ID   A0A0F8W6K7_9EURO        Unreviewed;       424 AA.
AC   A0A0F8W6K7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=L-type lectin-like domain-containing protein {ECO:0000259|PROSITE:PS51328};
GN   ORFNames=ARAM_003512 {ECO:0000313|EMBL:KKK13510.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK13510.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK13510.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK13510.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KKK13510.1}.
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DR   EMBL; JZBS01003799; KKK13510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8W6K7; -.
DR   STRING; 308745.A0A0F8W6K7; -.
DR   OrthoDB; 1332687at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd06903; lectin_EMP46_EMP47; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR035661; EMP46/EMP47_N.
DR   InterPro; IPR005052; Lectin_leg.
DR   PANTHER; PTHR12223:SF40; PROTEIN EMP46-RELATED; 1.
DR   PANTHER; PTHR12223; VESICULAR MANNOSE-BINDING LECTIN; 1.
DR   Pfam; PF03388; Lectin_leg-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51328; L_LECTIN_LIKE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..424
FT                   /note="L-type lectin-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002529324"
FT   TRANSMEM        391..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..233
FT                   /note="L-type lectin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51328"
FT   REGION          235..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          301..348
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        237..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  46676 MW;  E6044AEB0ED31293 CRC64;
     MKIPCSLVLL SAVASAQLVI DSSSFGHGKM IAPNRDGIPG WDLGGEGHIP QILSDKLILT
     PPYPGNTRGY AWSQSTLSES EWTAELQFRA SGVERAGGNL QLWYAKDGKE KIGSASIYTV
     GQWDGFALVV DTHSGRGGSV RGFLNDGTTD YKSHKSVDSL AFGHCDYSYR NLGRPSVVRV
     KHTNAVLEVT VDDKLCFATD KVSLPAGNTI GMTAATPENP DSFEIFKIVL QNSPSGVGKA
     PPVQQQQRQP NENQQQPLAA QGQANTQQVQ SASVDIRSIT EQFVDLGSRI QLINHAANNI
     IRELGNQGNK VENKQNELLQ KLATKEQVGS LEVRLQRLEQ TLQSIQRTLE GNDYRDRFNQ
     LHETLRSSHL SLTENLQGTL LNVITASTPR MGFFIFLVIA FQILLAASYV IYKRRRANMP
     KKFL
//