ID A7TJL8_VANPO Unreviewed; 935 AA.
AC A7TJL8;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 28-JAN-2026, entry version 82.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=Kpol_534p42 {ECO:0000313|EMBL:EDO17561.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO17561.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480402; EDO17561.1; -; Genomic_DNA.
DR RefSeq; XP_001645419.1; XM_001645369.1.
DR AlphaFoldDB; A7TJL8; -.
DR FunCoup; A7TJL8; 992.
DR STRING; 436907.A7TJL8; -.
DR GeneID; 5545786; -.
DR KEGG; vpo:Kpol_534p42; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; A7TJL8; -.
DR OMA; TVHQPLW; -.
DR OrthoDB; 1334205at2759; -.
DR PhylomeDB; A7TJL8; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0017177; C:glucosidase II complex; IEA:EnsemblFungi.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0106407; F:Glc2Man9GlcNAc2 oligosaccharide glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0033919; F:glucan 1,3-alpha-glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006491; P:N-glycan processing; IEA:EnsemblFungi.
DR CDD; cd06603; GH31_GANC_GANAB_alpha; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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:UP000000267};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..935
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002715743"
FT DOMAIN 97..330
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 373..697
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 706..797
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 822..857
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 935 AA; 107870 MW; 1DAD22428F6F8730 CRC64;
MIFNNRFLII FLLPLYWATA FGFTEYLLKT CQQSGFCHRN KVYSQNILKT KNSYYSIDLS
SINYEVEKSK SELNLFTANI IKTIPRPDVG DIKVVLPISI SFLKDTNSVR LTIDEDRHPE
LDNSISEILN PYRYNETWKW AFDIDNKDIL QGDKLSFYEL KGSSNNVISL YNRDNSIKVE
VYTNSFKIKV FYNDTLVFTV NDRLFMNLEH KRLKELNFQN INPEETPYNM FGDDFEYSKD
DTLKFGPESV ALDFTFNNME NVYGIPEHAD SLKLKDTSNT EPYRLFNVDV FEYTIDSPMP
MYGAIPFMIG TNKDTSAGIF WVNAADTWVD IAYEGSDTKT HWISETGIID VVLFLGKSPS
DLTKNYIKLT GKPQLPLLSS IGYHQCRWNY NDEPDVLNVD SEMDKYQFPF DFIWLDLEYT
DDKKYFTWKP NSFPNPKRLL NKLARLGRQL VVLIDPHLKL NYFVSDSVVE DQGCVYNSEG
DPFIGHCWPG NSIWIDTLNP IGQKLWDGFF KKFIGSIKNL HIWNDMNEPS IFSGPETTAP
KDLIHYAGFE ERSIHNIYGL SVHETTYDSL KEIKDGSGLR PFVLTRAFFA GSQRTAATWT
GDNAANWDYL RISIPMCLTN NIVGMPFIGA DVAGFSGDPE PELLVRWYQA GIWYPFFRGH
AHIDTKRREP YLLDEPDRSI VREAIQLRYA LLPMLYTSFF NAHRTGTPIM KPMFYDKTMY
PELYAIDDQF YVGDSGLLVK PIVDKEATSV EMMFVPGIYY EYTNLSPLII NGIVPQSRNI
DAPLDIIPMF IEGGHILTRR NKYRRSSKLM RHDPYTLVIA PDVYGNAFGD LYIDDGETFE
FEKGEYLETN FSLNDGKVLK STVLNEPQFD NVLGNTDIYE IKIATAAIKK TVKKTVTIIS
GSNKHEVPLH RSEDGNWVSI RYPKIKVDET WEITF
//