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
//