ID A0A1V8T7F6_9PEZI Unreviewed; 345 AA.
AC A0A1V8T7F6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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=B0A48_07761 {ECO:0000313|EMBL:OQO07191.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO07191.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO07191.1}.
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DR EMBL; NAJO01000015; OQO07191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8T7F6; -.
DR STRING; 1507870.A0A1V8T7F6; -.
DR InParanoid; A0A1V8T7F6; -.
DR OrthoDB; 1887559at2759; -.
DR Proteomes; UP000192596; 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; 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:SF10; 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 Polysaccharide degradation {ECO:0000256|RuleBase:RU368122};
KW Reference proteome {ECO:0000313|Proteomes:UP000192596};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368122};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368122}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..345
FT /note="Endo-beta-1,4-glucanase D"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010739851"
FT DOMAIN 309..344
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 345 AA; 35481 MW; F543CE23EBBF2D84 CRC64;
MQFTVQQLAL LASILPTVHS HGFVIGATVG KTWYPGFDIQ LAYQANHPKV YGWDTKALDS
GFVSPDSFAT ADIICHKSAT PAGLHIPVTA GGQVTLYWSN SWPEGHQGPV LDYLAACPNN
DCSTVTKTDL NFAKIDQVGL VSGSSPGYWG EDQLAVANRS WTVTIPSSLA AGAYVLRHEI
LALHSARSAN GAQAYPQCVN LMVSGGGSAT VKGSSPETFY SATDPGILID IYNNAAGTYQ
IPGPTVQAFG GSGGSAPASS TTLVTSVRTT TTTAKATTTT APPVTTTTTK AATTTTTKAA
TTTTSAAGGS ASLYAQCGGQ GWTGPTTCAS GTCKAQSQYY SQCLP
//
