ID I4YFM1_WALMC Unreviewed; 949 AA.
AC I4YFM1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=WALSEDRAFT_59929 {ECO:0000313|EMBL:EIM22763.1};
OS Wallemia mellicola (strain ATCC MYA-4683 / CBS 633.66) (Wallemia sebi (CBS
OS 633.66)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=671144 {ECO:0000313|EMBL:EIM22763.1, ECO:0000313|Proteomes:UP000005242};
RN [1] {ECO:0000313|EMBL:EIM22763.1, ECO:0000313|Proteomes:UP000005242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4683 / CBS 633.66 {ECO:0000313|Proteomes:UP000005242};
RX PubMed=22326418; DOI=10.1016/j.fgb.2012.01.007;
RA Padamsee M., Kumar T.K.A., Riley R., Binder M., Boyd A., Calvo A.M.,
RA Furukawa K., Hesse C., Hohmann S., James T.Y., LaButti K., Lapidus A.,
RA Lindquist E., Lucas S., Miller K., Shantappa S., Grigoriev I.V.,
RA Hibbett D.S., McLaughlin D.J., Spatafora J.W., Aime M.C.;
RT "The genome of the xerotolerant mold Wallemia sebi reveals adaptations to
RT osmotic stress and suggests cryptic sexual reproduction.";
RL Fungal Genet. Biol. 49:217-226(2012).
CC -!- PATHWAY: Glycan metabolism; N-glycan metabolism.
CC {ECO:0000256|ARBA:ARBA00004833}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; JH668227; EIM22763.1; -; Genomic_DNA.
DR RefSeq; XP_006957420.1; XM_006957358.1.
DR AlphaFoldDB; I4YFM1; -.
DR STRING; 671144.I4YFM1; -.
DR GeneID; 18473632; -.
DR KEGG; wse:WALSEDRAFT_59929; -.
DR eggNOG; KOG1066; Eukaryota.
DR HOGENOM; CLU_000631_7_0_1; -.
DR InParanoid; I4YFM1; -.
DR OMA; SNEIWYD; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000005242; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 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 InterPro; IPR017853; Glycoside_hydrolase_SF.
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 Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EIM22763.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005242};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..949
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003697930"
FT DOMAIN 87..332
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 377..704
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 713..805
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 822..874
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
FT REGION 254..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 107732 MW; C72C12882BB007D2 CRC64;
MRVTFLGILI ALFLGIAECV KQNDFKKCQQ SSFCRRLRSL SDRKTNSSVW ESPYAITRGL
EQLGDEAASY TWKLNNRLAP EGIAFDLAVD VLKDGLIRLR VDESGGLYQR YNQTASYILV
DQPELMQASS VKITSYDDVD NLAFQTSTNQ PMELKVYHNP LNVQLKNAQS GEILVDINGE
SLLHMEHFRH KDAEDTDNNS AFTWHSEQPF EDPNTDGLWE ESFNNKPDSK PKGPEAFTID
INFPSHSHVY GIPEHASPLA LPPTDGSSPR RVPYVDDPKP YTEPYRLYNL DVFEYEANSP
MALYGSVPLM HAHSPRSSLA VFLLSAAEMW IDVKHPTKES TSTQWISESG IIDLFLIPGP
TIEDVFSQYA SLTGVSQMPQ EFSLGHHQCR WNYFTSKDML GVVSGYDSID APVDVIWLDI
EYSDGHKYFM WDKKKFPDPV DMINKIASKG RKTVNIVDPH LSRDDEFYVF NEASDKEVLV
KKPDGQSEYE GWCWAGSSSW VDMFNPASWD WWISLFKFDK WKDSTPDLFT WVDMNEPAVF
NGPEITMPKD TVFYGGVEHR DLHNINGILF ANLTSQALEQ RQEKNSRSFV LSRSFFAGSQ
RFGAVWTGDN LGTWDHLRSA TPMNLANNIG GIVFTGADVG GFFGNPQPEY LVRWYQTGAF
HPFFRAHAHI DTKRREPYVL DEPYQSIVRE VLRLRYSLLP VWYTSFRENT QTGLPILRPQ
FVVHPSDAGG FDIDDQFYIS DSGLLVKPVV HEGAQSVDVY FAGEEPYYDY FTHEISLGSK
HKGRRKSFFA DLESLPLFIR GGSIIPSRQR ARRSASVMSK DPLTLTIALD KNGNANGRLY
LDDGHTFDYQ DGAFIDRQFT FKSDRRGWTL TSSEIVPGDS YEDGNEVFIE RIEVLGLKAP
PKEIKVDGRP LEFSWEDGTA ASSNKEDTAS LLNIKKPLTK IAHDFKIIA
//
