ID A0A0A2JGN7_PENEN Unreviewed; 426 AA.
AC A0A0A2JGN7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Concanavalin A-like lectin/glucanase, subgroup {ECO:0000313|EMBL:KGO54529.1};
GN ORFNames=PEX2_070620 {ECO:0000313|EMBL:KGO54529.1};
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:KGO54529.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54529.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54529.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:KGO54529.1}.
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DR EMBL; JQFZ01000221; KGO54529.1; -; Genomic_DNA.
DR RefSeq; XP_016596900.1; XM_016744333.1.
DR AlphaFoldDB; A0A0A2JGN7; -.
DR STRING; 27334.A0A0A2JGN7; -.
DR GeneID; 27679753; -.
DR HOGENOM; CLU_016508_0_0_1; -.
DR OrthoDB; 1891044at2759; -.
DR PhylomeDB; A0A0A2JGN7; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
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 Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Lectin {ECO:0000313|EMBL:KGO54529.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143}.
FT DOMAIN 250..412
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT SITE 66
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 426 AA; 48093 MW; E06CB1A0DE5681A5 CRC64;
MVGTGGLYAP TIRHHNGITY IICTNVIHGP SNVLGDERNE QFIIHTTDIR SGTWSDPIVF
GFPGIDPSLL FDDDGRVYVQ LCKTGPEFHI YNGEIDITTG AMIVKPTLIW KGWKKGYTEG
PHIYKKDGWY YLLCAEGGTF RYHMLSMARS RNIWGPYESY DMNPLYTASG TTQYVQNTGH
GDLFQDQSGQ WWVVMLGIRI KEGRSIMGRE TFLTTVDWPS DGWPAIESIT SDGKLGASFN
EGQDSLAAAP WVYLRDAKLD RYRIQNRCIT LQADPVEFTS PDESITFVGQ RQRRLQGNTT
VTVYKPQQST SVRAGLALYK DEHRFLTIGY DFQLQQVIFN GLNQAKSFSQ SETQSVEFQG
SMSFRIGYTE TSLQFFFRQG KANWRNLATV DTAILTDYDF TGPVIGIFAI GDDVAVEFRD
FAVDTV
//
