ID A0A0A2KVN6_PENIT Unreviewed; 443 AA.
AC A0A0A2KVN6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN ORFNames=PITC_026120 {ECO:0000313|EMBL:KGO71892.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO71892.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO71892.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO71892.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|PIRNR:PIRNR037299}.
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:KGO71892.1}.
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DR EMBL; JQGA01000915; KGO71892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KVN6; -.
DR STRING; 40296.A0A0A2KVN6; -.
DR HOGENOM; CLU_040459_0_0_1; -.
DR OMA; WNATANQ; -.
DR OrthoDB; 337487at2759; -.
DR PhylomeDB; A0A0A2KVN6; -.
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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; 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 InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037299, ECO:0000313|EMBL:KGO71892.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..443
FT /note="Glycosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001990625"
FT DOMAIN 75..276
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 344..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ SEQUENCE 443 AA; 46664 MW; 5EDDC6048A598445 CRC64;
MVRFVTPLVL ASLSVSAFAA QSCSSSEQCK DKEYPCCSQY GECGTGAFCL GGCDPLSSFS
LDSCAPMPVC ESKTYTWDNL DNAITQDKYL GNASAADWTY SGKVKTEDGN LIMTMPANSV
GTLFANNHYI WYGKISGKIK SSRGKGVVTA FILLSDVKDE IDYEWVGADL TAVQTNYYWQ
GVLDWHNSGN ISVEGADTFN DWHTYEIDWT PEKVDWIVDG TVHRTLNKAD TYNATSKQFQ
FPQTPSRLQM SLWPAGQASN AQGTINWAGG DIDWDSEDIK TVGYDFATVG EVSVQCYNPP
SDATVKGSKA YLYTNSAALE NDIAITNNNT VLASLGATGL DMDLGKASSS SSSNASSSNS
IPTNNGGSGG MASNTTSSHG SSSGSSGSSG SSGTSTTGAS ETSTAGFTQG TTAQGNGAAG
QNERVLRGSL FGVLVALVVL VTL
//
