GenomeNet

Database: UniProt
Entry: A0A195BFT5_9HYME
LinkDB: A0A195BFT5_9HYME
Original site: A0A195BFT5_9HYME 
ID   A0A195BFT5_9HYME        Unreviewed;       349 AA.
AC   A0A195BFT5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   13-SEP-2023, entry version 23.
DE   SubName: Full=Ephrin-B1 {ECO:0000313|EMBL:KYM83069.1};
GN   ORFNames=ALC53_06334 {ECO:0000313|EMBL:KYM83069.1};
OS   Atta colombica.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM83069.1, ECO:0000313|Proteomes:UP000078540};
RN   [1] {ECO:0000313|EMBL:KYM83069.1, ECO:0000313|Proteomes:UP000078540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM83069.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM83069.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Atta colombica WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00884, ECO:0000256|RuleBase:RU004375}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00884}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KQ976500; KYM83069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195BFT5; -.
DR   STRING; 520822.A0A195BFT5; -.
DR   Proteomes; UP000078540; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd02675; Ephrin_ectodomain; 1.
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   PRINTS; PR01347; EPHRIN.
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   Membrane {ECO:0000256|RuleBase:RU004375};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          44..179
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51551"
FT   REGION          188..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..281
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   349 AA;  38859 MW;  57B48383CA956E0B CRC64;
     MLLHDSYYQQ ELVQLSRLIE RDLSRETEGF MCLIPFGNIA LCESTTRRFR IDNTDHIIDV
     NKNNAMFEYD QVNIICPVYP PDTYVDDDAE KYIIYNVSKE EYETCRITNP SPRVIAVCDK
     PRKTMYFTIT FRPFTPQPGG LEFLPGHDYY FISTSSKDDL HRRIGGRCTS HNMKVVFKVC
     CSNEAETSAS SATSRNNSVA VTSSTVPSSS STSTAVLGGS AGLPAPPIVY RGGDRFYPEI
     SIDLDPHQPG TAAPTLPHVP SPAVYPVHPH QPQPPIHNGS PSSITPPKTS TGQKKKNKEY
     SDHPNEVVKN EELTYNSASS YARTQVRYTS LILATGSLLM SALLQQLLR
//
DBGET integrated database retrieval system