000544950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4793081.1,
RC   ECO:0000313|Proteomes:UP000544950};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) 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};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR   EMBL; CP009313; AJE41848.1; -; Genomic_DNA.
DR   EMBL; JACHMR010000001; MBB4793081.1; -; Genomic_DNA.
DR   EMBL; CP023747; QEV40383.1; -; Genomic_DNA.
DR   RefSeq; WP_043442705.1; NZ_JACHMR010000001.1.
DR   STRING; 40318.SNOD_18815; -.
DR   KEGG; snq:CP978_19135; -.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000031526; Chromosome.
DR   Proteomes; UP000325763; Chromosome.
DR   Proteomes; UP000544950; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 2.40.10.480; -; 1.
DR   Gene3D; 2.40.128.630; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   Pfam; PF13570; PQQ_3; 1.
DR   SMART; SM00564; PQQ; 6.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:AJE41848.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AJE41848.1};
KW   Transferase {ECO:0000313|EMBL:AJE41848.1}.
FT   DOMAIN          22..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          278..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   706 AA;  74214 MW;  762BA9495ACED91B CRC64;
     MTPRHNTGAG AEAELPEYAG HYRLESCLGS GGMGVVHLAR STSGMRLAVK VVHAEFAKDP
     EFRGRFRQEV AAARRVSGAF TASVVDADPE AERPWMATLF IPGPTLSEHV KQNGPLTPGQ
     LRRLMAGLAE ALNDIHRVGV VHRDLKPSNV LLAEDGPKVI DFGISRPKDS ELRTETGKLI
     GTPPFMAPEQ FQRPREVGPA ADVFALGAVL VHAATGRGPF DSDSPYVVAY QVVHDEPDLA
     GVPENLAPLV LRCLAKEPTD RPTPDELMRE LRSVAASYDT RAFIPQQRDG DRPDAPDAPQ
     PGPGTDKAGR SDLAQRPPGR RSRKRTVLAA GALGLMVGTL ASVVLLTEEG SAPVSTPSRT
     RRAEFEGWET KPVPKKPAAP QCSDDAGTLF CTQSGVVLAL DPSDGTVLWQ RSVTGAGRLA
     PVLSGGLVHV AAAEGHLEAL APSSGRTLWR RNVAAQGGWR FAGGSLLLTR ADGTVTGVDS
     TTGETLWSKQ IPGYSLPSLA SFTGDPLAYA TSTSGDGTNT RITAVDPLTG DIGWEAELTG
     TLVPVGTEDG SVFLLDLDTV NGDARAVVRY TPGSGTVRRV ALPVPRLAAQ AGVRKGVVHL
     LAAGGALEAV DMNTGKRLWH VETAVSSGSV PVSDGRYVYV VAADGRLLAL DARTGRLLGQ
     TRSRLGAASD RVTYDLAAPL LVDGHVYGTA PDGTVFAVDG SDPAAW
//
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