ID R7SM56_DICSQ Unreviewed; 838 AA.
AC R7SM56;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=DICSQDRAFT_150074 {ECO:0000313|EMBL:EJF56973.1};
OS Dichomitus squalens (strain LYAD-421) (Western red white-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Dichomitus.
OX NCBI_TaxID=732165 {ECO:0000313|EMBL:EJF56973.1, ECO:0000313|Proteomes:UP000053319};
RN [1] {ECO:0000313|EMBL:EJF56973.1, ECO:0000313|Proteomes:UP000053319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LYAD-421 SS1 {ECO:0000313|EMBL:EJF56973.1,
RC ECO:0000313|Proteomes:UP000053319};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; JH719459; EJF56973.1; -; Genomic_DNA.
DR RefSeq; XP_007370246.1; XM_007370184.1.
DR AlphaFoldDB; R7SM56; -.
DR GeneID; 18836886; -.
DR KEGG; dsq:DICSQDRAFT_150074; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR OMA; IRGVRYY; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000053319; Unassembled WGS sequence.
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; 3.
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Reference proteome {ECO:0000313|Proteomes:UP000053319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..838
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004455644"
FT DOMAIN 89..261
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 317..587
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 594..687
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 705..755
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 838 AA; 94097 MW; 7196A3D940F97600 CRC64;
MRTVGFLFVL AATPATLAFK SQDFKTCSQA GFCRCGRALS VIIRAAQSPS WTSPYAVDAS
SAALSRDQTS FIAAIRSSIY PDVKFGLDVR IHDDGVVRVR MDEEPKVGQQ QWELGRDGVS
AVYSAEKEVE VKEQVVLNNR GLLHMEHFRT KESVAKGKGR FDTDGSAQVV LNNHPRIAWF
EGEEEDGWWE ETFRSFVDCK PRGPESLFID IDFPNHGHVY GIAQHATRLD LPTTTGENAY
YPDPYRLYNA DVFEYLNSTA AVFNAVGSDT FIDIGHPIPK SSTSHWISET GILDVFIIPG
PTPADIFAQY TRLTGTPALP AQWALGYHQC RWAYVSSDDV RTVQKRFDEA DMPVDVLWLD
IEYAEEHKYF IWDKRHFPDP VDMIKDVEAV GRHMVVIVDP HLKRTNDYPV YKQAAELGIL
IKNGDDTTDY EGWRWSGSSA WADFFNPRTW DWFPAVFNGP EISMPRDNIH YGGWEHRDLH
NINEMLFHNL TSQAAMARTD PPERPFVLSR SFYAGSQRFG ATWTGDKLGT YGPDVGGYFG
NPDSEMLVRW YGVGVFSPFS RAHAHVDATR REPFLLNEPY KSIYTAFREA SVTGLPVVRP
HFVVFPQDEE GFSLDDQFFV GGSGLSVKPV TRKGATEEIV YLPAEDQVYY DSFNDHAYRS
SSSKGKLITV PAELHQIPVF VRGGSIIPTR ERPRRSSPLM KHDPFTLRVA LGSDGSARGE
LYLDDGETYS HQQGQFVWRE FAVEKLAKKS RCVWISSRDF AAQKPAEAVD RVALAAYDSG
NDFAKSIANV RVEKYSRPTT TITAGVASAD KKEGTASVLV IRDPKVAVTS DWAILVQA
//