ID A0A0A2J1V0_PENEN Unreviewed; 246 AA.
AC A0A0A2J1V0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=GH16 domain-containing protein {ECO:0000259|PROSITE:PS51762};
GN ORFNames=PEX2_052240 {ECO:0000313|EMBL:KGO49337.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO49337.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO49337.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO49337.1,
RC ECO:0000313|Proteomes:UP000030143};
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:KGO49337.1}.
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DR EMBL; JQFZ01000382; KGO49337.1; -; Genomic_DNA.
DR RefSeq; XP_016592767.1; XM_016742498.1.
DR AlphaFoldDB; A0A0A2J1V0; -.
DR STRING; 27334.A0A0A2J1V0; -.
DR GeneID; 27677917; -.
DR HOGENOM; CLU_077989_1_0_1; -.
DR OrthoDB; 1326761at2759; -.
DR Proteomes; UP000030143; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..246
FT /note="GH16 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002000625"
FT DOMAIN 14..244
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
SQ SEQUENCE 246 AA; 26901 MW; C6A23FBC65309030 CRC64;
MHVRGLSFVL LSTSVYCLSP NPSLERRATT EIPSDSFNSL DTYWNYLYPW GDTHNGGSRM
DADHVSVSDG ILTLTAEPVS GEPSPIHYLS GAIHAKSTFA VEEGGGLDLN AEFIAPISKG
TWPAFWLNAA SGWPPEIDIA EWKGSGKVSF NTFNTSSEVT TLDLDYPDPT DWHSVKAELR
DENGSDVSVK LYLDGELVMT QYAREYVGQG LRLIINYQTE GSSGSPGPSR TTTFQVRNVE
VISQNA
//
