ID Q1D546_MYXXD Unreviewed; 689 AA. AC Q1D546; DT 11-JUL-2006, integrated into UniProtKB/TrEMBL. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN OrderedLocusNames=MXAN_4049 {ECO:0000313|EMBL:ABF91254.1}; OS Myxococcus xanthus (strain DK1622). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Myxococcaceae; Myxococcus. OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91254.1, ECO:0000313|Proteomes:UP000002402}; RN [1] {ECO:0000313|EMBL:ABF91254.1, ECO:0000313|Proteomes:UP000002402} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402}; RX PubMed=17015832; DOI=10.1073/pnas.0607335103; RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C., RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R., RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R., RA Kaplan H.B.; RT "Evolution of sensory complexity recorded in a myxobacterial genome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006). 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; CP000113; ABF91254.1; -; Genomic_DNA. DR RefSeq; WP_011554056.1; NC_008095.1. DR AlphaFoldDB; Q1D546; -. DR STRING; 246197.MXAN_4049; -. DR EnsemblBacteria; ABF91254; ABF91254; MXAN_4049. DR GeneID; 41361379; -. DR KEGG; mxa:MXAN_4049; -. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG2114; Bacteria. DR eggNOG; COG4753; Bacteria. DR HOGENOM; CLU_433379_0_0_7; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000002402; Chromosome. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro. DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07302; CHD; 1. DR CDD; cd17536; REC_YesN-like; 1. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver. DR PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00072; Response_reg; 1. DR SMART; SM00044; CYCc; 1. DR SMART; SM00448; REC; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50110; RESPONSE_REGULATORY; 1. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:ABF91254.1}; KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}; KW Reference proteome {ECO:0000313|Proteomes:UP000002402}; KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ABF91254.1}; KW Transferase {ECO:0000313|EMBL:ABF91254.1}. FT DOMAIN 48..311 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 324..443 FT /note="Response regulatory" FT /evidence="ECO:0000259|PROSITE:PS50110" FT DOMAIN 492..622 FT /note="Guanylate cyclase" FT /evidence="ECO:0000259|PROSITE:PS50125" FT REGION 657..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 378 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169" SQ SEQUENCE 689 AA; 75152 MW; 1ED0F2C002C7E58F CRC64; MTNRSTPRGW LPRERAARST LRRAGVRHFP LPMVEDSHSE RQVIGDRYVL ERRLAGGGMG TIWVALDPKL QRRVALKLMA AHCAPAPLAR RQFEWEAQAI ARLQNPHVIQ VHDCDLSGET PYIVMEWLVG EDLEALLNRR GRLSLAMVER LVAQTARALT AAHAAGVIHR DLKPANLFLA RTEHGEQVKV LDFGLALLMS GGAARPHPEE EMAGTPRYMS PEQLRGLEPR LDHRCDLWAL AVVAYRALTG QHPFPLESLR QMRLGNVPPP ATPSSLSPEL GMEVDAFFAR ALDVDPAHRF QSAHELASAL TSAVDAGRPS RPAKILVVDD EPDIVVLMEQ SFRKQIRRSV YQFLFAADGE EALEEMRQHP DIEVVLCDIN MPRMDGLTFL SRVGEISSLT RVVIVSAYGD MNNIRTAMNR GAFDFITKPI DFPDLEATLV KTLKHVRELR RTVRYTEENG LLRMFVPGAV LERLPPLLQG SDAMAGEWVD GTVVFIDVDA FTPVLHQEAP PESLRRLNAN FEAIVPELLA RGGIVDKFMG DAVMAVFRGP GHVDLALEAC HAIHRQLGAL ASRGGEGAPY AHGVCMGLDS GDLVAGSVGA KASGRLDFTV LGDVVNTAAR LAARAGRGQV LVSGRAQARA ASRFRLSPVE TGLFELARDE GHGSPGPDDA TAFLAPDAAA EGRGTTQGG //