ID Q7NN29_GLOVI Unreviewed; 995 AA. AC Q7NN29; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 117. 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=gll0585 {ECO:0000313|EMBL:BAC88526.1}; OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421). OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae; OC Gloeobacter. OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC88526.1, ECO:0000313|Proteomes:UP000000557}; RN [1] {ECO:0000313|EMBL:BAC88526.1, ECO:0000313|Proteomes:UP000000557} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557}; RX PubMed=14621292; DOI=10.1093/dnares/10.4.137; RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., RA Tabata S.; RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a RT cyanobacterium that lacks thylakoids."; RL DNA Res. 10:137-145(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 --------------------------------------------------------------------------- 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; BA000045; BAC88526.1; -; Genomic_DNA. DR RefSeq; NP_923531.1; NC_005125.1. DR RefSeq; WP_011140588.1; NC_005125.1. DR AlphaFoldDB; Q7NN29; -. DR STRING; 251221.gene:10758058; -. DR EnsemblBacteria; BAC88526; BAC88526; BAC88526. DR KEGG; gvi:gll0585; -. DR eggNOG; COG0457; Bacteria. DR eggNOG; COG0515; Bacteria. DR eggNOG; COG5616; Bacteria. DR HOGENOM; CLU_013589_0_1_3; -. DR InParanoid; Q7NN29; -. DR OrthoDB; 9788659at2; -. DR PhylomeDB; Q7NN29; -. DR Proteomes; UP000000557; Chromosome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3. DR Gene3D; 3.40.50.10070; TolB, N-terminal domain; 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; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. 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; PF00069; Pkinase; 1. DR Pfam; PF13414; TPR_11; 1. DR Pfam; PF13432; TPR_16; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00028; TPR; 5. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50005; TPR; 2. PE 4: Predicted; KW Kinase {ECO:0000313|EMBL:BAC88526.1}; Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000557}; KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}; KW Transferase {ECO:0000313|EMBL:BAC88526.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 389..407 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 419..439 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 451..470 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 86..374 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REPEAT 705..738 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" FT REPEAT 773..806 FT /note="TPR" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339" SQ SEQUENCE 995 AA; 108945 MW; 1AB7F53A3667AA86 CRC64; MTPEQWQQLS EILGDALDYQ GAERLAFLDG CKLEAEQRRF IDQLLTIHEQ QPDFLSAPML SLLAGLADEA VPVGAPLRAG QRLGAYRVVR ELGRGGMGVV FLAERADGQF QKQVCIKVLQ TGWAAALQVG RFLSERQILA NLEHPYIARL IDGGSTEAGV PYLVMEFVDG MPIDRYCEAQ QLGLRPRLEL FSKVCQAVQY AHTCRVIHRD LKPSNILVNC EGEPRLLDFG IAKLLDPQGR SSEPTRTDLR VLTPRYASPE QIAGAELTPA SDVYALGVVL YELITGQRPA GAQAAASYEL AWTLSDQTAL LPSRAVGEQP TRAFAPAAAE GGAQGLSRQL EGALDRIVLR SLSKPLDRRY ATVGELLTEV RRYLDGAERT GMRPWPAGAL ARAVAVVALN GAAFWVANEL TARSLLAGPG WFAAAGLALL AGMMIYGLAE APRASGRRRR LAVGTVLLEL GLLAGLFWAA NPFVRLLSNP PNHAIAVLPF VNLGGDKQSA YFSAGMAVDI TNQLGKIADL KVIASSAAAQ YAESPKSLGE IARELGVSSV LTGSVRREGN KVRIVSQLVD PATGEQLWSG DYDRQLSDVF KIQEDVAQQI AGRLQAKLSP AEKERVTQTP TGNITAYDYY LKGREYFERG RNAENDLAIE LFKRALALEP NYALAHAALG NAYFRKAVDY SQGDVWLEAS LGASRKALAI DPQLGEAHRA LGNGLRGKGF FRKAQDAYRR AIALAPNNAA ALGSYGSVNF IRCELEEGVN WTLRAVALDP LSTPLQTNLG DFFTILGDDA RARQALEAAV TLRPDDAYAL WKWSQFYLLN GNFEAARQTA RRLIEAEPRQ LSGLYAAGDV ERFAGNRSQA RAYYRRILQG SGDLLAGTGY LLPTTVLGEL AWRDSRRTEA KALLERSLKL DKAAIARGNE DSFYRFDLAA VYAVQGKRDE ALRWLRAAVD EGYCHYRFLR REPVFASLHS DSEFLQLLKA LEQRVEAMRV RVANL //