ID A0A059J9J8_TRIIM Unreviewed; 925 AA.
AC A0A059J9J8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=H109_03799 {ECO:0000313|EMBL:KDB24353.1};
OS Trichophyton interdigitale (strain MR816).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=1215338 {ECO:0000313|EMBL:KDB24353.1, ECO:0000313|Proteomes:UP000024533};
RN [1] {ECO:0000313|EMBL:KDB24353.1, ECO:0000313|Proteomes:UP000024533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR816 {ECO:0000313|EMBL:KDB24353.1,
RC ECO:0000313|Proteomes:UP000024533};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., White T.C., Graser Y., Martinez-Rossi N., Heitman J.,
RA Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Martinez D., Murphy C., Pearson M.D.,
RA Persinoti G., Poon T., Priest M., Roberts A.D., Saif S., Shea T.D.,
RA Sykes S.N., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Trichophyton interdigitale MR816.";
RL Submitted (FEB-2014) 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}.
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:KDB24353.1}.
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DR EMBL; AOKY01000263; KDB24353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059J9J8; -.
DR STRING; 1215338.A0A059J9J8; -.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OMA; WWYWTWK; -.
DR Proteomes; UP000024533; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:UP000024533};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
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 393..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 562..801
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 105686 MW; 97B11F18C64567DF CRC64;
MSGTRHSPHP PHRSRGRHHS DDLQYDYTYD RDDSDGYDRA YRKRRESRAR ESKTRRSGYR
GVHAEDEGVH ALDEDDVFDD RRHRSRKREH QPSRDRRHRD RVRTRDERVT WDSATESEDI
VDSRPIFARP PNASHSPRAD RRERDRDRER HSHYPSPRSG HKAKESPATS PKKRDRERDR
EGHNRHRPRR DSTADEGGDK RLRDRRRRGY DTDQEREYND RDTRRHGRRE KHTSNDSANS
ATVLLNSDAL AQLDQLNRKA DEDMKKKARK EEIKQQKKEK KKKKKYIFES GFAGDSEKER
EKGWESPGDV QRKKRREKDR EKEKKRLVSG AYLEEGRSPE LRTRGGGRRR TEKYHGGGGG
GGDDYYFSDG YDYEEEGSSG NGCLQNWSKR KKIVVVVGVC LLLLAIIIAV AVLVSKKNAG
GGKHPDGPVT TGPSHSELDG ISPNSIPPDA KGTHLDPFSW YDTADFNVTY TDETVGGLPI
MGLNSTWDDS AQANEKVPAL DKPFPYGKQP IRGVNLGGWL SMEPFITPSF FQRYSARDNV
VDEYTLTKRL GNAGKPTLEK HYATFVNEQT FKEIRDAGFD HVRIPYGYWV VTTYDGDPYF
AKMGWRYLLR AIEYCRKFGL RVNLDLHGVP GSQNGWNHSG RQGEIKWLKG DDGAKWGQRA
LDLHDQLSKF FAQPRYKNVI ALYGLANEPM MLKLDIEPVL DWTTKAADIV GGNGMKQKIV
FGDGFLKLSK WSSILQNTGH DLIIDTHQYT IFNADLIKLT HKKKLEFVCD SWVDLITKSS
TKGSGYGPTI CGEWSQADTD CTIYINSVGV GSRWTGTMDK NPIGGDPVLT PSCPSGKQCS
CDAANADPSQ YSDSYKKWLR LYAEAQISAF EKGWGWFYWT WDSESAAQWS WKKGMAAGIL
PSKAYEPEFK CGDDIPDFGD LPENY
//
