ID Q0G9C1_9SAUR Unreviewed; 188 AA. AC Q0G9C1; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 24-JAN-2024, entry version 59. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; DE Flags: Fragment; GN Name=c-mos {ECO:0000313|EMBL:ABI30682.1}; OS Elaphe taeniura grabowskyi. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Colubridae; Colubrinae; Elaphe. OX NCBI_TaxID=400063 {ECO:0000313|EMBL:ABI30682.1}; RN [1] {ECO:0000313|EMBL:ABI30682.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17113316; DOI=10.1016/j.ympev.2006.09.009; RA Burbrink F.T., Lawson R.; RT "How and when did Old World ratsnakes disperse into the New World?"; RL Mol. Phylogenet. Evol. 43:173-189(2007). 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. CC {ECO:0000256|RuleBase:RU000304}. 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; DQ902085; ABI30682.1; -; Genomic_DNA. DR AlphaFoldDB; Q0G9C1; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. 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; PTHR44329:SF252; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU000304}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU000304}. FT DOMAIN 1..188 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 26 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABI30682.1" FT NON_TER 188 FT /evidence="ECO:0000313|EMBL:ABI30682.1" SQ SEQUENCE 188 AA; 20421 MW; 93940672D28A261F CRC64; LLHLLGSGGF GSVYKATYHG ATVAVKQVKR CSKNHLASRQ SFWAELNVAR LDHNNVVHIV AASTCTPTSQ DSLGTIIMEY AGNCTLHHVI YGTGYLTENN DGLKCDHGFL STAQAVIYSC DIVAGLMFLH SQLIVHLDLK PANIFITEHN VCKIGDFGCS QKLEDSKSSG LHLCHQGGTY THRAPELL //