ID A0A232LVZ6_9EURO Unreviewed; 413 AA.
AC A0A232LVZ6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=L-type lectin-like domain-containing protein {ECO:0000259|PROSITE:PS51328};
GN ORFNames=Egran_03993 {ECO:0000313|EMBL:OXV08244.1};
OS Elaphomyces granulatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Elaphomycetaceae; Elaphomyces.
OX NCBI_TaxID=519963 {ECO:0000313|EMBL:OXV08244.1, ECO:0000313|Proteomes:UP000243515};
RN [1] {ECO:0000313|EMBL:OXV08244.1, ECO:0000313|Proteomes:UP000243515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSC145934 {ECO:0000313|EMBL:OXV08244.1,
RC ECO:0000313|Proteomes:UP000243515};
RX PubMed=25753751; DOI=10.1111/1462-2920.12840;
RA Quandt C.A., Kohler A., Hesse C.N., Sharpton T.J., Martin F.,
RA Spatafora J.W.;
RT "Metagenome sequence of Elaphomyces granulatus from sporocarp tissue
RT reveals Ascomycota ectomycorrhizal fingerprints of genome expansion and a
RT Proteobacteria-rich microbiome.";
RL Environ. Microbiol. 17:2952-2968(2015).
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:OXV08244.1}.
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DR EMBL; NPHW01004229; OXV08244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232LVZ6; -.
DR OrthoDB; 1332687at2759; -.
DR Proteomes; UP000243515; 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:UP000243515};
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..413
FT /note="L-type lectin-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012624360"
FT TRANSMEM 380..401
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 237..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 290..337
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 237..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 46097 MW; F3FF1E51BA3943EE CRC64;
MRLFLSLALC SVTALADSII ESSSFGYNQR ISPNVDNIPG WHLVGEGHRP QILSDKVILT
PLYPGNTRGS IWADATVSEP EWIAELHFRA GGPERPGGNL QLWYVKDGES QIGATSIYTV
GKFDGLALAI DTHGGRGGSV RGFLNDGSTE YKSHNSIDSL AFGHCDYAYR NLGRPSVIRL
KQTPSQFEVT VDDKPCFQTD KVILPAGYKF GISAATPDMP DSFEIFKFIV KSITSTHKAP
PVQQARDDQQ PTNDQGSNDR PTPDDKTSDS HFADIRSRLQ TINTGSNSIL REIMSLNKDA
KDNYRELLQK VVTKDQLASL DSRLQRIEQA LQTVQRDLEG KDYRDRFNQL HETLRSSHAR
LSENLQSSIY HTITSSAPRM GFFIFLVISF QILLAGLYVG YKRRRAALPK KFL
//
