ID F8NS00_SERL9 Unreviewed; 968 AA.
AC F8NS00;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Glucosidase II subunit alpha {ECO:0000256|ARBA:ARBA00042895};
GN ORFNames=SERLADRAFT_447584 {ECO:0000313|EMBL:EGO26362.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO26362.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO26362.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) 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, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; GL945432; EGO26362.1; -; Genomic_DNA.
DR RefSeq; XP_007316535.1; XM_007316473.1.
DR AlphaFoldDB; F8NS00; -.
DR GeneID; 18816389; -.
DR KEGG; sla:SERLADRAFT_447584; -.
DR HOGENOM; CLU_000631_7_0_1; -.
DR OrthoDB; 5480935at2759; -.
DR Proteomes; UP000008064; 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; 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 Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EGO26362.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..968
FT /note="Glucosidase II subunit alpha"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003381602"
FT DOMAIN 88..325
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 369..704
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 712..803
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT DOMAIN 821..872
FT /note="DUF5110"
FT /evidence="ECO:0000259|Pfam:PF17137"
SQ SEQUENCE 968 AA; 108405 MW; 0D4A089048397714 CRC64;
MWSPSFVAAL LLLLTPAAHT LKTGDWKTCS QSGFCRRGRA LSARAQDAAD VWKSPYSVIP
SSVAVASNLA SFTAAVKSSI YPEINFELDV RVHKDGVVRV RMDEVGGLRK RYDEAASWAL
VQEPEISRAI QWSVGKQEIK AKYGEKKDVE VTVEYNPLKV TLSRNGKEEV VLNGRGLLHM
EHFRTKASGD DKPVEGSEGD AQAVMQTNPA AWFEGDTEDA WWEETFSSWT DSKPKGPESL
SIDINFPRHG HVYGIPQHAT SLSLPTTTGP SATFTDPYRL YNADVFEYLA SSSMSLYGSI
PLMHAHSAES TVAVFNAVGS ETWIDIGRSN DRSTETHWVS ESGILDVFIL PGPTPEEVFA
QYARLTGTPA LPAHWSLAYH QCRWNYVSSD DVRGVQKRFD EEDIPVDVFW LDIEYAEEHK
YFIWDKKTFP DPVEMTNDVD ALERKMVVII DPHLKRTSSY PVYQKASELA VLVKPKSGEG
EYEGWCWSGS SSWIDGFNPA SWEFWKGLFK TKSIDGQWSW TESTDAVHIW NDMNEPSVFN
GPEITMPKDN VHYGGWEHRD VHNINGMLFT NMTYQAVAAR SDPPKRPFVL TRSFYAGSQR
FGAMWTGDNL GTWEHMTVNL KMALANGIGG MTFGGSDVGG FFGNPEPEML VRWYAIGIFS
PFFRAHAHID TKRREPYLLD EPYKSILRDT IRLRYAMLPM WYTAFREATV TGIPILRPQY
VVFPKDEAGF AIDDQFYVGA SGLLVKPVTE KGATEASIYL AEDQVYYDYF AHYAHQGSVK
GKYVTVPAAL HQIPLLVRGG SIIPTRERHR RSSPLMKYDP FTLRVALDKV GSARGELYLD
DGETYSHQDG EIVWREFTAE TEKKSKVLRV SSKDLALEKP QEAVEGNALA HFDPANAYAK
KIAHVRVEKI VLVGLGKQPK AVRVEGGKEL DWDYAPGVSS GKEGQAGVLV VKDPAVTVVS
DWTLVVEL
//
