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Database: UniProt
Entry: K9GCH2_PEND2
LinkDB: K9GCH2_PEND2
Original site: K9GCH2_PEND2 
ID   K9GCH2_PEND2            Unreviewed;       461 AA.
AC   K9GCH2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   ORFNames=PDIG_06820 {ECO:0000313|EMBL:EKV18809.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV18809.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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:EKV18809.1}.
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DR   EMBL; AKCT01000031; EKV18809.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9GCH2; -.
DR   STRING; 1170229.K9GCH2; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_027506_3_2_1; -.
DR   InParanoid; K9GCH2; -.
DR   OMA; QTPMNIH; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000009882; 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:SF72; GLYCOSIDASE-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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037299-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   Glycosidase {ECO:0000313|EMBL:EKV18809.1};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..461
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003929372"
FT   DOMAIN          23..232
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          282..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   DISULFID        27..34
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-2"
SQ   SEQUENCE   461 AA;  47088 MW;  9BCB648D05ED7472 CRC64;
     MPSVMKFAAA ALAVAAPLVS AQTYSECNPM ERSCPPNKGL TESNLHFDFT QASSLDQWKI
     SGGSVPTGPN GAEFTINKEG DAPTLVSDFY FFYGELSIEM KTSPGQGIVS SAFLQSDDKD
     EVDWEALGGK ANTIETNYFG KGDTTTYDRE TYVPVTSPDE SFHTYTVQWS KDTVNWLIDG
     ANVRTLNYND AQGGARFPQT PMNIHVGIWA GGAPTNGQGT IDWAGGLTDY SKGPYSMYIK
     SISVKNTNPA ESYTWSDMSG SAESIQFTGS NVVSSRGTSS VAATSSTSEA PISSSTKAPS
     ATENTPTTES TSTESTFIES TSTESTSTES TSTESTSAPA TTLATKTSSS SSAQYTAEST
     AVSGSGAASA ASVASSGVSP SGSSSSGFRS SPSPSSGSSS ESGSSGSVSN TETGSTAPSG
     SGSLTSASAS ASPSFNAAAS VAASYLGPVS LLGLVTALLQ L
//
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