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Database: UniProt
Entry: V5FAI0_BYSSN
LinkDB: V5FAI0_BYSSN
Original site: V5FAI0_BYSSN 
ID   V5FAI0_BYSSN            Unreviewed;       438 AA.
AC   V5FAI0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   ORFNames=PVAR5_1974 {ECO:0000313|EMBL:GAD93364.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93364.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
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:GAD93364.1}.
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DR   EMBL; BAUL01000055; GAD93364.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FAI0; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_040459_0_0_1; -.
DR   InParanoid; V5FAI0; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000018001; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
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; IPR018371; Chitin-binding_1_CS.
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; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299, ECO:0000313|EMBL:GAD93364.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..438
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004732822"
FT   DOMAIN          62..291
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          342..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..411
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   438 AA;  45744 MW;  66AAB4B76E7A8517 CRC64;
     MVRFASTLLL GALSASAVLA ADSTTCSPDS KCPSDKPCCS QYGECGTGAY CLGGCDPLSS
     NALDSCAPAP ICQSKTYNFD NLDGIQSNTK YLGDASKADW VSSGQPLAND GSLILTMAPK
     TVGTLLANNH YMWYGKATAR MKSSRGKGVV TAFILLSDVK DEIDYEFVGA DLEHAQTNYY
     FQGITDYDNG ANASTTDTFD DWHTYEIDWT PDQITWSIDG QVNRVKKKSE TWNATANRYQ
     FPQTPARVQL SLWPAGLSTN APGTIAWAGG EIDWDSQDIK DHGYYYAMFD QVTLECYDPP
     TGANIQGNSS YIYTNDAGTN NTVEITDKPT VLSSFEATGT NMTAGASSSK SSSSASSSAS
     GDDTVPGVKG GSGAASGDSG SSSSSSGSGS GTSSGSGSST TGFSQGGSQN NGALSQNERV
     LKGSLFAVLV AVVVLVAM
//
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