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Database: UniProt
Entry: A0A0N5D4Y4_THECL
LinkDB: A0A0N5D4Y4_THECL
Original site: A0A0N5D4Y4_THECL 
ID   A0A0N5D4Y4_THECL        Unreviewed;       332 AA.
AC   A0A0N5D4Y4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Ephrin RBD domain-containing protein {ECO:0000313|WBParaSite:TCLT_0000804701-mRNA-1};
GN   ORFNames=TCLT_LOCUS8036 {ECO:0000313|EMBL:VDN05554.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000804701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000804701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN05554.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00884}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00884}.
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DR   EMBL; UYYF01004574; VDN05554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N5D4Y4; -.
DR   STRING; 103827.A0A0N5D4Y4; -.
DR   WBParaSite; TCLT_0000804701-mRNA-1; TCLT_0000804701-mRNA-1; TCLT_0000804701.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR031328; Ephrin.
DR   InterPro; IPR001799; Ephrin_RBD.
DR   PANTHER; PTHR11304; EPHRIN; 1.
DR   PANTHER; PTHR11304:SF29; EPHRIN; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..151
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   REGION          258..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  38952 MW;  730910ECD3FA9144 CRC64;
     MDNDNNTATS SLHILTLNVH LMDTIVIHCP VYELNPKLKD LIQNSILYLI DVIILIHETA
     TIADSDVFQV SETSFDKCQL DTSSKMLGYC KPSRQNKTIR FTLKRHESKL GRFSPGRNYF
     IITASKNDLD GMHQRKFGFC TNNNMKVIIH VLKEPYRMME PIEISADNSD EANKFIASKQ
     KHDEVLFMTE EFNELTWKKK LYDPRIPHFE QQNFSYSYPT IAPFGNRVFQ KFPKTHRIIT
     NDQVIPFLRN HHEMRRQRKS LAKHTSLNGD KNSRNEKTRV RMIVPKFRNE YLSSTKKFFW
     PSEMSEINSA ELERINETLD TVIKNDITNK VK
//
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