ID A0AAD9L789_PAPLA Unreviewed; 960 AA.
AC A0AAD9L789;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=DB88DRAFT_463214 {ECO:0000313|EMBL:KAK1925134.1};
OS Papiliotrema laurentii (Cryptococcus laurentii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Rhynchogastremaceae; Papiliotrema.
OX NCBI_TaxID=5418 {ECO:0000313|EMBL:KAK1925134.1, ECO:0000313|Proteomes:UP001182556};
RN [1] {ECO:0000313|EMBL:KAK1925134.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=5307AH {ECO:0000313|EMBL:KAK1925134.1};
RG DOE Joint Genome Institute;
RA Roman V.A., Bojanowski C., Crable B.R., Wagner D.N., Hung C.S.,
RA Nadeau L.J., Schratz L., Haridas S., Pangilinan J., Lipzen A., Na H.,
RA Yan M., Ng V., Grigoriev I.V., Spatafora J.W., Barlow D., Biffinger J.,
RA Kelley-Loughnane N., Varaljay V.A., Crookes-Goodson W.J.;
RT "Identification and recombinant expression of a fungal hydrolase from
RT Papiliotrema laurentii that hydrolyzes apple cutin and clears colloidal
RT polyester polyurethane.";
RL Submitted (FEB-2023) 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:KAK1925134.1}.
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DR EMBL; JAODAN010000004; KAK1925134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAD9L789; -.
DR Proteomes; UP001182556; 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 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 Reference proteome {ECO:0000313|Proteomes:UP001182556};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..960
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042138527"
FT DOMAIN 89..330
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 373..700
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 709..799
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 819..865
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 960 AA; 108165 MW; 85878A6A66FCEC11 CRC64;
MRLTSWALLA LPALLDGVAA VKQEDFKLCS QSSFCRRLRS IGQRQSAAPA HFTSPYSVGP
PATTAGTIDH ASWSWPVSSS LYPEISFELR VDILEKGDGI ARIRMDEVNS QTPFRRYNET
AKWALVDVNP PLASLADARL TSDAAKSTIT YAKGLSIEII HSPLKITQYR DGRPQVVFNE
RSLLHMEHFR QKQVEKVEEG ASESEQMVLQ AGEMDRSWFE EVDAEAFEER WKKWTDSKPK
GPEALSIDLS FPGVEHVFGL PEHASPLSLP DTVGPNAHYT DPYRLFNVDI FEYLADSPMS
LYGAIPLLHA HSAKSSVGVL NLVASDTWVD VLHDKQGTHT HWMSESGILD LLLLPGPKPQ
QLFEQFAILT GPTALPPQWS TAYHQCRWNY INEEDVLEVD RRFDETDIPL DVTWLDVEYS
VDRRYFDWNP SHFPDVKRML QKVADKGRKM VAIIDPHVKR SDSYRIYTDA KDLDILIKKP
DGSNFEGWCW PGNSVWVDFF NPKSWDWWKK MFDFKVWTDS APNLFIWNDM NEPSVFDGPE
ISVPRDTVHD GGWENRDVHN INGMLFHNAT AQALIARETP AKRPFVLSRA YYTGSQRFGA
IWTGDNMGDW EHFAGETAML LSNNIAGMSF CGADVGGFFG DPSHEILVRW YQAGAFMPFF
RAHAHIDTKR REPFLYDEPI RGYLRDAIRL RYQLLPVWYN AFHDASVSGA PIIKPQYAVF
PEDPAGFAID DQYYVGDSGI LVKPVVVEGA TKTDVYISDN QPYYDYFTHR LYPAKAKPHH
LSLDTPLSTF PVLIQGGSIF PVRQRVRRSS PLMWQDPFTL IIALSKQGTA SGQLYLDDGE
TFGHERGEFI WRSFDFSSTS KGGVLRSSDG ASDQTEASDA VTPYGENNLW AKTIAHVKVE
RVVVLGLKNK PHGVSVAGQG VEWSWEDGAA AGGKKEGGSS KLVIKNPGLG VVESWEVRIE
//
