ID W6QJU3_PENRF Unreviewed; 368 AA.
AC W6QJU3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN ORFNames=PROQFM164_S03g001218 {ECO:0000313|EMBL:CDM34494.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34494.1};
RN [1] {ECO:0000313|EMBL:CDM34494.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34494.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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}.
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DR EMBL; HG792017; CDM34494.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QJU3; -.
DR STRING; 1365484.W6QJU3; -.
DR OMA; WYIMFGR; -.
DR OrthoDB; 337487at2759; -.
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: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:SF27; GLYCOSIDASE CRH1-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 GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW Lectin {ECO:0000313|EMBL:CDM34494.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|PIRNR:PIRNR037299, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..368
FT /note="Glycosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004882099"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..228
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT DISULFID 25..32
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-2"
SQ SEQUENCE 368 AA; 39502 MW; 0D01B608752BB6F1 CRC64;
MRFFLGAALG LISSTLVVAQ TYTDCNPTKK TCPADPAFGQ SDKTFDFTSG ASDAFKSTGS
VTYDSTNGAT FTISKQGDGP LIQSGWYIMF GRVECTIKAA AGTGIVSSAV LQSDDLDEID
WEWLGGNNAQ VQTNYFGKGD TTSYSRGAYH DNAGNHDEFH TFSIDWTSTQ IVWAIDGKTV
RVLTPETADT NQYPQSPMMI KVGVWAGGDS NNAQGTIDWA GGETDYTQGP FKMYLKSMTV
TDYSTGTSYK YGDTSGSWES IVAEGGKVNG NKAAEPTSTE SAPLITATVD SVPVPWSGTH
KETTSWVTPN VWPWVASDSP SASSTGSQYD WESGSGQNKP PGGDSMIYLP LYVSSIAFLF
GCLFPLWR
//
