ID   Q81ZY6_STRAW            Unreviewed;       663 AA.
AC   Q81ZY6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=pkn5 {ECO:0000313|EMBL:BAC69973.1};
GN   ORFNames=SAVERM_2262 {ECO:0000313|EMBL:BAC69973.1};
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS   14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC69973.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC69973.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA   Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT   deducing the ability of producing secondary metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2] {ECO:0000313|EMBL:BAC69973.1, ECO:0000313|Proteomes:UP000000428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
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; BA000030; BAC69973.1; -; Genomic_DNA.
DR   RefSeq; WP_010983702.1; NC_003155.5.
DR   AlphaFoldDB; Q81ZY6; -.
DR   KEGG; sma:SAVERM_2262; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2373; Bacteria.
DR   HOGENOM; CLU_442057_0_0_11; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR030616; Aur-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24350; SERINE/THREONINE-PROTEIN KINASE IAL-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAC69973.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000313|EMBL:BAC69973.1}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          24..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          373..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  66754 MW;  2027C55110CF77B9 CRC64;
     MAGATDRDGW KVERGDDSWT VPGYIDLKKL GKGGAGRVMI ARHAGTGRNV AIKYLNEELC
     SKVEFRTALR AEARLLGGLT SPHVTRLYEY VEAEQGAAIV MELVYGAALR TLLKKEGSTD
     IEAALVVLKG SLLGLAAAHG VGVVHRDYKP ENVLVNWDGQ TKLVDFGISA RTGDRHNLRG
     TCAYMPPEQW KLEAATPAGD VYAATATLYE CVTGVRPFEG PEPWDFQRQH VDEPVPMDRV
     PEEVRALVRH GMAKDPALRP PSALDFLREL EWAAENAYGP DWEERGQSRL AAVAAALVPL
     AISRLDARLV GSSAELARTV LTARRRSRLR RRGDVLTGAA AVAVVGLLSL MPSGWAAGGA
     EGHAGAHAQA VTRLDARKDT GSATEARGTE HGDTAESDPD SDRAGTSGAQ GGGGHGDGGA
     GLAPADGGTR SDSGSGGGAG DSGTDSPDDG NNTVERNGGT ENGGTENGGT ENGGTENGGT
     ENGGTENGGT ENGGTENGGT ENGGTENGGT ENGGTENGGT ENGGTENGGT ENGGTENGGT
     ENGGTENGGT ENGGTENGGT ENGGTENGGT ENGGTENGGT ENGGTENGGT DNGGTDNGGT
     DNGGTDARHG HSNAGTSDGD PASTGGTDSG NSAGGTGTGT GSGSTSAVTP RQGDPAAVEG
     EPG
//