ID M2Q417_CERS8 Unreviewed; 976 AA.
AC M2Q417;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=CERSUDRAFT_119754 {ECO:0000313|EMBL:EMD31533.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD31533.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD31533.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD31533.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(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; KB445818; EMD31533.1; -; Genomic_DNA.
DR AlphaFoldDB; M2Q417; -.
DR STRING; 914234.M2Q417; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000016930; 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; 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; 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 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.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EMD31533.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..976
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004023584"
FT DOMAIN 86..333
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 378..711
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 719..810
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 828..880
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 976 AA; 110218 MW; 10E1BA8E107B8D5D CRC64;
MRGLKVILLT LVALPAVFAV KSHDFKTCSQ AAFCRRGRAL ATRARESSSW TSPYSVDPAS
VTIDPTKATF TAGVRSSIYP EIKFGLDVRV HEDGVVRVRM DEVDGLRKRY DEASSWALIA
DPEISREIQW TVAKDAVRAV YGHNNNIEVV VAYEPLKVSL LRNGQEQIVL NGDGLLHMEH
FRTKEAVDQE KSGWALPEAP EEGLDLEDAQ VVMQMNPRSW FEGVGDDGWW EETFGTWTDS
KPKGPESLSI DINFPNHGHV YGIPQHATRL SLPTTAGEDA YYSDPYRLYN ADVFEYLADS
TMSLYGSIPV MHAHSAESTV AIFNAVGSET WIDVAHFVPK STHTHWISES GIMDIFLMPG
PTPADVFAQY ARLTGTSALP AQWALGYHQC RWNYISSDDV RDVQTRFDEE DIPVDVFWLD
IEYAEDHKYF IWDKKSFPDP VDMLHDVEAI QRKMVVIVDP HLKRTDNYPI YQQAKDLDLL
IKKKDGQEYE GWCWPGSSAW VDFFNPASWD WWKSLFKTMP EGDKWAWIDS TENTYIWNDM
NEPSIFNGPE ISMPRDNIHY GGWEHRDVHN INGMLFHNMT AQAVMHRTDP PKRPFVLTRS
FYAGSQRLGA MWTGDNLGTW EHMAVGVSMV LSLNVGGFSF SGSDVGGFFG NPEPDMLVRW
YGVGAFSPFF RAHAHIDTKR REPYLLEEPY KSIVRDILRL RYSLLPVWYT AFREASVNGL
PVVRPHYVVF PQDEGGFDLD DQYFVGGSGL LVKPITRKDV TETTMYLPEN EVYYDYFTGH
AYRGAATGKN VTVPAELHQI PLLIRGGSIV PTRERPRRAS PLMKHDPFTL RVALSTTGTA
RGELYLDEGE TFAHQAGQFV WRAFEATAEK GGKEIRIRSR DLAARNLDTA VDGVALTTYD
ARNAFAKDVA RVRVERIVVL GLSREPRSVV ADGKEVHWEY KAGAAAASKG EGTASMLLVK
DPHASITTDW EITIHL
//
