ID G4T7S3_SERID Unreviewed; 426 AA.
AC G4T7S3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=PIIN_01190 {ECO:0000313|EMBL:CCA67360.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA67360.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA67360.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA67360.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:CCA67360.1}.
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DR EMBL; CAFZ01000013; CCA67360.1; -; Genomic_DNA.
DR AlphaFoldDB; G4T7S3; -.
DR STRING; 1109443.G4T7S3; -.
DR eggNOG; ENOG502QXN4; Eukaryota.
DR HOGENOM; CLU_029718_0_1_1; -.
DR InParanoid; G4T7S3; -.
DR OMA; FRMERLI; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000007148; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..426
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003468250"
FT DOMAIN 21..53
FT /note="CBM1"
FT /evidence="ECO:0000259|SMART:SM00236"
SQ SEQUENCE 426 AA; 46576 MW; C7789F56B0B638CB CRC64;
MKLSLSLAAI AALLPQALGI SRWDTCGGGG VTTGKCDDGL VCVELSEYYY QCLKLAPPYS
PTSTSTSTST RTTSTTFVVV YEHPELEQLY LDFSINFYKH LDDDYVQYKF FDVRNIDICL
PRCQEVQVLR SSAEFGSAIP GTLNKDYTWP SPSSVDYFLG KGMNFFRIPF MMERMSPPAT
GLTGPFDSAY LSGLKTIVNY ITSKGGYAAL DPHNYARYNG SVITDVSLFK TWWKNMATEF
LTNDHVIFDL NNEPWGIPAT DAAALMQAGL DGVRAAGATQ SVFVQGTSWT GAWSWESSGN
GDAFKTISDP LNNVVIEMHQ YLDTDGSGTN STCVSPTVGA ERLQVATNWL KANNKKGFIG
ELGAGSNNDC ISAIRGALCL MQTSDVWIGF AWWAAGPWWG NYYQSIEPPS GPAIARILPE
ALLPFA
//
