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Database: UniProt
Entry: M7BSV8_CHEMY
LinkDB: M7BSV8_CHEMY
Original site: M7BSV8_CHEMY 
ID   M7BSV8_CHEMY            Unreviewed;       404 AA.
AC   M7BSV8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   03-JUL-2019, entry version 33.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   ORFNames=UY3_11644 {ECO:0000313|EMBL:EMP31222.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia;
OC   Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP31222.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z.,
RA   Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y.,
RA   Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M.,
RA   Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J.,
RA   Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G.,
RA   Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield
RT   insights into the development and evolution of the turtle-specific
RT   body plan.";
RL   Nat. Genet. 45:701-706(2013).
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.
CC       {ECO:0000256|RuleBase:RU000304}.
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DR   EMBL; KB546351; EMP31222.1; -; Genomic_DNA.
DR   STRING; 8469.XP_007064765.1; -.
DR   Proteomes; UP000031443; Unassembled WGS 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; 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; 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|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031443};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000304,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:EMP31222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304,
KW   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     26     48       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       76    105       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      106    398       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
SQ   SEQUENCE   404 AA;  46185 MW;  361D617711E2DAB2 CRC64;
     MERDKRHFAG HVKENEPQSS WGPVELVAVI AGPVFLLFVV MIVVVFVFHH HQRVYHNRQR
     LDMEDPSCEM CLSKDKTLQD LVYDLSTSGS GSGLPLFVQR TVARTIVLQE IIGKGRFGEV
     WRGRWRGGDV AVKIFSSREE RSWFREAEIY QTVMLRHENI LGFIAADNKD NGTWTQLWLV
     SDYHEHGSLF DYLNRYTVTI EGMIKLALSA ASGLAHLHME IVGTQGKPGI AHRDLKSKNI
     LVKKNGMCAI ADLGLAVRHD SVTDTIDIAP NQRVGTKRYM APEVLDETIN MKHFDSFKCA
     DIYALGLVYW EIARRCSSGG IHEEYQLPYY DLVPSDPSIE EMRKVVCDQK LRPNIPNWWQ
     SYEALRVMGK MMRECWYANG AARLTALRIK KTLSQLSIQE DVKI
//
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