ID A0A163CP54_DIDRA Unreviewed; 315 AA.
AC A0A163CP54;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=EKO05_0009560 {ECO:0000313|EMBL:UPX19292.1}, EKO05_008460
GN {ECO:0000313|EMBL:KAF9704679.1}, ST47_g6311
GN {ECO:0000313|EMBL:KZM22603.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM22603.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM22603.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM22603.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:KAF9704679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704679.1};
RA Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF9704679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704679.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [4] {ECO:0000313|EMBL:KAF9704679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:KAF9704679.1};
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UPX19292.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX19292.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has endoglucanase activity on substrates containing beta-1,4
CC glycosidic bonds, like in carboxymethylcellulose (CMC),
CC hydroxyethylcellulose (HEC) and beta-glucan. Involved in the
CC degradation of complex natural cellulosic substrates.
CC {ECO:0000256|ARBA:ARBA00025192}.
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|ARBA:ARBA00000966,
CC 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}.
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DR EMBL; RYYQ01000017; KAF9704679.1; -; Genomic_DNA.
DR EMBL; JYNV01000212; KZM22603.1; -; Genomic_DNA.
DR EMBL; CP095304; UPX19292.1; -; Genomic_DNA.
DR STRING; 5454.A0A163CP54; -.
DR OrthoDB; 2722085at2759; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 17.
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:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd21175; LPMO_AA9; 1.
DR Gene3D; 2.70.50.70; -; 1.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR PANTHER; PTHR33353:SF17; ENDO-BETA-1,4-GLUCANASE D; 1.
DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 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 Monooxygenase {ECO:0000313|EMBL:UPX19292.1};
KW Oxidoreductase {ECO:0000313|EMBL:UPX19292.1};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU368122};
KW Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368122};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368122}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..315
FT /note="Endo-beta-1,4-glucanase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041079723"
FT DOMAIN 279..315
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 235..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 315 AA; 32158 MW; 9C04880D95CD17A9 CRC64;
MKFSAVLAVA AASQLASAHT TVWNILVNGK DAGVGNSQGG YIDSPPNNNP VTDVTSSAMT
CNVAGVKAAK SIAVKGGDKI AFQWHHDSNQ ASDDIIASSH KGPIMVYASK AGSSYSWTKI
WEDGYTDGKW AVDKLIAGSY TGKAGQHDLT LPNLAPGEYV LRPEINALHE GDRQGGAQFY
MECVHIKVEG SGTAVLPAGV SFPGAYKATD PGVLFNIYSG FTSYTAPGPK VWNGASSGSA
PAAPAPTKAP AATAKPTATK TTLATVAKPT PTKAAGAAGS AAKWGQCGGI GYTGATACVS
GSTCTKQSDY YSQCL
//
