ID A0A093YRQ9_9PEZI Unreviewed; 540 AA.
AC A0A093YRQ9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Endo-beta-1,4-glucanase D {ECO:0000256|RuleBase:RU368122};
DE Short=Endoglucanase D {ECO:0000256|RuleBase:RU368122};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU368122};
DE AltName: Full=Carboxymethylcellulase D {ECO:0000256|RuleBase:RU368122};
DE AltName: Full=Cellulase D {ECO:0000256|RuleBase:RU368122};
GN ORFNames=V492_08526 {ECO:0000313|EMBL:KFY05458.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY05458.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY05458.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY05458.1,
RC ECO:0000313|Proteomes:UP000029299};
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: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds. Involved in the degradation of complex natural
CC cellulosic substrates. {ECO:0000256|RuleBase:RU368122}.
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|RuleBase:RU368122};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU368122}.
CC -!- DOMAIN: Has a modular structure: an endo-beta-1,4-glucanase catalytic
CC module at the N-terminus, a linker rich in serines and threonines, and
CC a C-terminal carbohydrate-binding module (CBM). The genes for catalytic
CC modules and CBMs seem to have evolved separately and have been linked
CC by gene fusion. {ECO:0000256|RuleBase:RU368122}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC {ECO:0000256|ARBA:ARBA00009585}.
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:KFY05458.1}.
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DR EMBL; JPJU01003684; KFY05458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YRQ9; -.
DR STRING; 1420902.A0A093YRQ9; -.
DR HOGENOM; CLU_503558_0_0_1; -.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030248; F:cellulose binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd21175; LPMO_AA9; 2.
DR Gene3D; 2.70.50.70; -; 2.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR PANTHER; PTHR33353:SF9; ENDOGLUCANASE II; 1.
DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR Pfam; PF03443; AA9; 2.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU368122};
KW Cellulose degradation {ECO:0000256|RuleBase:RU368122};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU368122};
KW Glycosidase {ECO:0000256|RuleBase:RU368122};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368122};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU368122};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368122};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368122}.
FT DOMAIN 272..308
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 250..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 55102 MW; C147972082896403 CRC64;
MKLQDAYNLA AVLSVASAHT IMQSFNGNPM GDAIYMPSSN MYQSDVNANT LACNGAPATG
FRSSSKKITV QAGSTVTGLW LHELGSTDSN PGSDTDNKVI ASSHKGPLLA YMKKVSDATQ
NPSAGPGNGW FKISEVGLIS STQWAVDALI SAGGVQSVKI PSCIENGDYL LRFEIIALHS
ASTYPGAQFY VECAQITVTG GTGTATPSTV SIPGTYSGSD PGIKVSIYNT KGTPYPSSYT
IPGPPVFTCP SGSGSNPPAT TTPGGGSGGG SGAAPKYGQC GGIGWTGPTV CAAGSTCKAS
GDYYSHMKHI ISLAALVASA VAHSTFQELW VDGVDQEGTC IRTPPSNSPV QSVTSGDITC
NVGGTTGVAG LCSVAAGQTV TVEMHAQAGD RSCDTEAIGG NHFGPVIVYM GKVDDATTAD
GSGPIWFKVD QEGYDVPTKT WGTMTLNDNC GKRTFTVPSS LAPGNYLLRA EVIALHAAGS
SGGAQFYMSC YQLEVTGSGT ASPSGVSFPG AYSASDPGIL IDIYSEITSY TVPGPDVFTG
//
