ID G1XIV6_ARTOA Unreviewed; 487 AA.
AC G1XIV6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN ORFNames=AOL_s00097g283 {ECO:0000313|EMBL:EGX46857.1};
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:EGX46857.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX46857.1, 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 16 family.
CC {ECO:0000256|PIRNR:PIRNR037299}.
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:EGX46857.1}.
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DR EMBL; ADOT01000174; EGX46857.1; -; Genomic_DNA.
DR RefSeq; XP_011124418.1; XM_011126116.1.
DR AlphaFoldDB; G1XIV6; -.
DR STRING; 756982.G1XIV6; -.
DR GeneID; 22895325; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_3_1_1; -.
DR InParanoid; G1XIV6; -.
DR OMA; QTPMNIH; -.
DR OrthoDB; 337487at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR PANTHER; PTHR10963:SF27; GLYCOSIDASE CRH1-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..487
FT /note="Glycosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003427099"
FT DOMAIN 16..231
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 266..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ SEQUENCE 487 AA; 51358 MW; 1F89DC45C56B6986 CRC64;
MQVKRFVLIA AALLPAAFAQ TSSDCNPLKG CFKDDPALGT TYSWDYTKNH GEAPRFDIVS
SASRISYQDD GMHMSVMMRG DSPTLQSQFY IFWGRAEIVM KAGPGAGIVS SLVFQSDVLD
EIDVEFIGNQ PGNVQTNIFS KGNQDVHIYG ANTAVADTVG VFHKYTVDWT PQQITWSIDG
NVVRVLSRAE LGEVVYPQTP MQIKFGPWAA GDPSNAPGTI EWAGGPIDYS LAPFDMVVAS
LSITDYSTGA TKYRYKDTSG SAASIEITGG GIVNPPPQQE TTSSAPPPAP TTTSAPPPPP
TTTSSKPSPP PPTTTSTPPP PPPPPTTTSS KSTPPPPPPP PTTTSEPTTT SESTTSTTEE
PETTTSKLNI PTKIITTSSS PVTTSSKPPP PPKPTTTSSE EEETTTSVKE TSTSYRPTKS
TFSVETTHSS TSSEPTERSG ETTLATVIST QSSGVRLPTN SDVPSSGSSI RTASSLVIAI
VALFVLF
//
