ID A0A0A2L9X6_PENIT Unreviewed; 372 AA.
AC A0A0A2L9X6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Concanavalin A-like lectin/glucanase, subgroup {ECO:0000313|EMBL:KGO75981.1};
GN ORFNames=PITC_011380 {ECO:0000313|EMBL:KGO75981.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO75981.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO75981.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO75981.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
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:KGO75981.1}.
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DR EMBL; JQGA01000367; KGO75981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2L9X6; -.
DR STRING; 40296.A0A0A2L9X6; -.
DR HOGENOM; CLU_027506_1_1_1; -.
DR OMA; TEHTWWF; -.
DR OrthoDB; 337487at2759; -.
DR PhylomeDB; A0A0A2L9X6; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR10963:SF72; GLYCOSIDASE-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lectin {ECO:0000313|EMBL:KGO75981.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..372
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001990031"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..244
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
SQ SEQUENCE 372 AA; 41508 MW; 3A92D1672AD9FE90 CRC64;
MRSWTSFFLL PLTTIVGVTN AITAYTGTDC NPLNKTTCSP DPALGTEHTW LFNSTLDTDL
WDMRTGTLDY TSEGADFSMK TENSSTLLVS NFYIFFGVME AHVKMAKGPG VISSVILQSD
DLDEIDWEWV GYNTSGVQSD FFGKGNTTTS DRGGNHAVAN ADTEFHNYTS YWDKDRLEWW
IDGDLVRTVH YSEPLTVYGK NYPQTPCQVK ISNWPVGVKG QTEGNLEWGG GLVDWSDVPF
TMTVSKLRVQ DFHSGKEYRY NGTSGTRESI EVVSGNSTAI THLNKEPVKT LSQKWHDLGQ
GAHVGVYCAV SVVVAVLLGA FIFYCLKQRR SGRLQQALDD GQYSAELTTL EQSKMRWRQS
ELRGKGSYQP VP
//
