ID A0A091FWT3_9AVES Unreviewed; 475 AA. AC A0A091FWT3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-MAY-2022, entry version 44. DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271}; DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271}; DE Flags: Fragment; GN ORFNames=N303_11387 {ECO:0000313|EMBL:KFO73594.1}; OS Cuculus canorus (common cuckoo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus. OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO73594.1, ECO:0000313|Proteomes:UP000053760}; RN [1] {ECO:0000313|EMBL:KFO73594.1, ECO:0000313|Proteomes:UP000053760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO73594.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho- CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA- CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, CC ChEBI:CHEBI:456216; EC=2.7.11.30; CC Evidence={ECO:0000256|RuleBase:RU361271}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU361271}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|RuleBase:RU361271}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. CC {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|RuleBase:RU361271}. 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; KL447456; KFO73594.1; -; Genomic_DNA. DR STRING; 55661.A0A091FWT3; -. DR Proteomes; UP000053760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0030154; P:cell differentiation; IEA:UniProt. DR Gene3D; 2.10.60.10; -; 1. DR InterPro; IPR003605; GS_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR045860; Snake_toxin-like_sf. DR InterPro; IPR000333; TGFB_receptor. DR PANTHER; PTHR23255; PTHR23255; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF08515; TGF_beta_GS; 1. DR PRINTS; PR00653; ACTIVIN2R. DR SMART; SM00467; GS; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF57302; SSF57302; 1. DR PROSITE; PS51256; GS; 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:RU361271}; KW Magnesium {ECO:0000256|RuleBase:RU361271}; KW Manganese {ECO:0000256|RuleBase:RU361271}; KW Membrane {ECO:0000256|RuleBase:RU361271}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU361271}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271}; KW Reference proteome {ECO:0000313|Proteomes:UP000053760}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU361271}; KW Transmembrane {ECO:0000256|RuleBase:RU361271}; KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}. FT TRANSMEM 90..112 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU361271" FT DOMAIN 144..173 FT /note="GS" FT /evidence="ECO:0000259|PROSITE:PS51256" FT DOMAIN 174..468 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 201 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:KFO73594.1" FT NON_TER 475 FT /evidence="ECO:0000313|EMBL:KFO73594.1" SQ SEQUENCE 475 AA; 53252 MW; DCAFDD4540712E60 CRC64; ELIHYECVCE GMSCGNGDRC QGQQCFASLS INDGAKVYQK GCFQVYEQGK MTCKTPPSPD QAVECCQGYL CNMNITAQLP SSKGYSVETL IMVILAPVIV LIVFSAIAVL IIRRIQKNHM ERLNSRDAEY GTIEGLIASN VGDSTLADLL DHSCTSGSGS GLPFLVQRTV ARQITLVECV GKGRYGEVWR GQWQGENVAV KIFSSRDEKS WFRETELYNT VLLRHENILG FIASDMTSRN SSTQLWLITH YHEMGSLYDY LQLTTLDTVS CLRIVLSIAS GLAHLHIEIF GTQGKPAISH RDLKSKNILV KKNGQCCIAD LGLAVMHSQS TNQLDVGNNP RVGTKRYMAP EVLDETIQAD CFDSYKRVDI WAFGLVLWEV ARRMVSNGIV EDYKPPFYDL VPNDPSFEDM RKVVCVDQQR PNIPNRWFSD PTLTSLAKLM KECWYQNPSA RLTALRIKKT LTKIDNSLDK LKADC //