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Database: UniProt
Entry: S3BYV1_OPHP1
LinkDB: S3BYV1_OPHP1
Original site: S3BYV1_OPHP1 
ID   S3BYV1_OPHP1            Unreviewed;       449 AA.
AC   S3BYV1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   ORFNames=F503_02582 {ECO:0000313|EMBL:EPE06454.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06454.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE06454.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06454.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|PIRNR:PIRNR037299}.
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DR   EMBL; KE148153; EPE06454.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3BYV1; -.
DR   STRING; 1262450.S3BYV1; -.
DR   VEuPathDB; FungiDB:F503_02582; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_040459_0_0_1; -.
DR   OMA; WNATANQ; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000016923; 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:SF22; GLYCOSIDASE CRH2-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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299, ECO:0000313|EMBL:EPE06454.1};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..449
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004518262"
FT   DOMAIN          61..276
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          343..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        162
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        166
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ   SEQUENCE   449 AA;  46748 MW;  AEAF0E20F185C51D CRC64;
     MRSFVPIGAA LLGISSVALA AQAKCSLTQK CPESAPCCSQ YGECGVGAYC LGGCDPRMSF
     SLDACVPEPQ CESRVMKMDS LDRMISADKY LGDASEADWV YQGNPLVYND EAVLLTMPAK
     SVGTVLSSTV YMWYGNVKAT FKTSRGAGVI TAFILMSDVK DEIDYEFVGA DLKIAQTNYY
     FQGILDWHNS GNISLSDTYE NYHTYEIQWT PDSITWLVDG QVGRVKKKSD TWNATSNQWE
     FPQTPSRVGL SIWPGGASSN AQGTIDWAGG PIDWNSADIK NYGYDFATFK DVEIECYNAS
     SGAGTNNKVS YTFNNIAATN NTIVNGKDST VLKSFQGTGL DMDAGSSSAS SSAAGSSATD
     TNTVPGGSSS GPGSGPADNS GSGSGSGSDS GSTTGTAAGC SSTGFSQSCD SSGSGSSKSD
     GGRVAVGGER VFGASAFAVV VAFAGMLML
//
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