UniProt: A0A0D7BU38

Database: UniProt
Entry: A0A0D7BU38_9AGAR

LinkDB:  A0A0D7BU38_9AGAR 
Original site:  A0A0D7BU38_9AGAR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (12)   

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ID   A0A0D7BU38_9AGAR        Unreviewed;       596 AA.
AC   A0A0D7BU38;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CYLTODRAFT_428306 {ECO:0000313|EMBL:KIY73740.1};
OS   Cylindrobasidium torrendii FP15055 ss-10.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC   Cylindrobasidium.
OX   NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY73740.1, ECO:0000313|Proteomes:UP000054007};
RN   [1] {ECO:0000313|EMBL:KIY73740.1, ECO:0000313|Proteomes:UP000054007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY73740.1,
RC   ECO:0000313|Proteomes:UP000054007};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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         ECO:0000256|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10060,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; KN880434; KIY73740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7BU38; -.
DR   STRING; 1314674.A0A0D7BU38; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000054007; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10060};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10060}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        566..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          68..517
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          448..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        496
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        505
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   596 AA;  64118 MW;  8195CCE9A5EAD995 CRC64;
     MSPSVQGVCT KNPSREGLRV MARSKNWTGD HRIRTQCSGS VGRQPWALAQ VSLPTEPWLP
     ADNTDATFAN LLGHLVYFYD AQRTGKLPAS NRVSWRNDSC LEDGKEDGVD LSGGFFDAGD
     YIKATFPMSF AIMSICWGAT DFGHGYDLAN QTAYLDGVLR WGLDWLMKAH DSDNSLYVLV
     ANAGLNNDYW GGDENIPTPR PTFQVNATNP GTDVVAGVSA AFSACSSLYN GQSFGGPYSN
     PASLKNTTYA KTLLSHSEKL YTFAVNASGG QALYQESVPE VGSSYPSSSY EDELTIAALF
     LARASNSTTL FNEAIGDFDK YKLRNSDAVF NWDSKTPGIA VLFAQMTCAN STDQLGGDFE
     QWRDAAEDYF DDVISHQGKT DGGLAYWEGD SQSASLNPAL NVAMLLARYA PLASSDDKRQ
     KYEEYAKGQL DYVLGKNPMN VPYVVGVNSN SPSNPHSAPA SGGDDVGAID TSPAEEAYVL
     YGATVGGPDR WDDFYDIRSD WPQTEVALDY NAPLLTLAAM YVLKDGSDPY YAALKEGARI
     TPKGSPCDEA ITTGCKAGSL PSTGKIVVGV VVSAVGAFIV GLGCYYVWLV TTVQTA
//

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