ID   Q81ZV3_STRAW            Unreviewed;       692 AA.
AC   Q81ZV3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:BAC74831.1};
GN   Name=pkn31 {ECO:0000313|EMBL:BAC74831.1};
GN   ORFNames=SAVERM_7120 {ECO:0000313|EMBL:BAC74831.1};
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:BAC74831.1, ECO:0000313|Proteomes:UP000000428};
RN   [1] {ECO:0000313|EMBL:BAC74831.1, 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:BAC74831.1, 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};
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; BA000030; BAC74831.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q81ZV3; -.
DR   KEGG; sma:SAVERM_7120; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_397894_0_0_11; -.
DR   Proteomes; UP000000428; Chromosome.
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; 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; 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; 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:BAC74831.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:BAC74831.1};
KW   Transferase {ECO:0000313|EMBL:BAC74831.1}.
FT   DOMAIN          18..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          289..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..414
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..547
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   692 AA;  72296 MW;  68ACCA1976D9B637 CRC64;
     MPSGSPQSGV GRVIAGRYLL LNRLGSGGMG HVWLAHDQRL ACEVALKEIV FRSPAEAGQE
     RTARVARARA EARHAAGLRG HPHVVTVHDV LEHEGLPWIV MEYVAGALDL RDLVRRRGPL
     APAECARIGL AVLDALTAGH ERGIMHRDVK PANILLAPDR TGAAYARVLL TDYGISVQPD
     AGETRYTLTS ALVGTPGYLA PERATGGPPT ATADLFSLGC TLYFGVEGCG PFERDTHLAE
     VTAVVLEEPR PPVRAGALEP VLAAMLAKDP GQRITAEDTE AALSAIVTPQ PHPRTQFDLG
     SQPPWAEAGW TTETGYPGHG PGAGPGGNGT SGAYGPGGTG SGAGSAPGSP PPGATAGTAG
     RGTPSEPGPV RGPAAGPSGQ DPNAAPYAHD PATPSYGQEP GAPRPGPGPT ASPYGRSPTA
     PSYGQSPAAT PYAHDPTASP YGQSPAATRT ARPQCLLVRF GCHRPARRSG VRCRWFRFRS
     AASQAPSCPS VRHRLHPRPR PRAGRCLVRG GASAARRRRR EALRSGRGPR RAAQGRRLRR
     RRLARRRLPG HAEAGRGPDL RREGAGRPGH GGRRGDVRRG GAAARSGRVR AAHAGDPGEA
     RRRAQLRRGA DAGGIRGGRA AHRLSGAGRA RCGVRAARPS PHARHVVRGH GEHAEAGLSG
     RPFPPQGPAG LLCRTARSAS ARLHPAQRRH HP
//