ID   A0A0D0CM12_9AGAR        Unreviewed;       984 AA.
AC   A0A0D0CM12;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Glycoside hydrolase family 31 protein {ECO:0000313|EMBL:KIK64069.1};
GN   ORFNames=GYMLUDRAFT_71514 {ECO:0000313|EMBL:KIK64069.1};
OS   Collybiopsis luxurians FD-317 M1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC   Collybiopsis luxurians.
OX   NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK64069.1, ECO:0000313|Proteomes:UP000053593};
RN   [1] {ECO:0000313|EMBL:KIK64069.1, ECO:0000313|Proteomes:UP000053593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK64069.1,
RC   ECO:0000313|Proteomes:UP000053593};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; KN834762; KIK64069.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0CM12; -.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   OrthoDB; 5480935at2759; -.
DR   Proteomes; UP000053593; 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; cd06602; GH31_MGAM_SI_GAA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR030459; Glyco_hydro_31_CS.
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:SF133; ALPHA-GLUCOSIDASE; 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.
DR   PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:KIK64069.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053593};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..984
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002225335"
FT   DOMAIN          337..758
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          766..857
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   984 AA;  107919 MW;  AC15B6AEB7162F2B CRC64;
     MFFIHGLCFG FVVARLFPGV LGIHRFHSQN PLMSSETSFI AESLSDGDLA SAVFSKNVSS
     CPGYSLHSLQ ESDIGLVAQL SLAGSACNAF GNDFENLTIE VTYETEARLR VRIADAENKQ
     FTIPDSVISR PSPPTTSFTK SSDLVFNYES NPFSFWITRR SNPDAAPLFD TRLSSLPETP
     IPPVIANDDS TALDGFPLVF EDQYLQLTSA LPLDANIYGM GEAVASSGFR RNVASNGGSI
     QTLWARDAAD PVDENMYGNH PIYLEHRFNE TTNEAQSHGV FLFSSSGADV LLLTPSGASQ
     SLIQYRMIGG ILDFYFFSGP SPHAVIEQYG ALVGLPTWIP HWAFGFHLCR WGYISINETM
     EQVQNMRAAD IPLEVMWNDI DLYHAFRDFT SDPVSFPGDE VRAFIQELAS NNQHYIPILD
     AAVPVLTNAS DVYDPYSRGH ELDVFVKNPD QTEYIGEVWP GYTVFADWFA DATQQWWTEA
     LKNWSDGGVE YSGIWLDMNE ISSFCQGSCG TGADLSNTSV PFLLPGEPGA LVTDYPECYD
     ASKFGPSGNI TINGALTCID PFTLPDTLAE RGLGAGGESG VNLNSPPYVI HNGAGDLSVN
     TLATNATHVG GIVELDVHNM WGMMEEKATH LALLELQPGK RPVIIARSTF PSSGKWTGHW
     LGDNFSKWEY LYYNIQGILQ FQIFNIPFVG ADTCGFNGNT DEELCARWME MSAFVPFMRN
     HNEKGALSQE PYRWENVANA SRTAISVRYS LLPYWMTLFA NASMQGTPPV RALWYEFPTE
     PELFGLDKQF LVGGDLLVTP VLSPNVSTVE GIFPGRGKVT WRDFYTHAVV DADANGTATL
     SAPLTHINVH IRGGAAILMH ANPAYTTTET RAGPFSLLVS LESDSHAFGT AYLDDGLSNP
     PAENRIATFT ANANQLQISS RGNFTVQQKL EQLTILGVSK EPGTVSVGGT NLKSSSWEFM
     SELQKLVISN VSIDLSDAET SVTW
//