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Database: UniProt
Entry: G0RXC7_HYPJQ
LinkDB: G0RXC7_HYPJQ
Original site: G0RXC7_HYPJQ 
ID   G0RXC7_HYPJQ            Unreviewed;       438 AA.
AC   G0RXC7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   Name=cel5b {ECO:0000313|EMBL:EGR44174.1};
GN   ORFNames=TRIREDRAFT_82616 {ECO:0000313|EMBL:EGR44174.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR44174.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR44174.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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}.
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DR   EMBL; GL985099; EGR44174.1; -; Genomic_DNA.
DR   RefSeq; XP_006969897.1; XM_006969835.1.
DR   AlphaFoldDB; G0RXC7; -.
DR   SMR; G0RXC7; -.
DR   STRING; 431241.G0RXC7; -.
DR   EnsemblFungi; EGR44174; EGR44174; TRIREDRAFT_82616.
DR   GeneID; 18489491; -.
DR   KEGG; tre:TRIREDRAFT_82616; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_82616; -.
DR   eggNOG; ENOG502QTP4; Eukaryota.
DR   HOGENOM; CLU_029718_1_1_1; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF5; CBM1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:EGR44174.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008984};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..438
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003409107"
FT   DOMAIN          59..308
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          354..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   438 AA;  46855 MW;  4CB5DF426A29D710 CRC64;
     MRATSLLAAA LAVAGDALAG KIKYLGVAIP GIDFGCDIDG SCPTDTSSVP LLSYKGGDGA
     GQMKHFAEDD GLNVFRISAT WQFVLNNTVD GKLDELNWGS YNKVVNACLE TGAYCMIDMH
     NFARYNGGII GQGGVSDDIF VDLWVQIAKY YEDNDKIIFG LMNEPHDLDI EIWAQTCQKV
     VTAIRKAGAT SQMILLPGTN FASVETYVST GSAEALGKIT NPDGSTDLLY FDVHKYLDIN
     NSGSHAECTT DNVDAFNDFA DWLRQNKRQA IISETGASME PSCMTAFCAQ NKAISENSDV
     YIGFVGWGAG SFDTSYILTL TPLGKPGNYT DNKLMNECIL DQFTLDEKYR PTPTSISTAA
     EETATATATS DGDAPSTTKP IFREETASPT PNAVTKPSPD TSDSSDDDKD SAASMSAQGL
     TGTVLFTVAA LGYMLVAF
//
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