ID   A0A068RW12_9FUNG        Unreviewed;       525 AA.
AC   A0A068RW12;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glycosyl family 43 {ECO:0000313|EMBL:CDH54199.1};
GN   ORFNames=LCOR_05466.1 {ECO:0000313|EMBL:CDH54199.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH54199.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH54199.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:CDH54199.1}.
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DR   EMBL; CBTN010000021; CDH54199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RW12; -.
DR   STRING; 1263082.A0A068RW12; -.
DR   VEuPathDB; FungiDB:LCOR_05466.1; -.
DR   OrthoDB; 1891044at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
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; cd18617; GH43_XynB-like; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR041542; GH43_C2.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR   PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR   Pfam; PF17851; GH43_C2; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT   DOMAIN          352..523
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            150
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   525 AA;  59466 MW;  848F798430EC2110 CRC64;
     MTYNNPIIPG FNPDPSICRV ENDYYLVTST FQYFPGVPIY HSQDLVNWEH IGKPQTIEQT
     SQYVGLIYAQ SGNVLDRPEL VPGLDKTLIN GGIWAPTLRY HDGVFYMVTT MVFVDKAYNN
     FQRWKNFFVT ATNPKGPWSD PIFFDYPGYD TSLYIFDKDH AYVQGSFYHR IRKEISQSKI
     DLKTGQVTEP RRIWSGTGEK APEAPHVLYK DGWYYLVIAE GCGTEAGHRV AMARAKSIDA
     PEDEWEACPV NPILTHHDLP DELVQCTGHA DFFQDTMGNW WIVFLASRVY DGERFPIGRE
     TFLAPVDWSG EWPVVQRPIK AFAPKEYHGP NIAAALNTSK GLCKFGTRAH GWGIEWLWLR
     IPDMQKYQLT DLTDIDDVYH GCKISGSTSN LASEMQSSSL VGIRQCHIRC CVTVDLELDT
     NADYAALVAY LDPLHHASVG VADNQILFSG GRIPLPKEPW IKLAIKADER NYNFMYSFGG
     LQDWHNIGTV DTKELSTGFT GVIFGIHVQG VGKTAHFKNF TYEIL
//