ID A0A177CI66_9PLEO Unreviewed; 994 AA.
AC A0A177CI66;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Probable beta-glucosidase E {ECO:0000256|ARBA:ARBA00039576};
DE EC=3.2.1.21 {ECO:0000256|ARBA:ARBA00012744};
DE AltName: Full=Beta-D-glucoside glucohydrolase E {ECO:0000256|ARBA:ARBA00041269};
DE AltName: Full=Cellobiase E {ECO:0000256|ARBA:ARBA00041599};
DE AltName: Full=Gentiobiase E {ECO:0000256|ARBA:ARBA00041811};
GN ORFNames=CC84DRAFT_1204596 {ECO:0000313|EMBL:OAG06951.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06951.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG06951.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06951.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes
CC involved in the degradation of cellulosic biomass. Catalyzes the last
CC step releasing glucose from the inhibitory cellobiose.
CC {ECO:0000256|ARBA:ARBA00024983}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00000448};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000256|ARBA:ARBA00004987}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV441551; OAG06951.1; -; Genomic_DNA.
DR RefSeq; XP_018037316.1; XM_018181915.1.
DR AlphaFoldDB; A0A177CI66; -.
DR STRING; 1460663.A0A177CI66; -.
DR GeneID; 28765401; -.
DR InParanoid; A0A177CI66; -.
DR OrthoDB; 5486783at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF20; BETA-GLUCOSIDASE E-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 889..985
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 994 AA; 108374 MW; 4E36B0C6299DC28A CRC64;
MAPLEFHELR RGKYAKLDAP VDDESPSRLS FASDASSFED LEEYDPLNYD AGTLKRKKST
GDLRTRKPSF KKEADGFALR PKPGRSCGIR QWCCWLLIFV TSVVLLFTAG GLWAYRRTLV
KDGMSPPWYP TPKGGADAAW QQSYSKAADM VRQMTLVEKV NITTGVGWSM GMCVGNTGPV
QRLKFPSLCL QDGPLGIRFA DNITAFPAGI TVGATWNKEL MYLRGKAHGE EARLKGVNVL
LGPAMGPLGR MPAGGRNWEG FGSDPVLQGV AAAQTIKGIQ DAGVIATAKH FILNEQEHFR
QAWEWGLPNA ISSNIDDRAL HEIYAWPFAE SVKAGVGSVM CSYNQVNNSY ACQNSKLMNG
ILKDELGFQG FVQSDWLAQR SGVAAALAGL DMSMPGDGLK WADGDSLWGA QLTKAVLNGS
VPIDRVDDMV TRIVAAWYQV GQDKWPEDGP NFSSWTNDEI GKIYEGSPSD DTKGVVNKFV
NAQGEGEDFH GNLVRKVAAE GTVLLKNEGH LLPLSRDGWQ EHEKKTDKYR VGIFGEDARL
SRDGINSCPD QSCNDGTLAS GWGSGAVDYP YLVDPLSALR KAFNNESVYV TDWPENTLPK
EKEIVEDQDL CIVFANAHGG EGYLKWSDVH GDRNDLNLQK GGDKLIQDVA KDCGKGKGDV
IVVIHAIGPV IMEKFISLPS VKAVVLANLP GQESGNALVD VLFGDVNPSG RLPYTIAKKE
EDYGPGSRIK YLPNPVEGLT PQQNFSEGLY IDYRHFDKYD IAPRYEFGHG LSYTTFHLSS
LLISSHGGRS PYPAPRPDPT IVPPTYPTTI PDPSSALLPP GFHKIEKYIY PYISSTSSVQ
KSQPKILANQ LQSPLSPAGG GPGGNPDLYS VLFTVSCVLT NIGLLPGSAV VQLYLSFPAD
SKHPETGEKV DFPVRVLRGF EKVFVDVEKG GVVKGVKGST HGGKGGNRVK VEFEVTRKDV
SYWDVQAQNW VIPEGTFGVG VGWSSRDLPL KGTW
//
