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Database: UniProt
Entry: A0A087VE32_BALRE
LinkDB: A0A087VE32_BALRE
Original site: A0A087VE32_BALRE 
ID   A0A087VE32_BALRE        Unreviewed;       511 AA.
AC   A0A087VE32;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 42.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE   Flags: Fragment;
GN   ORFNames=N312_13322 {ECO:0000313|EMBL:KFO10874.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO10874.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO10874.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO10874.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL489820; KFO10874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087VE32; -.
DR   Proteomes; UP000053309; 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; cd14220; STKc_BMPR1a; 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:SF50; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1A; 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}; Kinase {ECO:0000256|ARBA:ARBA00022527};
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:KFO10874.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053309};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        132..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          183..212
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          213..504
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         240
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:KFO10874.1"
FT   NON_TER         511
FT                   /evidence="ECO:0000313|EMBL:KFO10874.1"
SQ   SEQUENCE   511 AA;  57672 MW;  93D9466949AFCF84 CRC64;
     GQNLNSMPHG TGMKTNPDQK KQANGVTLAP EDTLPFLKCY CSGHCPDDAI NNTCITNGHC
     FAIIEEDEHG EPTLASGCMK YEGSDFQCKD SPKAQLRRTI ECCRTDFCNQ DLQPTLPPLD
     STDGLFDGSI RWMAVLISMA VCIIVMIILF SCFCYKHYCK SMAKRHCYNR DLEQDEAFIP
     AGESLKDLID QSQSSGSGSG LPLLVQRTIA KQIQMVRQVG KGRYGEVWMG KWRGEKVAVK
     VFFTTEEASW FRETEIYQTV LMRHENILGF IAADIKGTGS WTQLYLITDY HENGSLYDFL
     KCTTLDNRAL LKLAYSAACG LCHLHTEIYG TQGKPAIAHR DLKSKNILIK KNGTCCIADL
     GLAVKFNSDT NEVDVPLNTR VGTKRYMAPE VLDESLNKNH FQPYIMADIY SFGLIIWEMA
     RRCVTGGIVE EYQLPYYDMV PNDPSYEDMR EVVCVKRLRP VVSNRWNSDE CLRAILKLMS
     ECWAHNPASR LTALRIKKTL AKMVESQDVK I
//
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