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
//