ID A0A0A1TDQ6_9HYPO Unreviewed; 398 AA.
AC A0A0A1TDQ6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN ORFNames=VHEMI04239 {ECO:0000313|EMBL:CEJ86897.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ86897.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ86897.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|PIRNR:PIRNR037299}.
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DR EMBL; CDHN01000002; CEJ86897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TDQ6; -.
DR STRING; 1531966.A0A0A1TDQ6; -.
DR HOGENOM; CLU_027506_3_1_1; -.
DR OrthoDB; 337487at2759; -.
DR Proteomes; UP000039046; 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; IPR017168; Glyco_hydro_16_CRH1_prd.
DR PANTHER; PTHR10963:SF72; GLYCOSIDASE-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037299-2};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..398
FT /note="Glycosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001979544"
FT DOMAIN 31..240
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 278..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..375
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"
FT DISULFID 29..36
FT /evidence="ECO:0000256|PIRSR:PIRSR037299-2"
SQ SEQUENCE 398 AA; 40035 MW; 79A8239249B7CE0D CRC64;
MAFKSLSTTA VAVIAMGASL ASAQTSTSCD PTKTNCPADP ALGTSVNCDF TKGACDAFSL
VPGTQLTYGG QGAVFSISST QAPTIESNKY IFFGRVDVQL QAAPEAGIVT SIVFESDCLD
EIDWEFVGAD TSNAQSNYFA KGNTATYNRM IKVPVANAMS TSHLYSVEWT SDAIKWFVDN
KLVRTVTPAD AAAGGNGFPQ TPMRIRVGTW GAGLPTSPSG TRDWAGGLTD FSKAPFNAYY
KSITITDYAG GNAAGNGGVK EYTYGDRSGT WQSILVDGKK ATGGSSSGGN NNNTPPPASS
SAVVVPSSSS APPPASSSAA PPASSSTPPP ASSSAVTSQT GAPSTIVTST VAAPGNSSTT
APGTSPTNTP PPASGSTKLA VGGAFAAIAA GLVAQLLL
//
