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Database: UniProt
Entry: A0A094A098_9PEZI
LinkDB: A0A094A098_9PEZI
Original site: A0A094A098_9PEZI 
ID   A0A094A098_9PEZI        Unreviewed;       734 AA.
AC   A0A094A098;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-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=V493_06125 {ECO:0000313|EMBL:KFY23061.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY23061.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY23061.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-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:KFY23061.1}.
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DR   EMBL; JPJV01002317; KFY23061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094A098; -.
DR   STRING; 1420906.A0A094A098; -.
DR   HOGENOM; CLU_004624_4_2_1; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000029327; 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:UP000029327};
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        195..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          370..560
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          1..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  83676 MW;  52DFFCA9BD5EC267 CRC64;
     MPREAERPRH RERDPDRERE REQRRRERER DPERERRHRE RDPDRERRRR ERDPERELER
     EERRRERARR KSRNPDRDSR DSRSRDEPPS SQSSSQPLSA DTLAQLNLLN KKEGSRKPEK
     RPKPERPRKK RHREAFNEKY EAIGVDKPRR EKKKKRRVVS GALLEEGDGK RLSYIRGGGY
     DKQAEADAAK RKKRIWIIVG VVILLLAIII PVAVVVSNKN KGKTAEADKT EGPTDVTGPS
     NSNLDDVDPA SVPAAAKGSR TDPFSWFDTT DFNVTYTGEK VGGLPVIGLF SEWDDSAKAN
     EKVPALNEPW GTYATRPARG VNVGGWLSVE PFITPSLFNP YDPRLGIKDE WTLCEHLGPT
     AAKQTLEKHY ATFVTEQTFA EIKDAGLDHV RIPFSYWALQ NHYGEPYVEG VAWRYLLRGI
     EWARKYGLRI NLDVHGLPGS QNGWNHSGRQ GDIGWLNGTD GAINAERSLE MHRSLSAFFS
     QPRYKNIIAF YGLVNEPKMT ALEPAEVNAW TEKAYTLVRK NGITCPIVFG DGFLGLGNWK
     GQLQGHEGLV LDVHQYVIFN VGQIVYTKQA KVKYACTGWT GQAQQSMDVS TGFGPTIFAE
     WSQADTDCAT YLNNVGWGNR WEGTYDTGNP LTRVLSATCP TNKDGPTCSC TNANADPSQY
     SEGYKQFLQM FAEAQMDSFE HGWGWFYWTW QTEKATQWSY KRGLAAGILP AKAYAPEFNC
     QKTIPDFKDV PENY
//
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