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Database: UniProt
Entry: A0A5N5MSX0_9PEZI
LinkDB: A0A5N5MSX0_9PEZI
Original site: A0A5N5MSX0_9PEZI 
ID   A0A5N5MSX0_9PEZI        Unreviewed;       471 AA.
AC   A0A5N5MSX0;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   22-FEB-2023, entry version 5.
DE   SubName: Full=Concanavalin A-like lectin/glucanase domain-containing protein {ECO:0000313|EMBL:KAB5558008.1};
GN   ORFNames=GE09DRAFT_1286300 {ECO:0000313|EMBL:KAB5558008.1};
OS   Coniochaeta sp. 2T2.1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1571157 {ECO:0000313|EMBL:KAB5558008.1, ECO:0000313|Proteomes:UP000325492};
RN   [1] {ECO:0000313|EMBL:KAB5558008.1, ECO:0000313|Proteomes:UP000325492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2T2.1 {ECO:0000313|EMBL:KAB5558008.1,
RC   ECO:0000313|Proteomes:UP000325492};
RX   PubMed=31572496;
RA   Mondo S.J., Jimenez D.J., Hector R.E., Lipzen A., Yan M., LaButti K.,
RA   Barry K., van Elsas J.D., Grigoriev I.V., Nichols N.N.;
RT   "Genome expansion by allopolyploidization in the fungal strain Coniochaeta
RT   2T2.1 and its exceptional lignocellulolytic machinery.";
RL   Biotechnol. Biofuels 12:229-229(2019).
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:KAB5558008.1}.
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DR   EMBL; VSMA01000011; KAB5558008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5MSX0; -.
DR   Proteomes; UP000325492; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; 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};
KW   Lectin {ECO:0000313|EMBL:KAB5558008.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000325492};
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..471
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025523037"
FT   TRANSMEM        441..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..246
FT                   /note="L-type lectin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51328"
FT   REGION          250..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          376..410
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   471 AA;  51635 MW;  F950C7D2263F8F11 CRC64;
     MRLPSSIAVL VASIAQAQAQ YLVTELSFGH GVRADAYIRS HRISPEGTPT IPNFSLQGNP
     NPPELLSNKL ILTPPAPGNQ RGAVWSDSTL KNQNWILDVD FRANGPERGG GNLNIWVVRD
     GVHDVGSASI YTAGRFEGLA LVIDGHGGYG GMLRAFLNDG STDYRQQHNV DQLSFGHCSV
     IYRNLGRPSQ LKLRHSDSSF KVEIDGHLCF ESDKVRIPEG YHIGITAASA DNPDSFEVFK
     LVTLTENTND RRGQQAATEN AIPNDGPGTP ERADGQHVVY GKAGFRVGDN AGATSQNNNY
     NNKEPHWDAE IPDAEADKIT SSKAQFADLH NRLQSVNHHL STIFRTIATN VQTGEHRHEE
     MSVMMGELKG LLTSRVLDKL EKLDALEGKI AGLEREVKSV RNELAQKMRE TEHAVKSVVT
     DKHETLADHI KANAAPGHTR LIVAIFGSQL VLVGLFVLYK RRKASGPKKY L
//
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