ID W6PXF9_PENRF Unreviewed; 341 AA.
AC W6PXF9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Concanavalin A-like lectin/glucanase {ECO:0000313|EMBL:CDM28471.1};
GN ORFNames=PROQFM164_S01g002282 {ECO:0000313|EMBL:CDM28471.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM28471.1};
RN [1] {ECO:0000313|EMBL:CDM28471.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM28471.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG792015; CDM28471.1; -; Genomic_DNA.
DR AlphaFoldDB; W6PXF9; -.
DR STRING; 1365484.W6PXF9; -.
DR OMA; PTENSTC; -.
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:InterPro.
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 4: Predicted;
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 Lectin {ECO:0000313|EMBL:CDM28471.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..341
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004879470"
FT DOMAIN 35..230
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT ACT_SITE 123
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT DISULFID 26..33
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-2"
SQ SEQUENCE 341 AA; 36530 MW; 32F7337F95E7D3B2 CRC64;
MGFPSYCKWA ALALAATAAA QTTTSCDPMN KTCPADTGLN KYRLNTDFTA GSLGRWNTTA
GTVTTTDLGA KFTINEQGDA PTIESEFYIF FGHVDVKMRT ANGTGIVSTW ILESDDLDEI
DWEQISTWDT EAETDYFGKG NTTSYDRGTT VTVSTPEETF HTYSVDWTAE RIEWLLDGVV
VRTLEYADAV DGTNYPQTPM RIRIGIWAGG DPDNSEGTIE WAGGETDYTE GPFSFYVESV
NIINYTPASA YRYTDKTGDY TSIKATNATI STNLGSSNSS SSVASSRTSS SAKASSSLIA
SSSASASAAA SSMSYVSAAP AYYSSIFAMA VGSFVAGLMQ F
//
