ID A0A0Q3MGX5_AMAAE Unreviewed; 495 AA.
AC A0A0Q3MGX5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN ORFNames=AAES_109238 {ECO:0000313|EMBL:KQK81703.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK81703.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK81703.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK81703.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK81703.1}.
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DR EMBL; LMAW01002224; KQK81703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3MGX5; -.
DR STRING; 12930.A0A0Q3MGX5; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
DR CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
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:SF58; ACTIVIN RECEPTOR TYPE-1C; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KQK81703.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..495
FT /note="receptor protein serine/threonine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006205790"
FT TRANSMEM 114..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..196
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 197..487
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 495 AA; 55062 MW; ED47D55E93E4EAC8 CRC64;
MWRAPSPVLR VALPLLGAAV SLCAGLKCVC QLCEHTNFTC QTEGACWASV MLTNGREEVI
KSCVSLPELN AQVFCHSSKN ITKTECCYTD FCNNITLRLP VSSEPPSRAS MGSVVLAVTV
VVPVCILSLV VVLVACTCQS RRCARGRAKQ PSVEEPLSEC NLVNSGKTLK DLIYDMTTSG
SGSGLPLLVQ RTIARTIVLQ EIVGKGRFGE VWRGKWCGED VAVKIFSSRD ERSWFREAEI
YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSEYHEQGSL FDYLNRGTVT VEGMVKLALS
VASGLAHLHM EIVGTQGKPA IAHRDLKSKN VLVKRNESCA IADLGLAVKH DSVLNTIDIP
QNPRVGTRRY MAPEILDDAM NMNIFESFKR ADIYSLGLVY WEIARRCSVG GITEEYQLPY
YDVVPSDPSI EDMRRVVCEQ KLRPNIPNQW QSCEALRVMG RIMRECWYAN SAARLTALRI
KKTISQLCVQ EDSKA
//
