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Database: UniProt
Entry: A0A183HY70_9BILA
LinkDB: A0A183HY70_9BILA
Original site: A0A183HY70_9BILA 
ID   A0A183HY70_9BILA        Unreviewed;       658 AA.
AC   A0A183HY70;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN   ORFNames=OFLC_LOCUS12432 {ECO:0000313|EMBL:VDP11304.1};
OS   Onchocerca flexuosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=387005 {ECO:0000313|Proteomes:UP000050787, ECO:0000313|WBParaSite:OFLC_0001243301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:OFLC_0001243301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP11304.1, ECO:0000313|Proteomes:UP000267606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605}.
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DR   EMBL; UZAJ01039842; VDP11304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A183HY70; -.
DR   STRING; 387005.A0A183HY70; -.
DR   WBParaSite; OFLC_0001243301-mRNA-1; OFLC_0001243301-mRNA-1; OFLC_0001243301.
DR   Proteomes; UP000050787; Unplaced.
DR   Proteomes; UP000267606; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.10.60.10; CD59; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF68; RECEPTOR PROTEIN SERINE/THREONINE KINASE; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          267..297
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          298..638
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          50..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   658 AA;  73582 MW;  6580DDA85C80353F CRC64;
     MFTNYSVVAL PRMELVKLWI SEVVETFTAL LLLGILLSVN GNLQEYGRKQ DHDSAERYDA
     DGDLSMPTDV QGRPYQFNSS RVESEADRKR KSAPAKYEDE RSFCYCNYAP EFCGGFTNFT
     CIKHLEASCF HFTEEIYDKT LKQVETVHLF GCAPLTHGSG GSYFTCKAHL VAHARPKSIA
     CCQEGNYCNR NLSVPAYINV SPEGIIVDHY TFSYMTITVI IYVVIFSLFS GIALLLFWRR
     NFIVIYFTAE KLKPSLQKST VQLMDAGEIE KAPMLYDVSS GSGSGFASLN QRTVAQDLQF
     LSIVGKGRYG EVKKACYRGD RIVAVKTFYT TEEDSWKNEK EIYQTQMLNH ENILQFVAAD
     IGSEDSITRM LLITDFHAYG SLFEYLQRGE TLSVSEALHL AYSAVCGLEH LHSALHGTGT
     PQKPAIAHRD VKSKNIIVKR PYVCCIADFG LALTEDMVKI KTDINIQVGT KRYMAPEVLD
     KSLNVKNFHH FKMADIYSFA LVIWEILRRI QEDNRLSRAS ESDSGIGSSG SGSGTTKLMS
     GFIANLDASG YITNVSSNVV DHQSISENSM PLKARPPMQP FDGMVDPDPS FEQMRRLPCL
     KEICELISEC WNASIDCRHT ALRVKRKIKD TVLKHKGLGG SQTSGSTKQD CSAKSLSV
//
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