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Database: UniProt
Entry: A0A158PRW1_BRUPA
LinkDB: A0A158PRW1_BRUPA
Original site: A0A158PRW1_BRUPA 
ID   A0A158PRW1_BRUPA        Unreviewed;      1281 AA.
AC   A0A158PRW1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   ORFNames=BPAG_LOCUS11342 {ECO:0000313|EMBL:VDN92528.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001138001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0001138001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN92528.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
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DR   EMBL; UZAD01013225; VDN92528.1; -; Genomic_DNA.
DR   STRING; 6280.A0A158PRW1; -.
DR   WBParaSite; BPAG_0001138001-mRNA-1; BPAG_0001138001-mRNA-1; BPAG_0001138001.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   CDD; cd00096; Ig; 2.
DR   CDD; cd00192; PTKc; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF503; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 4.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        60..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        813..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..185
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          291..383
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          612..714
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          723..809
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          895..1220
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        1083
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         934
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1088
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         1101
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ   SEQUENCE   1281 AA;  147730 MW;  590157958A28E29C CRC64;
     MAVQCSNPWP FRFGSSRHEV YSRSLYTAPT TFSTKEHYHI SFDYSLPTPH CRTSCWRFML
     LFYPFIRYLL IAVCFITIDA SLYPPVIIGN KDFQEYKGQP YTEKKDGETL ELNCSTTEAV
     KWILPDNIFH TNFDPKERTG RVIESSFDIG FRSLRIEQLK SSDTGEYVCV AEHSGFSSSV
     YVYVSSNKNG KSVRTGSFLN SGPLIISKEL RGLNVILPCR TDKFIESGVE LFINHIKQTG
     EIQFDPRIGF IVDRGLLNDR AEVPVRCEYL GHTSEMIIVP IKNDKEMEYS PVIEVSNTWP
     YVSQELNMNC TFHTRDGFRY MLTWKCPQCE NETDRVVSNR YMKIGDGIKK LLFIRDLRES
     DSGNYECIVT NRDDGHDVRR STHRLQVSPT RGQLKVIDFS ENIDSEEGKT VRLFHIARAF
     PSDEYSSEWR KYSKTISSGE EFMEIIKKDI RSEMNADLHE DELSIINATV DDSAIYQLVI
     RVSQDYIYRK NWTLSIRPID IQPHITIHDQ FGQLLLSDVL IDSKIIVTCL VKDTRSHKLR
     LLYVTRGGEW EQPDDSKELS GFTFESAIKW ITYAKEHMRI RCEDDEANKV DEKNLVVSEV
     ETINASFIAK KPIDLLNEDN SIYEKDHLEL ICILPLNDDL LVPNLLACLE NMMYFSDVVW
     MRDDVQLAYP ERHVTIYSQK FITTLDDISS NESGDYECIA KSKNTHIYRS YTLHIKINVV
     VAPHIVGTEE EYEHLAKYGE KAELVCPIEG EPEPLYRWLK NGIEYNGYGS LTKKIDFPRV
     LVEDKATYTC VAKNRAGSQQ LVDEPAYIRS SKYWWTLGFA TVSVLVLLLM ALLFLLKQRC
     KSKRQEERLR ALYNQLMSES NGEYHDGSIG LKQPLHERVE QLPYDRRYEI NKDKLFFKQS
     LGGGHFGQVY LGELSKPRVS DSLAVSDVLK VAIKAPRDGR NVHHQKALAD ELKIMIAVGV
     HPNVLCLIGA VTKQMSSGQL YMIMEYCEND NLKDYLSKNS AGFLNEVEIS REPLSSDGYL
     TPTRNAQHKA QIYLAELKLQ WAIEVDEERM AGKMITTSDL ISFGYQVANG MEYLSSKTCI
     HRDIAARNIL VTKKRAIRIA DFGLARKDST VYHIRSSQSV PLPLKWMALE SILYHNFTEQ
     SDVWSYGVLL WEIFSLGKVP YPQIDNNDLL SYLLEENRME QPKLAPDDIY NLMRQCWLSD
     PSNRPMFSEC KVLMKTHLSR ASPPLSTRLD KILEEDQIMM EKYSEWRDSE EIEQDLRSQA
     TRNGFIAIPT QEPQTNSNIY M
//
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