ID A0A2D3UMI5_9PEZI Unreviewed; 770 AA.
AC A0A2D3UMI5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN ORFNames=RCC_02386 {ECO:0000313|EMBL:CZT16552.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT16552.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT16552.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT16552.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
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 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
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DR EMBL; FJUY01000003; CZT16552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3UMI5; -.
DR STRING; 112498.A0A2D3UMI5; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000225277; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277};
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 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 398..639
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 87094 MW; 2EAB1BB255BBB0EA CRC64;
MPASSSQVPR DSPARRQRRR RTHQRTDSNG ELLGNYDEDA IPASPGRARR SHHERRSSRT
PRSEQTRTSS TALSSEQLAR LDRLNQNQGW SEYERVPQPR RVDREDEIRA ERARAERDEK
DREERRERER QRRRDERRRR RREEAEAEAS LDEQEREELA YEPRRTKRRS ERRSQRPERR
VISGQTLERG AGRYYSDKEE FRDDVREGTS SSAVSAEEGE RKRKRKRNIL IGVAIIIIAL
AIIIPVAVVV SKKSGSSSTE KTGGTSTGGS SKPSNSNLDS ISKDDIPQAA QGTVLDPFTW
YDTLDFNLTY TDATVGGLSV MGLNSTWDDS KRANNNVPPL NKPFEYGKMP IRGVNVGGWL
SLEPFITPSF FSRFTTSDGV IDEWTLTERL GGQAKSTIET HYSSWVQEST FADIQAAGFD
HVRIPFSYWA VTTYDGDPYV AQVSWRYMLR GIEWARKYGL RINLDLHGAP GSQNGWNHSG
RQGIIRWLNG TDGTLNGDRT IDIHKQLSAF FTQPRYKNIV TMYGLVNEPR MVKLEESTVI
AWTKAAAEAV RGNNFTGIIV FGDGFMGLDN WQGELQGIDD LLLDVHQYVI FNVDQIVLNH
QDKINFACGG WTAQALRSQN TATGFGPTLC GEWSQADTDC APNLNNVGVG SRWEGTLNMV
STPGGGVDGS ILNPTCPTKN SPRCSCDGAN ASPSEWSDGY KQWLLMFAEA QMHSFEQGWG
WFYWTWQTES APQWSYKTSL AAGTMPKLAY ERSFNCSSDI PDFSDLPEYY
//
