ID A0A1Y2G0B3_9BASI Unreviewed; 1489 AA.
AC A0A1Y2G0B3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glucosidase 2 subunit beta {ECO:0000256|ARBA:ARBA00022387};
DE AltName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=BCR35DRAFT_300413 {ECO:0000313|EMBL:ORY89292.1};
OS Leucosporidium creatinivorum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY89292.1, ECO:0000313|Proteomes:UP000193467};
RN [1] {ECO:0000313|EMBL:ORY89292.1, ECO:0000313|Proteomes:UP000193467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=62-1032 {ECO:0000313|EMBL:ORY89292.1,
RC ECO:0000313|Proteomes:UP000193467};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY89292.1}.
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DR EMBL; MCGR01000006; ORY89292.1; -; Genomic_DNA.
DR STRING; 106004.A0A1Y2G0B3; -.
DR InParanoid; A0A1Y2G0B3; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000193467; 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 Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
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 InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR InterPro; IPR028146; PRKCSH_N.
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 Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS51914; MRH; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:ORY89292.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193467};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1489
FT /note="Glucosidase 2 subunit beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012078964"
FT DOMAIN 1367..1472
FT /note="MRH"
FT /evidence="ECO:0000259|PROSITE:PS51914"
FT REGION 1217..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1104..1175
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1489 AA; 166694 MW; 9E50EA13EA819F07 CRC64;
MVLRSPRRYW AIPPLLLVLL LVFSSPTSAV KRHDFKTCSQ SGFCRRNRAL ADRAVEHKSF
NSPYSLEQPS FVANSFHAAI SNALFPSIHF SLEVRFQKDG VARILMDEVD GLRQRYNEAG
MWAVQTEPLL ADESDFEVDI GAERTSIKYA NGRHELQVQH QPLLLTFYRD GQPHIVINER
SLLNMEHFRV KAIGGEPEEV VVQDAEHPEE QKVIVREEAF PGFLPKDEDG MWEETFGGKT
DPKPKGPESL SLDITFPGYE HVYGIPQHAS SLSLKQTRGG DGAYTDPYRL YNLDVFEYDA
DSEMAIYGAI PFMKAHRAGS TVGVFLVSGS EAWIDITKQP TSKEVTSSFK KFKKSSTKGA
DAGPSASTTS THWMAESGIL DLFVFLGPSS ADIFQQYTAL TGRAPLPQLF ATAYHQCRWN
YLNQADVQDV QTRFDEADIP MDVMWLDIEY AEEHKYFIWD RRNFPEPEKM QDDLAARGRK
LVAIVDPHIK RDKNLYIYTE AQELDILSKT ADGKEFEGWC WTGSSAWTDW FHPASWQWWI
DQFKFSKFKG STKNLFVWND MNEPSIFNGP EITMQKDTIH YGGWEHRDVH NIGGMIYQNV
TAQGLIEREE IPKRPFVLTR AFYAGSQRFG AMWTGDNLGT WPHLASTVPM LLTNGIAGMV
FAGSDVGGFF GNPEAEMMVR WYQVGAFSPF FRAHGHIDTK RREPYLFDQP YQGYIRDSIR
LRYTLLPTLY TAFYEASLDG TPILRPQYVV FPDDPNGFAI DDQFYFGSSG LLVKPVVKEG
ATDAEVYISD QQPYYHYTTD DVYFGVANGG THVKVPAPLD STPILQRGGS ILPRRDLVRR
SSTLAWRDPI TLVVAADLTG KSASGSLYLD DGESYAYEKG EFVSRKFDLK VGNSKTLVLN
SRSAYVSKES ALANYDPSGN EWAKKIADVV VREIVILGLE TKPSCIKLAG SSVGLDFEWI
EGVAATASRR KSGKGASKLV IKDAGASIIH DWDITLEFGA NSCSTTPAID YDAALQSPEC
PAGRFLCRNE GHIPSCILRS RFNDGICDPE CCDGSDETDG KVRCANRCQR VGFEHKKKVA
EEARKTRVGA AVRKEYETFG AKEKAKLEAE VEKVKGDLRR LEQKEHAAKA SLEALENAEA
GEIERKKESV LYQKIVEMQE AIKALREHRT NLEGHISDLS GILSDLSRDF NPNYQDMAVL
GASRAYKDWQ VANGLLSADE SSESDSESAP APPAVPIADE IKDYSDRELK AMEEEDPLSL
IDSLNSRVGT PVLSTVTSLF RIDDYVPDVW RPKYDSYKKS FVDLLVRTGI VYAPSTTQSD
RPELARARTS HSSILDEIKG AEGKLSSAEE SLNTDWGRDW EWKKLDGTCV EQNLGEYTYS
LCFFGEAVQK SNNNNQRSSL GKFQGWAEGE EKGSDAYYSK QLYADGQRCW NGPARSAKVD
LICGTTNALI NVAEPEKCTY LFQVSTPAVC IVKDELPTGE AASAPKDEL
//