ID Q8YZC9_NOSS1 Unreviewed; 427 AA. AC Q8YZC9; DT 01-MAR-2002, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 125. DE SubName: Full=Serine/threonine kinase {ECO:0000313|EMBL:BAB72506.1}; GN OrderedLocusNames=alr0548 {ECO:0000313|EMBL:BAB72506.1}; 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:BAB72506.1, ECO:0000313|Proteomes:UP000002483}; RN [1] {ECO:0000313|EMBL:BAB72506.1, 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000019; BAB72506.1; -; Genomic_DNA. DR PIR; AC1875; AC1875. DR RefSeq; WP_010994724.1; NZ_RSCN01000059.1. DR AlphaFoldDB; Q8YZC9; -. DR STRING; 103690.gene:10492559; -. DR KEGG; ana:alr0548; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG1716; Bacteria. DR OrthoDB; 437733at2; -. 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; cd00060; FHA; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000253; FHA_dom. 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 InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 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:BAB72506.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002483}; KW Transferase {ECO:0000313|EMBL:BAB72506.1}. FT DOMAIN 26..78 FT /note="FHA" FT /evidence="ECO:0000259|PROSITE:PS50006" FT DOMAIN 171..424 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 114..143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 427 AA; 47011 MW; EDDEB6166604F5A6 CRC64; MVTLTLLEPQ QKTPLKQWCF ENSSVIRIGR AADNHVILSD NLVSRHHLEI RQVSSGGGGS WQVVSKGTNG TFLNGVLVIQ DALPNNALLQ LAQGGPILQF QVQGIIPPEW QSISGSDSPL SGRGSLAEKS SPELSNNPGS LTCTHEGNSP QNLFCIHCGQ PLSVIQTIRH YQVLRTLGQG GMGTTYLAWD AAGVIVGHPK LLVLKQMNAD MARIAKAQEL FEREAYTLKS LDHPGIPRYY DFFVEGGKKY LAMELVHGQD LEKRIYATGP VIPSLAIAWM IQTCDILDYL HRQEQPLIHR DIKPANLMVR TANNQIAVLD FGAVKEIGTT PGTRIGAEGY CAPEQERGQP LTQSDLYAIG PTIIFLLTGE NPFKFYRQKG RGFRFDVSKI PTITPKLRDV IERTTEPLPR DRFQSAKELA AALAACK //