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Database: UniProt
Entry: G1WY49_ARTOA
LinkDB: G1WY49_ARTOA
Original site: G1WY49_ARTOA 
ID   G1WY49_ARTOA            Unreviewed;       555 AA.
AC   G1WY49;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN   ORFNames=AOL_s00004g209 {ECO:0000313|EMBL:EGX54176.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX54176.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX54176.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX54176.1}.
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DR   EMBL; ADOT01000005; EGX54176.1; -; Genomic_DNA.
DR   RefSeq; XP_011117161.1; XM_011118859.1.
DR   AlphaFoldDB; G1WY49; -.
DR   STRING; 756982.G1WY49; -.
DR   GeneID; 22888060; -.
DR   eggNOG; ENOG502QQH8; Eukaryota.
DR   HOGENOM; CLU_016508_2_0_1; -.
DR   InParanoid; G1WY49; -.
DR   OMA; WLVNMIW; -.
DR   OrthoDB; 1891044at2759; -.
DR   Proteomes; UP000008784; 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:UP000008784};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..555
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003425581"
FT   DOMAIN          360..550
FT                   /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT                   /evidence="ECO:0000259|Pfam:PF17851"
FT   ACT_SITE        28
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   SITE            148
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   555 AA;  62905 MW;  0AEB55EE24F92ABB CRC64;
     MLTTLLFTLL IGVSCAFRNP IIPGFNPDPS IIRVENDYFL VTSTFEFFPG VPVYHSKDLI
     DWTCIGHALN RPSQLNLRGT APSGGIFAPT LRYHEASKTF YMITTWFDVI SPPDNTTGTP
     RSMYVSTKNI LDETSWGDPI YVDQWGFDPD LFFDTDGKTY LTTTMGSGFI DPDSGYFAIW
     ITEIDLKTGN SLTESRYFYR SELPINTPRL AEGSHIYKFN GTYYLLTAEA GTEVQHRAMW
     HRSNSLHGPW ESSPYNPFVF NGRNLSQPIL STGHADIVQT PNGDWYTVFL ATRPQNPTDS
     SGVPQLGRET FLAPVTWKDG WPIANGGKDI TFEISGLYNK PRPKVWQDHF WNGEYNGFAD
     RRYYTQRTPT KAFHSFKARK GWLRLYGNVY TLSDRQTPAM FLRKQEDINT VFNTELEFYP
     TSARHKAGVT AFLSTWLHQD IVITLHPETG KRVVAATTRT GKEPVAKTTY VEIPETGTVK
     LWIKCEADKY TLGYSLGHDR KATWVASAES KWMQSYPSGW QNFVGTHLGV FATGDGLPIL
     VPADFKWIKT EGGDW
//
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