ID G9MH42_HYPVG Unreviewed; 964 AA.
AC G9MH42;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 28-JAN-2026, entry version 58.
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=TRIVIDRAFT_86135 {ECO:0000313|EMBL:EHK26032.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK26032.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK26032.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK26032.1}.
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DR EMBL; ABDF02000002; EHK26032.1; -; Genomic_DNA.
DR RefSeq; XP_013960248.1; XM_014104773.1.
DR AlphaFoldDB; G9MH42; -.
DR FunCoup; G9MH42; 951.
DR STRING; 413071.G9MH42; -.
DR GeneID; 25798653; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_86135; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; G9MH42; -.
DR OMA; TVHQPLW; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000007115; 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; 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; 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:UP000007115};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..964
FT /note="alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003523408"
FT DOMAIN 98..332
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 388..716
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 725..815
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 837..873
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 964 AA; 109857 MW; 718507E97AEDDDE0 CRC64;
MRSTMGLSWK WTALFSLLSA FLCLIEPTLA VKEHDFKKCA QAGFCKRNRD YADQAAAQSS
TWISPYQVVL ESPSLKDGQI QAVILKTINA AGETVRLPVT ISFLQSGVAR VVVDEERRQN
KDIEVRHGSA ARKERYNEAA KWSIVGGLEP DLKAEIVHQD DSQINVKYGP EANFEAVIKL
SPFGIDFRRD GASQIKFNER GLLNFEHWRA KIERPEGEEN TEEDESTWWD ESFGGSTDTK
PLGPESVALD ISFHGYEHVY GIPEHTGPLS LKQTRGGEGN YAEPYRLYNA DVFEYILDSP
MTLYGSIPFM QAHRKDSSVG LLWLNAADTW VDIIKTKGSS NPLSLNAEAP SSTQTHWISE
AGILDIFVFL GPTPQDITKK YGELTGTTAM PQEFALGYHQ CRWNYISQDD VKDVDRRFDK
AQIPYDVIWL DIEYADGVRY FTFDPHSFSD PISIGKQLDS HGRKLVVIID PHIKRVDNYP
INEQLQSLDL AVHDKDGNIY EGDCWPGLSN WIDCFNPKAR EWWKTLHKYE NFNGTMENTF
IWNDMNEPSV FHGPETTMPK DNLHYDNWEH RDVHNLNGMT YHHSTFEALK SRKKGEYRRP
FVLTRAFFSG SQRFGAMWTG DNLADWGHLQ TSITMLINQG ISGFPFSGAD VAGFFGDPES
ELITRWYQTA AFYPFFRAHA HIDTRRREPY LLGDPYSAIA TAALRLRYSL LPSWYTTFFY
ANRDGSPILR PMFWTHPSSE GGLAIDDQFF LGSTGLLVKP IAEKDKYSTD IWIPDDETYY
EYTTYNLVKT QQGKHVTFDA PIDRIPILMR GGHIISRRDI PRRSSTLMRF DPYTLVISVS
KSGEAEGELY VDDGDSYEYQ DGQYIYRKFS LKDDVISSAD AEGRDTRKIK PGKWLKAMRD
VHVDKIIIVG APASWNREEV QVESEGRTWS AKVNYQAANG DRAAFATVSH IRARVGENWS
IKLA
//
