ID A0A371DGC8_9APHY Unreviewed; 977 AA.
AC A0A371DGC8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=OH76DRAFT_1378889 {ECO:0000313|EMBL:RDX51572.1};
OS Lentinus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Lentinus.
OX NCBI_TaxID=2498619 {ECO:0000313|EMBL:RDX51572.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX51572.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX51572.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000256|ARBA:ARBA00004833}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; KZ857394; RDX51572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DGC8; -.
DR STRING; 139420.A0A371DGC8; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0017177; C:glucosidase II complex; IEA:TreeGrafter.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:TreeGrafter.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IEA:TreeGrafter.
DR CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; GH.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000256964};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..977
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016846059"
FT DOMAIN 85..331
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 375..710
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 718..810
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 828..872
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 977 AA; 109602 MW; ED5B1BF19650ED5C CRC64;
MRALSSLLIV AAIPAVLAVK THDFKTCSQA GFCRRGRALS ARAAENPSWK SPYSIDASSV
DLSPDQAAFT AAVRSSIYPE VKFGLDVRIH DDGVVRVRMD EVDGLRQRYN EAASWALLEE
PKVSQKIQWS VGKNGVRAAY GPKNGVEVDV SFEPLQVTLR RDGKEQVVLN GRGLLHMEHF
RTKESVEKSK EGVEVPEEGL DTDENAQVVL RALPRTAWFE GDSEDGWWEE SFNSFTDPKP
RGPESLSVDI DFPNHGHVYG IPQHATRLDL PLTTGEGAHY SDPYRLYNAD VFEYLADSTM
SLYGSIPVMY AHSADSTVGI FNAVGSETWI DVGRPSPKST SSHWISETGI LDIFILPGPT
PADIFGQYTR LTGTPALPAH WALGYHQCRW NYISSDDVRS VQKRFDEEDI PVDVFWLDIE
YSEDHKYFIW DKRHFPDPVD MIHDVEAIQR KMVVIVDPHL KRTDDYPVYT QARDRGLLVK
KGDGKTDYEG WCWSGSSAWV DFFHPGSWDW WKSLFKVQPQ GDQWSWVEST VDTGIWNDMN
EPSIFNGPEI SMPRENIHHG GWEHRDLHNI NGMLFSNLTS QAVMARTDPP KRPFVLTRSF
YAGSQRFGAM WTGDNLGTWE HMAVGVKMVL ANNIAGFSFA GSDVGGFFGN PEPEMLVRWY
GVGVFSPFLR AHAHIDTKRR EPYLLDEPYK SIVRDMLRLR YSMLPVWYTA FREASVTGLP
VVRPHFVVFP GDENGFSLDD QFFVGGSGLL VKPVTRKGAT EESVYLPAED QVYYDYFNHN
AYRSTSKGKN ITVPAELHQI PLFIRGGSII PTRERPRRSS PLMKHDPFTL RVALSNDGSA
RGELYLDDGE TFSHRDGEFV WREFVAEKPA KKSKGVRLSS RNLAAQKPAE AVDQVALATY
DSSNGFAKDV AEVRVEKVVV LGLAAKPSSI TAGGKELQWT FTPGVAASDK KEGTASVLII
KDPKLSITSD WEILVQA
//
