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Database: UniProt
Entry: R7SM56_DICSQ
LinkDB: R7SM56_DICSQ
Original site: R7SM56_DICSQ 
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
//
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