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Database: UniProt
Entry: A0A1V9XZE3_9ACAR
LinkDB: A0A1V9XZE3_9ACAR
Original site: A0A1V9XZE3_9ACAR 
ID   A0A1V9XZE3_9ACAR        Unreviewed;       237 AA.
AC   A0A1V9XZE3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Origin recognition complex subunit 5-like {ECO:0000313|EMBL:OQR78830.1};
GN   ORFNames=BIW11_02659 {ECO:0000313|EMBL:OQR78830.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR78830.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR78830.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR78830.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
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}.
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:OQR78830.1}.
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DR   EMBL; MNPL01001767; OQR78830.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9XZE3; -.
DR   STRING; 418985.A0A1V9XZE3; -.
DR   InParanoid; A0A1V9XZE3; -.
DR   OrthoDB; 5402021at2759; -.
DR   Proteomes; UP000192247; 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:UP000192247};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          1..53
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
SQ   SEQUENCE   237 AA;  26222 MW;  38EA2BE644D0314C CRC64;
     MCHRSFTPQP GGHEFRPGRD YFLISTSSGR PDGLMQERGG ACREHNMRLV LKICCKPPQP
     SATFADQGSV HGRTESQESG VATAQVGVDP IAENLGSNSS LLETSFTTQP TGQHHRSIYG
     VGYRYRSGVR DREIDGPVNT EERRHIDSNR RLVPTGQTLL PLEHPKAFKD QRQPRFGASS
     AFVNLPCPAI KESFTDGGLT GQRKGPFIFS WADERPTLQW TESPHTAGIQ CGCLYRL
//
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