ID A0A673H6Z8_9TELE Unreviewed; 744 AA. AC A0A673H6Z8; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 29-MAY-2024, entry version 19. DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513}; DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513}; GN Name=LOC107725591 {ECO:0000313|Ensembl:ENSSRHP00000021553.1}; OS Sinocyclocheilus rhinocerous. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Cyprininae; Sinocyclocheilus. OX NCBI_TaxID=307959 {ECO:0000313|Ensembl:ENSSRHP00000021553.1, ECO:0000313|Proteomes:UP000472270}; RN [1] {ECO:0000313|Ensembl:ENSSRHP00000021553.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2023) to UniProtKB. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}. 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 AlphaFoldDB; A0A673H6Z8; -. DR Ensembl; ENSSRHT00000022227.1; ENSSRHP00000021553.1; ENSSRHG00000008852.1. DR Proteomes; UP000472270; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0048513; P:animal organ development; IEA:UniProt. DR GO; GO:0048468; P:cell development; IEA:UniProt. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:TreeGrafter. DR CDD; cd20811; C1_Raf; 1. DR CDD; cd17134; RBD_BRAF; 1. DR CDD; cd14151; STKc_B-Raf; 1. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR003116; RBD_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR23257:SF731; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1. DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF02196; RBD; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00455; RBD; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50898; RBD; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000472270}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022527}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}. FT DOMAIN 113..185 FT /note="RBD" FT /evidence="ECO:0000259|PROSITE:PS50898" FT DOMAIN 192..230 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 432..692 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 268..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 319..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 402..426 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 458 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 744 AA; 84034 MW; 57CC4E2024562472 CRC64; QLPTIWNIKQ MIKLTQEHLE ALLDKFGGEH NPPSIYLEAY EEYTSKLDAL QQREQQLLEA IGNGTEFCSS PTPTQLDVKG PGVQSAPATP NTLAVLQTPT DVTRGNPRSP QKPIVRVFLP NKQRTVVPAR CGMTLRDSLK KALMMRGLIP ECCAVYRVQD GEKKPIGWDT DISWLTGEEL HVEVLENVPL TTHNFVRKTF FTLAFCDFCR KLLFQGFRCQ TCGYKFHQRC MFMGDVSLLH YVAFNRVLCR ITLYSPVSVF SRSLCHPTVS PSKSIPIPQS FRPGEEDHRN QFGQRDRSSS APNVHINTIE PVNIDDLIRD QGLPRSDGAP SQHPARCLRK NRTRTSSPLL SSHPNDIVFD FEPEPVFRGS TTGLSATPPA SLPGSLPNVK VSKSPCPPRE RKPSSSSEDR NKMKTLGRRD SSDDWEIPEG QITLGQRIGS GSFGTVYKGK WHGDVAVKML NVTAPTPQQL QAFKNEVGVL RKTRHVNILL FMGYTTKPQL AIVTQWCEGS SLYHHLHIIE TKFEMIKLID IARQTAQGMD YLHAKSIIHR DLKSNNIFLH EDLTVKIGDF GLATVKSRWS GSHQFEQLSG SILWMAPEVI RLQDKNPYSF QSDVYAFGIV LYELMSGALP YSNINNRDQI IFMVGRGYLS PDLSKVRSNC PKAMKRLMAD CLKKKREERP LFPQTLASIE LLARSLPKIH RSASEPSLNR AGFQTEDFSM YICASPKTPI QFLRHLVFLR WVHP //