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Database: UniProt
Entry: A0A1Z5SUY1_HORWE
LinkDB: A0A1Z5SUY1_HORWE
Original site: A0A1Z5SUY1_HORWE 
ID   A0A1Z5SUY1_HORWE        Unreviewed;       570 AA.
AC   A0A1Z5SUY1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   28-JUN-2023, entry version 14.
DE   RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN   ORFNames=BTJ68_11861 {ECO:0000313|EMBL:OTA24619.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA24619.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA24619.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA24619.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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:OTA24619.1}.
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DR   EMBL; MUNK01000236; OTA24619.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5SUY1; -.
DR   STRING; 1157616.A0A1Z5SUY1; -.
DR   VEuPathDB; FungiDB:BTJ68_11861; -.
DR   InParanoid; A0A1Z5SUY1; -.
DR   OrthoDB; 1891044at2759; -.
DR   Proteomes; UP000194280; 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; cd18833; GH43_PcXyl-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:UP000194280};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..570
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013369200"
FT   DOMAIN          354..551
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        208
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            152
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   570 AA;  63450 MW;  23A75BC78AB98BD4 CRC64;
     MKSLLTLSAL GVVTALHGYS DKNSTYFNPI IPGFHPDPSC IFVPEWEDTF FCAVSSFIAF
     PGMPVFASKD LQNWRLISHV HNRPEQALTF GNISRNSAGW YAPTLRFHEG TFYVINVDVD
     AQAPSSGIFT TTNPYQDSAW SDLMPIPVGG YDPDLFFDPD GTVYIQYAAT ISNDPFTTEI
     DQVTVDLSTG NTSEPHFLSN GTGVQPPEGP HMYYKDGYYW LLLAEGGTAL DHQVTMSRSK
     SPTGPWELDP GNPVLTAINS SSLFQTVGHA DLFHDAAGNW WACALSTRSG PEYVHWPMNR
     EAVLTPVSWP GDDWPVFDPV DGLMPGPLPR VNPFVAGRGQ FVGSNDYYKF APRTSLPEHF
     TFWRFPKREN YVVSPPGHPY RLQLTPSNAN LTGFEDFSPL DGQTFVGRRQ EHTLFSYRVA
     MEFSPSNAGE EAGVTVFLRQ ERNAELGLIS MDDKYALRFR ATGPDAPETV VREVPQWWAH
     RGIQFEIKAF NFTHYSLSAG PKGKRHLETV ALVDNSLFST SFTGVFVGVY ATTNGNGEGG
     TKAYFSDWRY KGIAQAIGID EYHYEGYGHH
//
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