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Database: UniProt
Entry: E2A758_CAMFO
LinkDB: E2A758_CAMFO
Original site: E2A758_CAMFO 
ID   E2A758_CAMFO            Unreviewed;       581 AA.
AC   E2A758;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   RecName: Full=Receptor protein serine/threonine kinase {ECO:0000256|SAAS:SAAS00138132};
DE            EC=2.7.11.30 {ECO:0000256|SAAS:SAAS00138132};
GN   ORFNames=EAG_06597 {ECO:0000313|EMBL:EFN70714.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata;
OC   Formicoidea; Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN70714.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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; GL437267; EFN70714.1; -; Genomic_DNA.
DR   RefSeq; XP_011252737.1; XM_011254435.2.
DR   RefSeq; XP_019882447.1; XM_020026888.1.
DR   GeneID; 105249162; -.
DR   KEGG; cfo:105249162; -.
DR   InParanoid; E2A758; -.
DR   KO; K04675; -.
DR   OMA; LSHNDMI; -.
DR   OrthoDB; 776697at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000333; TGFB_receptor.
DR   InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   PIRSF; PIRSF037393; TGFRII; 2.
DR   SMART; SM00467; GS; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR037393-2,
KW   ECO:0000256|SAAS:SAAS00138218};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000311};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW   Kinase {ECO:0000256|SAAS:SAAS00138139};
KW   Membrane {ECO:0000256|SAAS:SAAS00138203, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR037393-2,
KW   ECO:0000256|SAAS:SAAS00138212};
KW   Receptor {ECO:0000256|SAAS:SAAS00138179, ECO:0000313|EMBL:EFN70714.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00138186};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL        1     26       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        27    581       Receptor protein serine/threonine kinase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003156870.
FT   TRANSMEM    167    191       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      242    272       GS. {ECO:0000259|PROSITE:PS51256}.
FT   DOMAIN      273    580       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   BINDING     305    305       ATP. {ECO:0000256|PIRSR:PIRSR037393-2}.
FT   DISULFID    139    144       {ECO:0000256|PIRSR:PIRSR037393-3}.
SQ   SEQUENCE   581 AA;  65078 MW;  BCEC47D43CB69442 CRC64;
     MAGVIFMHFA LLLTFKLCYL GEGVSALQDQ DISLDSEKLN LPESSEHNFV NNAVGHKRFK
     CHICEDAECS PSSICEDAIT CWKSRVKEID GTESVSRGCY KLEEHKLFMC NKEDNQNAEY
     NKRHVRGLVS GVQYSVECCQ ADFCNVGPYP VLQDSTNSDK GNYVMKLTFA ILGPMIALVV
     AGGILFCFLA HRTRRKRPVS RRNKLILDPD NEPSMLHFSF SSPTSSATCH PHELRATAAG
     DSTLKEYLDG RSLTSGSGSG LPLLVQRTLA KQVALVECLG SGSSGSGFGG EVWRGIWHGE
     NVAVKIYFSR DEAAWARETE VYSQLLPSRH DNILGYVGSD MTSRASCTQL WLVTQYHPLG
     SLFDQLNRHP LTHHQTLNIC LSIANGLLYL HTEIHGTRGK PAMAHRNLKS KNILVKTNGC
     CVIADFALAA TQDRLTADRV DLRQGTKRYM SPEILDQTVN IECLESFRRA DIYSLGLVMW
     EVCRRCISNG VVLEYAMPYY EWLPSNNQEP SIEEMRKLIS FDQRRPPLPN RWHSDPTLAG
     MGKLMRECWH GKPAARLPIL RVKKTLVKLA ANDSRVHLPL D
//
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