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Database: UniProt
Entry: A0A182DXY6_ONCOC
LinkDB: A0A182DXY6_ONCOC
Original site: A0A182DXY6_ONCOC 
ID   A0A182DXY6_ONCOC        Unreviewed;      1221 AA.
AC   A0A182DXY6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-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=NOO_LOCUS522 {ECO:0000313|EMBL:VDK62308.1};
OS   Onchocerca ochengi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00522-RA};
RN   [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t00522-RA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
RN   [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t00522-RA}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDK62308.1, ECO:0000313|Proteomes:UP000271087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; UYRW01000051; VDK62308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182DXY6; -.
DR   STRING; 42157.A0A182DXY6; -.
DR   WBParaSite; nOo.2.0.1.t00522-RA; nOo.2.0.1.t00522-RA; nOo.2.0.1.g00522.
DR   Proteomes; UP000077448; Unassembled WGS sequence.
DR   Proteomes; UP000271087; Unassembled WGS sequence.
DR   GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0038127; P:ERBB signaling pathway; IEA:UniProt.
DR   GO; GO:0000003; P:reproduction; IEA:UniProt.
DR   CDD; cd00064; FU; 3.
DR   Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR032778; GF_recep_IV.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000494; Rcpt_L-dom.
DR   InterPro; IPR036941; Rcpt_L-dom_sf.
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:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 6.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        711..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          779..1047
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         814
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1221 AA;  139083 MW;  BE00A3CC77D945F4 CRC64;
     MITLRNLEII WGDKQHDDVV ALHISNNMNL KYVNLPKLRS VQRGQIVLMH NPYLCNWNTT
     VSYDELLGKP SESRVQLIDN FEECLGDIHT KCSTVCGKHC WGPIKGMCQI VYREICPEEC
     PSQMCYQSKN ETHCCDEECA GGCFGEGKSA CIACAKLEQD SKCVDKCNGL TDYDWTLKMT
     VPHPDPRYTY DRYCVKQCPE ETLIQGEYCV IHCAESYWHD PERNTRICEK CEHDICPKTC
     YLDEPIDSSN IGDLENCTLI EGFVEILRHP FEPHRKFFSD GRPPIDIEKL TVQMLKALSK
     VKIVTEYVNV QAADYSPESL NFLRSLRTIE GRKLPDQIAL LVTSNHNLKQ LGLRSLKKIK
     NGRVYIGNNP KLCYLDTIND YWKEIMQGNV TTDLKIISNQ LPNVCENVGK ICDETCDENY
     GCWGEGPTMC VKCADYEMDD KCSSFCPSEG YYVEGKKCQK CQSQCKTCNG PTTLNCTECL
     NIRMQQGNNW ECLAKCPTTH YLHKNTCLPC SPACYNFGCT GPNAVAGKDG CNKCKYAKRF
     DHGKQLMCLH TTGKPKDVCR DNNLTRYYAT ASSNEMLVVE FECNECSEEC LSCSGYGTSV
     NRHKCKCAHY LTKTTSGNEY CTMKCEMNSF MIRPKSLDTI GECERCHELC DPSMGCIGRT
     TANCTRCAKA GVLLENQLVC LEQCPINHPF IANDKICHTL DPEEQASKRR MYIIIISALC
     AAIFIVALVG ITVKYIKYKK RYKEELEMNL PSIPEYEPMD PSMRPNMTRL CIITSENLEK
     TQQSLGQGAF GTVFLGYWWP KGKDDGEKLA VAIKVVNDGS STAAHQEMLQ EAGIMACMRH
     EHLLRLVGVC LSNGMQIVTP MRPLGSLKNY LKKHRQKLGA RDLLLYCYQI ASAMEYLYKN
     RLVHRDLAAR NVLVKRTNHV EVTDFGLAKL LEKGKSEVVV GGKVAVKWLA LESLEKQIYT
     HYTDVWAFGV TCWEVLTFGQ TPFQSVPPDQ IRKHLATGNR LEQPNNCTQE VYQTFLQCWL
     RNPESRPSFV ILKEKFNQYC KAPHLYVLDR HYKQQFESVL LENQHELTDE MMYNNELPDQ
     FKFSGITTTT TSTSVPPSPT TPCWVTFQQG DINMRQERRL GSTDSGRYQS DPVCDGRTEL
     SMDEGNYLVP NNKLILYTPV VVRENGETEL MESAEYYNDK LGTDYYNQLR SLSQETKEKA
     KSIKIATYQN DYYFAETETS L
//
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