ID   Q81ZY1_STRAW            Unreviewed;       564 AA.
AC   Q81ZY1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAC72038.1};
GN   Name=pkn10 {ECO:0000313|EMBL:BAC72038.1};
GN   ORFNames=SAVERM_4326 {ECO:0000313|EMBL:BAC72038.1};
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:BAC72038.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC72038.1, 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:BAC72038.1, 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; BAC72038.1; -; Genomic_DNA.
DR   RefSeq; WP_010985751.1; NZ_JZJK01000079.1.
DR   AlphaFoldDB; Q81ZY1; -.
DR   KEGG; sma:SAVERM_4326; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 9762169at2; -.
DR   Proteomes; UP000000428; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
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   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:BAC72038.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC72038.1};
KW   Transferase {ECO:0000313|EMBL:BAC72038.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..264
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          281..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..428
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..474
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..537
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  59129 MW;  202DD340B91DAE1B CRC64;
     MGEVFAGRYE LVDPIGRGGV GAVWRAWDHR RRRYVAAKVL QQSDAHALLR FVREQAMRID
     HPHVLAPASW AADDDKVLFT MDLVAGGSLV HLIGDYGPLP PSFVCTLLDQ LLSGLTAVHA
     EGVVHRDIKP ANVLLEATGT GRPRLRLSDF GIAMRLGEPR LTETNYVVGT PGYLAPEQLM
     GDEPDFPADL FAVGLVALYL LEGAKPDARA LIEYFLANGT PAAPRGIPEP LWQVVAVLLQ
     PDPAARFRTA TGARKALAAA AELLPEPGPD DELVEIFDQL GPLPPGFGTD GPLKRAPGVT
     AAHAVPQRPG RDATGSTPSG DDSSSGPRPE RPNQRPNRRH HDPGAASGAA SGAAPGTGST
     GAVRPAEDCG EVRPTTGSSH IPPEPDSGPP QPGPPTPLPP PPNSAPLPPQ PASAPGSAPG
     PVQMPPLPDA TPSRSFTMSD TGSFHLPPPR PSTPVRPQPL PERPPTPPAS VALPSPAYAP
     HLEPTRVPSP RPSAAPAASV QHHAYASAGA HTAPAAQVHT RPQAISRRRR RRPKRPGPPA
     KVAVPVLLLA LACFAVGFWA LAQL
//