ID   A0A386WIS2_9ACTN        Unreviewed;       461 AA.
AC   A0A386WIS2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   02-DEC-2020, entry version 9.
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=CSH63_07990 {ECO:0000313|EMBL:AYF27370.1};
OS   Micromonospora tulbaghiae.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=479978 {ECO:0000313|EMBL:AYF27370.1, ECO:0000313|Proteomes:UP000267804};
RN   [1] {ECO:0000313|EMBL:AYF27370.1, ECO:0000313|Proteomes:UP000267804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNY-010 {ECO:0000313|EMBL:AYF27370.1,
RC   ECO:0000313|Proteomes:UP000267804};
RA   Kim M.C., Machado H., Jensen P.R., Fenical W.;
RT   "Integration of genomic and chemical information greatly accelerates
RT   assignment of the full stereostructure of myelolactone, a potent inhibitor
RT   of myeloma from a marine-derived Micromonospora.";
RL   Submitted (OCT-2017) 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; CP024087; AYF27370.1; -; Genomic_DNA.
DR   KEGG; mtua:CSH63_07990; -.
DR   Proteomes; UP000267804; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AYF27370.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AYF27370.1};
KW   Transferase {ECO:0000313|EMBL:AYF27370.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        320..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          14..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          289..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..428
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  46951 MW;  2DC9F690F288D6C0 CRC64;
     MGVLSSDVVL SGRYRLDDRV ATGGMGDVWR ATDLVLGRPV AVKVLLPALA SDPDFIARFR
     SEARIMASLR HPGVVQVFDC GEDDLPGGGR ADYLVMEFVA GEPLSRRIEA AGQLEVVETM
     SIVAQVAQAL HAAHGRGIVH RDVKPSNLLV QDDGTVVLVD FGVARSTNVT SITSTNAVPG
     TALYMAPEQA AGRPVSGATD VYALGAVAYC CLTGSPPFTG DNPLQVAVRH LDDEPPELPA
     EIPASVRELV SRALAKDPAD RYPSAAAMAD AARAARTDSP TATVALRGAA GPARSRNDQP
     AVRPGAAVAT SRRRSRRGTL VGALGAVLVA MGALGALVAA ANDTGEPATK IDKTAPAVAP
     SEQAAEPVVD EPSADDDYTY RPVGPGDRPS ATPSVTPSSS PTPSAQPSVT DEPAPTDEPS
     STPSSAPTTT APTTPPAPAP VPTTAGPGTG GGRDTGGQPA T
//