ID A0A165SSW5_9APHY Unreviewed; 964 AA.
AC A0A165SSW5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=DAEQUDRAFT_723159 {ECO:0000313|EMBL:KZT72443.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fomitopsis.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72443.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT72443.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT72443.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429041; KZT72443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165SSW5; -.
DR STRING; 1314783.A0A165SSW5; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000076727; 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; 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.
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:UP000076727};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..964
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007866655"
FT DOMAIN 85..323
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 367..701
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 709..800
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 818..865
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 964 AA; 108301 MW; 6A28D89D9A217A7D CRC64;
MRALSSFLLL TIVPAAFAVK SQDFKTCAQA AFCRRGRALS ARAQESQAWK SPYSVDPSSV
AVSPEQASFV AAVKSSLYPN IKFSLDVRVH DDGVVRVRMD EVDGLRKRYD EAASWALTAE
PTISPDVKWA VSKKDVRATY GAKNDIEVVV SYDPLTVILY RGGKAQVVLN GRGLLHMEHF
RTKATGEEKA PVDAPADDSQ VVMQVNNRAW FEGEEEDGFW EEKFGSWTDS KPKGPESLSI
DINFPNHGHV YGIPQHATRL DLPTTTGENA HFSDPYRLYN ADVFEYLADS PMSLYGSIPF
MHAHSAESTV AIFNAVGSET WIDVGHPSAT STETHWISES GILDVFIMPG PTPADVFAQY
TRLTGTPALP AHWALAYHQC RWNYISSDDV RDVQRRFDAE DMPVDVFWLD IEYAEEHKYF
IWDKKTFPDP VDMMHDVEAI GRKMVVIIDP HLKRTDDYPV YKEAKELGVL VKSPGGENNY
EGWCWSGSSA WIDFFNPSSW DWWKSLFITE QGDKWSWTES TVDTYIWNDM NEPSIFNGPE
ISMPRDNVHH GGWEHRDIHN INGVLLHNLT SQALMSRTDP PRRPFVLTRS FYAGSQRFGA
MWTGDNLGTW EHMAVGVKMV LVNNIGGFSF AGSDVGGFFG NPEPEMLVRW YGVGIFSPFF
RAHAHIDTKR REPYLLDEPY KSILRSLLRL RYSLLPVWYT AFRETSVTGL PVLRPHWVVF
PKDEGGFSLD DQYFLGSSGL LVKPITDKGV TETSIYLPED QVYYDYYSYE AYRGASKGKN
VTVPAALDRV PFLVRGGSIV PTRERPRRSS MLMKRDPFTL RVALDTSGAA AGELYLDDGE
TFSHRDGKFI WRKFVASKQH KDLRIKSVDL AAQRPGEAVD GVALSNYNGA NDFAKDIATV
RVERVVVFGL STKPKSVQVG GKELYWEYTP GVASDTKKQG TASVLVIKDP GVGVSSDWEI
AVQV
//
