ID A0A397SSA4_9GLOM Unreviewed; 936 AA.
AC A0A397SSA4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=C1645_696596 {ECO:0000313|EMBL:RIA86837.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA86837.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA86837.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA86837.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RIA86837.1}.
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DR EMBL; QKYT01000341; RIA86837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397SSA4; -.
DR STRING; 658196.A0A397SSA4; -.
DR OrthoDB; 3237269at2759; -.
DR Proteomes; UP000265703; 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 FunFam; 3.20.20.80:FF:000039; Glucosidase, alpha neutral C; 1.
DR FunFam; 2.60.40.1180:FF:000023; neutral alpha-glucosidase AB isoform X2; 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:UP000265703};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 73..314
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 370..697
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 705..792
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 811..851
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 936 AA; 107908 MW; D39584E4F6DF04BA CRC64;
MVVTILVVSA VKPQDFRTCA QTSFCRRNRA YADKATSGSF ISPYNVIKDT INIEDGIISG
ELINTENRVL FIFEIHILIN NSVRIRINEK NPLKPRYDRV KYWSLIQEPS NTLEYTENSI
NGKDMFTSLS FGIDRNHKVI IYHTPFHIEL LINDVPIITF NNRGFFNFEH LRKKDDPVNK
PELVIQPDIN AEEAEIQTEE EKEEKQEEGL WEETFNGKID SKPNGPESIG LDISFPGFGH
VYGIPEHTTT LSLKETRGGD GGYNDPYRLY NLDVFEYDLD SPTALYGSIP FMLAHRKGAS
AAILWLNAAE TWIDIVKSKD DKSFLGFGKA TPSTHTHWFS ESGIIDVFAF LGPTTSDIFE
QYGSLTGFTA LPQSFAIGYH QCRWNYLNQR DVAEVDAGFD ENDIPYDVIW LDIEHTDGKK
YFTWDKTKFS DPEKMQKDIG RKGRKMVTIV DPHVKRDDNY YIYKEAKDLD ILIKDKDGKA
FDGWCWPGSS VYPDWTNPKA QDWFVKKFAF DQYEGSTEYL FIWNDMNEPA VFSGPEITAP
KDLIHYEGWE HRNLHNLFGM AFHAATSQGL INRTNPNHRP FVLSRSFFVG SQRFGPIWTG
DNFAKWDHLA ASSPMLLTIG ISGIPFSGAD VGGFFGNPEP ELLVRWYQTG AFQPFFRGHA
HIDTKRREPW LFGEPYTSYI RDAIRQRYIL LPFWYTLFQE ASTNGMPIIR PMFVVFPDNE
ETFAMEDQYF VGNSLLVKPI TSQGQTSTEV YFAGKDIYYD YYTFKKVQGS GKVRVDVLMN
KIPVFLRGGS IIPRRQRFRR SSLAMYSDPF TLIVALNKKG EATGTLYLDD GKSYEYQKGH
YIYRKFNFTS GKFTSTSLNN DQVQNDENNY IRSNKFIKIE RIIILGIDKL PKKIIGYYND
LIDDKKELEF KISKDIVIIR NPKLLISNDW TIEFVN
//
