ID   Q8YVQ5_NOSS1            Unreviewed;       546 AA.
AC   Q8YVQ5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Serine/threonine kinase {ECO:0000313|EMBL:BAB73618.1};
GN   OrderedLocusNames=all1919 {ECO:0000313|EMBL:BAB73618.1};
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:BAB73618.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB73618.1, 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};
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; BA000019; BAB73618.1; -; Genomic_DNA.
DR   PIR; AI2045; AI2045.
DR   RefSeq; WP_010996083.1; NZ_RSCN01000031.1.
DR   AlphaFoldDB; Q8YVQ5; -.
DR   STRING; 103690.gene:10493938; -.
DR   KEGG; ana:all1919; -.
DR   eggNOG; COG0515; Bacteria.
DR   OrthoDB; 581647at2; -.
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; 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:BAB73618.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Transferase {ECO:0000313|EMBL:BAB73618.1}.
FT   DOMAIN          12..279
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          358..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..546
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   546 AA;  59585 MW;  648B45C5D5CF0E40 CRC64;
     MLAGKILQGG KYTLIQEVGR GGFGITFKAT HHYLGHEVVM KTINERLRQH PDFAKFERQF
     QDEARRLATC IHPNIVRVSD FFVEDGLPYM VMEYIPGETL GDAFVLPAIP LPEETAIHYI
     RQIGAALQVV HNNGLLHRDV KPDNIILRQG TQEVVLIDFG IAREFNSGVR QTHTGLVSEG
     YAPIEQYLTQ APRTPATDVY GLAATLYALL TGQVPLPALL RDREQMPAPR ELQPHLSAAV
     NQAVMRGMAV ESRFRPPTVA EWLQLLPGSG VNLPIHALPT HVVPTIDLSV HLQEKFSGAK
     TSGSGKKPSP LKNLALIAQK SGTSQVFLGV IIAVVAAAAG FSATSLFSRS WTQPSAKPLF
     EERPMVPVGG KPQVDSSQER DNTRQNSQNY SASETTPVSP SRRRRRNLTN QPSESSNPNS
     NSSEQSPQPN TGESQRRNYE QPGLSPNTSS TPSLVEKLRE IRSSRTAKPA NTTDTSPPSS
     TQNSTTPVEP PANSIVVPVQ PAEPKNSDSS VVVPTVEVKQ NSSTDSQIPA PSQKNEKFPE
     NTQINN
//