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Database: UniProt
Entry: A0A0D1YPG7_9EURO
LinkDB: A0A0D1YPG7_9EURO
Original site: A0A0D1YPG7_9EURO 
ID   A0A0D1YPG7_9EURO        Unreviewed;       777 AA.
AC   A0A0D1YPG7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=PV11_00493 {ECO:0000313|EMBL:KIV84727.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84727.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV84727.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84727.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072}.
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DR   EMBL; KN846951; KIV84727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1YPG7; -.
DR   STRING; 1016849.A0A0D1YPG7; -.
DR   HOGENOM; CLU_006010_0_0_1; -.
DR   OrthoDB; 2100839at2759; -.
DR   Proteomes; UP000053599; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..777
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002237229"
FT   DOMAIN          189..270
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          281..770
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          451..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  83038 MW;  75A758971F03AEAA CRC64;
     MAAFLTAVAT TASLLSIFTS LVNARSAPVQ ARDVTLPPIP GSPQIITNGA FTNATYGWES
     SPTGKIQNGL YCITVPSGSA PGNSSYLRTT YQFLETKNDV YTVNFTASSS VGFDINVQTP
     DPPLDPNLNT TAPLTTTPHP FSFTFSPANQ APNATLEFDL GGAPAEAQVC IGDVSMKRID
     RSGYVQFVGP ALKVNQLGYL PQGPKLATLV ANDTQAVTWS LLSSSGNTVA SGKTTPKGMD
     AASGQVVSTI DFSNVTQEGY GYVLTTGNAS SYPFTISSTV YDTLRQDSLL FFYQQRSGIA
     IDAALAGSQY ARAAGHVQVP PNQGDVQVPC QAVHDSMIAY LEPWTCNYTL NVTQGWYDAG
     DQGKYVVNGG ISAAQLLMEY ERTLHIANAT NALVDGSLRI PERNNGIPDI LDEARWEIDF
     LLKMQVPSGS PPQLFNGSMI DMSGLAHHKM HDNQWTPLPT DPSQDPKRRE LHRPSTAATL
     NLAAVGAMAA RSFAKYDSAF SQQCLQAATT AYTAAKKNPA ILAPSTDWDL GGGAYNDDDV
     TDEFYWAAAE LYLTTGQQQY LTDLTNNTYH TANVSTLFSI PGGFSWGSVA ALAQLDLATI
     PSNISNHSAI VQSVLAAADM YLAVQRNSSN GYGVFLNSYP WGSNSNNLNN VQVVATAYDL
     SGNTTYRDAA LQGIDYVLGR NALAFSYIRN YGTNYVQNVH SRLYAHELND QVPQAPAGAM
     SGGANEDASD PPADDVLQGC KPQLCHVDDV NSYSTNEVAI NWGSALAWVV GWAASQA
//
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