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Database: UniProt
Entry: A0A178DTF8_9PLEO
LinkDB: A0A178DTF8_9PLEO
Original site: A0A178DTF8_9PLEO 
ID   A0A178DTF8_9PLEO        Unreviewed;       538 AA.
AC   A0A178DTF8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
DE   Flags: Fragment;
GN   ORFNames=IQ07DRAFT_515839 {ECO:0000313|EMBL:OAL47097.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47097.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL47097.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47097.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; KV441652; OAL47097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DTF8; -.
DR   STRING; 765867.A0A178DTF8; -.
DR   InParanoid; A0A178DTF8; -.
DR   OrthoDB; 1891044at2759; -.
DR   Proteomes; UP000077535; 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:UP000077535}.
FT   DOMAIN          326..532
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        13
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            125
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"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OAL47097.1"
SQ   SEQUENCE   538 AA;  59574 MW;  789AFB1A889298EA CRC64;
     AFRNPIISGV NADPSAIRVG DDYFLATSSF EYFPGLPIYH SKNLVDWNII GHGLTRQNAI
     FDRQALTSGG IFAPTLRHHN DTFFLITNYA DSFNPSDQRP FLITTKDIFS GEWSQPLYFD
     QTGIDPDLFF DDDGTVYLST ALPEFGPKGG NSTIWQSTVD LKTGNSLTQP ELIYRSDLPL
     SIRWAEGAHL YKINGTYYLS VAEGGTEVLH RQTIHRGPSP SGPWTRSPLG PLVFNSRDPT
     LPIQQTGHAD LLTRPDGKWY TVFLAVRPQL PQNINGTYQL GRETYLSPVT WSEDGWPLAN
     NGSAITFEID DASLPSQEIC ETSWNEDFSS PDLSTAWEFR GTPYGNWYHV SNSSLTLRGT
     PRTLSALDGI ALVLTRQDAL AYNFSVDLVF QPTLETHEAG IVAWVNEEYH HSVSLMLCKN
     QTSTVCLKTE TIAQGREVDG NVTTTYTALP DEYVSEGEAA ARLHIRATPD VYQLGYSGGD
     SSSPVWLTTF SAAWMAPRSG GRIAWNGARV GMFATGNGVP MLRDATFRHV EVSRDKCV
//
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