ID   Q8YP33_NOSS1            Unreviewed;       597 AA.
AC   Q8YP33;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Serine/threonine kinase {ECO:0000313|EMBL:BAB76067.1};
GN   Name=pknD {ECO:0000313|EMBL:BAB76067.1};
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB76067.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB76067.1, ECO:0000313|Proteomes:UP000002483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC   {ECO:0000313|Proteomes:UP000002483};
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB76067.1; -; Genomic_DNA.
DR   PIR; AH2351; AH2351.
DR   RefSeq; WP_010998505.1; NZ_RSCN01000027.1.
DR   AlphaFoldDB; Q8YP33; -.
DR   STRING; 103690.gene:10496417; -.
DR   KEGG; ana:alr4368; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 428678at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAB76067.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB76067.1}.
FT   DOMAIN          10..281
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          341..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..371
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..439
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   597 AA;  65148 MW;  C1F9DC745B5BB85E CRC64;
     MTSILLNNRY QVIQILGAGG FGETLLAEDT HMPSRRRCVI KRLKPVSNDP QAYQSIQQRF
     EREAATLEFL GEHSNQIPRL YAYFSENGQF YLVQEWIHGH TLRQLLVSQG IQGEGIVKTI
     LLSLLSVLDY VHSKGIIHRD IKPDNIILRD FDQKPVLIDF GAVKETIRSV VSSPGYATRS
     LVIGTPGYMP SEQAVGRPVY ATDIYSLGLT AIYLLTGKSP EELPTHPQTG EILWQNMAPH
     VSQQLVSVLN QAIKPHAGDR YSTASKMLYA LSSSVTAQPS ILPSTTPTQQ TQALSIPAIK
     PQGEPLRWAE PNRQKSLLIF GGLIAGGLMA GVAMSTLTRQ PQSQTPVVSN PIPSPVSQIP
     TTAPNTPPVS PDSILPDSTE QPVAPDTPPQ PETRQENPNP PAVFTPAPDN TPITADTPAP
     QPTSIPEPEN QPVPAPPTQV DSLPRRKANT TRSSVPAFPT GTARSTVEAT LGKPNRDLRG
     VWGNTRAVVY RLVPNQVDLG YLFDRKSGVL RQTEVSFAQS VDPEIMQATL NGMLGGQSTA
     KIQQGLQKIQ QRQSDNFSFT SGGVKGQIVR QNCDLIYISV WDSDLHDFVN PASAKRC
//