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Database: UniProt
Entry: A0A0A2VR60_BEABA
LinkDB: A0A0A2VR60_BEABA
Original site: A0A0A2VR60_BEABA 
ID   A0A0A2VR60_BEABA        Unreviewed;       961 AA.
AC   A0A0A2VR60;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   28-JAN-2026, entry version 42.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE   AltName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN   ORFNames=BBAD15_g5812 {ECO:0000313|EMBL:KGQ08842.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ08842.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ08842.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ08842.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001657};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ08842.1}.
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DR   EMBL; ANFO01000533; KGQ08842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2VR60; -.
DR   STRING; 1245745.A0A0A2VR60; -.
DR   eggNOG; KOG1066; Eukaryota.
DR   HOGENOM; CLU_000631_7_0_1; -.
DR   OrthoDB; 3237269at2759; -.
DR   Proteomes; UP000030106; 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:0004558; F:alpha-1,4-glucosidase activity; IEA:UniProtKB-EC.
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; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..961
FT                   /note="alpha-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002007154"
FT   DOMAIN          94..329
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          386..714
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          722..811
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          833..872
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
FT   REGION          209..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..225
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  109280 MW;  25806F179FEB158F CRC64;
     MALRSQWIAL LIALGILMCL VMPGASVKEH DFKKCDQSGF CKRNRAYADK ATTEGSRWQS
     PYTVQPSSVS FKDGQLHAVI HKTINANGDT VNLPITVSFL KSGNARVTVD EERRQKQDIE
     LRHDSKVRKE RYNEAEKWVL VGGLALDKDA KVSHQDDAQT NVQYGKEGNL EAAIKYSPLA
     IDFRRDGVSH VRFNDRGLLN VEHWRPKIER EEGQEEKDSE DESTWWDETF GGNTDSKPRG
     PESIALDISF LGYEHVFGIP EHTGSLSLKQ TRGGSGNHNE PYRMYNSDVF EYILDSPMTL
     YGSIPFMQAH KKDSTVGVFW LNAAETWVDI VKSKAATNPL TLGKTGKTNT ETHWISESGL
     IDVFVFLGPT PQDVTRTYGE LTGYSAMPQE FAIGYHQCRW NYISDDDVKD VDRKMDKYKI
     PYDVIWLDIE YLDDRKYFTW DPHSFADPTG MGKQLDDHSR QLVIIIDPHI KKLEGYSIYD
     ELSSQDLAVY DKEGKPYEGW CWPGSSNWVD CFNPKAIEWW KTLYKYDKFA GTAENTFIWN
     DMNEPSVFNG PETTMPKDNI HFGQWEHRDI HNINGLTFHN ATFEALKTRK KGELRRPFVL
     TRSFYSGSQR LGAMWTGDNQ ATWEHLAASI PMVLNQGISG FPFAGADVGG FFGNPSKDLM
     ARWYQAGAFY PFYRGHAHID SRRREPYLLG EPYTGILTQA LRLRYALLPS WYTAFFQANR
     DGSPIVRPMY WTHPSEEAGF AIDDQLFVGS TGILVKPIVE ENKFSTDIWI PDEEVYYDYT
     TYDVVNTQKA KRVTIAAAID QIPMLMRGGH VFARRDIPRR SALAMKYDDY TLVVSVSRDG
     TATGELYADD GDTFEHEKGQ YIYRKFSFDK DGVRSVDAEG RSAKSVKAGA WLKEQSRVHI
     DKIVIVGATD AWNRKEVEIE SDGKTWTVPV DYHEAAKGRA AYAVVGRVGA KISSDWSIKL
     A
//
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