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Database: UniProt
Entry: A0A0V0VED9_9BILA
LinkDB: A0A0V0VED9_9BILA
Original site: A0A0V0VED9_9BILA 
ID   A0A0V0VED9_9BILA        Unreviewed;       940 AA.
AC   A0A0V0VED9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Discoidin domain-containing receptor 2 {ECO:0000313|EMBL:KRX61832.1};
DE   Flags: Fragment;
GN   ORFNames=T09_5646 {ECO:0000313|EMBL:KRX61832.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61832.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX61832.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX61832.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX61832.1}.
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DR   EMBL; JYDN01000044; KRX61832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VED9; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.60.120.1190; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR048525; DDR1-2_DS-like.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
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:SF580; DISCOIDIN DOMAIN RECEPTOR, ISOFORM F; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF21114; DDR1-2_DS-like; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00023137}; Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KRX61832.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        450..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..242
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          623..940
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          523..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX61832.1"
SQ   SEQUENCE   940 AA;  106436 MW;  C901ED64485CCA62 CRC64;
     LSFFCHKLFI YFSFIWRKQK KSSSSIKMNS FDKNVFLFLT LLLLFIKVVK SSVVDFDDCH
     LPLGMESREI ADEALTASSS FDESSVGPQN ARGLTYNRIS SGARRQSGQQ LSSPNWASSI
     RTEQLGGAWC PRRQIRPDVH EWIQVDLGAA RIVTAIETQG RYGDGLGQEF TTGYSVEYWR
     PGMHGWYRYR NQHGQEVLQG NNDTSSAVKR EIDSPFVASK LRIIPWSEHT RTVCIRFELY
     GCSFTDRVVE YRMPQGYVGA DRNLADESYD GEQLANGTLV GGLGQLHDRQ VGTEPFTESA
     FRWVGWRRSL TGHWLDIKFI FNELRNFTSV QLHCAHFNRK SVAIFSAAQL FFVQDQEHEH
     HQPLEYSPSG EISSGRGVRW IVIPVQHQTA KILHIRLFFA AEWLLISEIE FDSTPAKIFS
     GPKQNKSPPS TKRSSSSVAI LTYDVIPTEY VALSLGVLLV VVATGAVGLA VFVVRSSRRQ
     AKTTPPPTLI PFYAYGALNR PEQLSAKDLK SGITAGKTSV QYAVNGPLNN NSKRSPLSEE
     DDEEEDTYYY SEYADPDINS NQTAPLLPEP QGTAQRRRNG NNAPGRQAVF DSDKHRLAYS
     LYYASSDVTN DDEHTTSANT TTIAAAAAAN GGNTSEPVES QDRRPTSFVH LCRLHNNDGS
     WKRVAVKTRR NSNADVNQWR DFERELHLLA KLNHVNIVQL LGVIAEQDQC LLVFEHMENG
     DLNQYLRNHD VTQLSGEQLL RFARQIANGM QYLESLNLVH RDLATRNCLL GQDLTIKIAD
     FGMARSLYQS DYYRIEGRFV LPIRWMAWEC VLLGKFSSKT DVWAYGVTLW EIYTLAREQP
     FAKLNDQQVI ENLQYIYYND SLLVKLDRPP VDRCPSEFLP TPTHTMPLAA DWHCTGSRMS
     TSVTCFSYPM LENENRKWQP RCLQTNGATS KHLASGLVCR
//
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