ID A0A168HZN2_CORDF Unreviewed; 431 AA.
AC A0A168HZN2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Legume-like lectin {ECO:0000313|EMBL:OAA78529.1};
GN ORFNames=LEL_05352 {ECO:0000313|EMBL:OAA78529.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA78529.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA78529.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA78529.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA78529.1}.
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DR EMBL; AZHF01000003; OAA78529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168HZN2; -.
DR STRING; 1081108.A0A168HZN2; -.
DR OrthoDB; 1332687at2759; -.
DR Proteomes; UP000076881; 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}; Lectin {ECO:0000313|EMBL:OAA78529.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..431
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007897770"
FT TRANSMEM 401..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..237
FT /note="L-type lectin-like"
FT /evidence="ECO:0000259|PROSITE:PS51328"
FT REGION 242..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 324..364
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 242..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 48017 MW; 4F67802EB5C074F8 CRC64;
MRTASLVLAA LAAGLGQAQY LINELSFGID SKLSHDESPG TIPHYHVNGQ PNRPDVLSNK
VILTPMGIGN QRASIWGERT LQRDDWVADI DFRANGPERA SGNINIWLAK DGRATVQENS
VYTVGRFEGL VLVIDQYGGS GGMLRGFLND GTKDYAHQTN IDALAFGHCQ VSYRNLGRPS
QIKLHHAGGH FKVEIDGHKC FESDKIALPQ GYTFGITAAT PENPDSFEIF KLTVMSETVD
PRHTQQTNNN NNNNNQNNQQ AAPGGFDNPE DAFKQSIPDK SADTFQTSAQ QFADLHNRLQ
STYHQLAAVY RSVTAHHAVD EQRHKEVQEM VQNIRADLKR LDKVDSLERT VEDLKRDVAS
LRDTLDRRIS SHETSFRGAL TDHHRQLSER MADSIPGHGK LIFILIGTQV VLAGVYIVYK
RRKMAGPKKY L
//
