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Database: UniProt
Entry: A0A0M5IYV7_DROBS
LinkDB: A0A0M5IYV7_DROBS
Original site: A0A0M5IYV7_DROBS 
ID   A0A0M5IYV7_DROBS        Unreviewed;       506 AA.
AC   A0A0M5IYV7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   ORFNames=Dbus_chr2Lg1409 {ECO:0000313|EMBL:ALC39324.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC39324.1, ECO:0000313|Proteomes:UP000092553};
RN   [1] {ECO:0000313|EMBL:ALC39324.1, ECO:0000313|Proteomes:UP000092553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC39324.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-serine + ATP = [receptor-protein]-O-
CC         phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA-
CC         COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421,
CC         ChEBI:CHEBI:456216; EC=2.7.11.30;
CC         Evidence={ECO:0000256|SAAS:SAAS01128400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[receptor-protein]-L-threonine + ATP = [receptor-
CC         protein]-O-phospho-L-threonine + ADP + H(+);
CC         Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-
CC         COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.30; Evidence={ECO:0000256|SAAS:SAAS01128404};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|SAAS:SAAS00595019}.
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DR   EMBL; CP012523; ALC39324.1; -; Genomic_DNA.
DR   RefSeq; XP_017851974.1; XM_017996485.1.
DR   GeneID; 108606393; -.
DR   OrthoDB; 776697at2759; -.
DR   Proteomes; UP000092553; Chromosome 2l sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092553};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092553};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00138186};
KW   Transferase {ECO:0000256|SAAS:SAAS00138167};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00138220,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00488859,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    124    148       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      166    196       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      197    498       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   506 AA;  56972 MW;  52BF899F681DFDE9 CRC64;
     MAPKSRKKKA HVSRSLTCYC EGSCPNNVSN GTCETKSSCF SSVQEVYDET TNSYEEERTY
     GCMPPEDNGG FLMCKVAASQ VHGKHIVCCD NEDLCNRNLQ PAFTPKLTTP SPDLPVSSES
     MQTFMLLGSV VMCAFVLTVV LLIVCLIYKR REKQRKPRLI NSMCNSQLSP LSQLVEQSSG
     SGSGLPLLVQ RTIAKQIQMV RLVGKGRYGE VWLAKWRDER VAVKTFFTTE EASWFRETEI
     YQTVLMRHEN ILGFIAADIK GNGSWTQMLL ITDYHEVGSL HDYLSTSVIT PQKLQLLAYS
     FSSGLAHLHD EIFGTPGKPA IAHRDIKSKN ILVKRNGQCA IADFGLAVKY MSELDEIHIA
     QNTRVGTRRY MAPEVLSQAL NPQQFEEFKR ADMYSVGLVL WEMARRCYTP ITGTKTTTCE
     DYALPYHDVV PSDPSFEDMH AVVCIKGFRP PLPARWQEDD VLATVAKIMQ ECWHHNPTVR
     LTALRVKKTL GRLDMDALND MPMKIV
//
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