ID A0A9P9Y0Y6_9HYPO Unreviewed; 517 AA.
AC A0A9P9Y0Y6;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361164};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361164};
GN ORFNames=J7T54_005269 {ECO:0000313|EMBL:KAI6781558.1};
OS Emericellopsis cladophorae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Bionectriaceae; Emericellopsis.
OX NCBI_TaxID=2686198 {ECO:0000313|EMBL:KAI6781558.1, ECO:0000313|Proteomes:UP001055219};
RN [1] {ECO:0000313|EMBL:KAI6781558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MUM 19.33 {ECO:0000313|EMBL:KAI6781558.1};
RX PubMed=35049971;
RA Goncalves M.F.M., Hilario S., Van de Peer Y., Esteves A.C., Alves A.;
RT "Genomic and Metabolomic Analyses of the Marine Fungus Emericellopsis
RT cladophorae: Insights into Saltwater Adaptability Mechanisms and Its
RT Biosynthetic Potential.";
RL J Fungi (Basel) 8:0-0(2021).
RN [2] {ECO:0000313|EMBL:KAI6781558.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MUM 19.33 {ECO:0000313|EMBL:KAI6781558.1};
RA Goncalves M.F.M., Hilario S., Van De Peer Y., Esteves A.C., Alves A.;
RL Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000256|ARBA:ARBA00001641};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000256|ARBA:ARBA00006044, ECO:0000256|RuleBase:RU361164}.
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:KAI6781558.1}.
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DR EMBL; JAGIXG020000020; KAI6781558.1; -; Genomic_DNA.
DR RefSeq; XP_051362414.1; XM_051506211.1.
DR AlphaFoldDB; A0A9P9Y0Y6; -.
DR GeneID; 75831754; -.
DR OrthoDB; 412382at2759; -.
DR Proteomes; UP001055219; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR InterPro; IPR000254; CBD.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR PANTHER; PTHR33753:SF2; GLYCOSIDE HYDROLASE FAMILY 7 PROTEIN; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361164};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361164};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361164};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361164};
KW Reference proteome {ECO:0000313|Proteomes:UP001055219};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..517
FT /note="Glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040499733"
FT DOMAIN 481..517
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 443..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 55413 MW; 7D5E1EC88BF6E4DF CRC64;
MLTLAALSLL SVATAQKVGS DTPEVHPSMT WTQCTGSGCQ QVDGEVVIDA NWRWIHDSSL
ANCYDGNEWT GVCTSNTECA EECALEGANY GSTYGASTSG DALTLDFVTT HAYGTNIGSR
LYLMQDTDTY QMFNLLGNEL SFDVDLSTVP CGMNSALYFV AMEADGGMSS YPVNEAGAKY
GTGYCDAQCA RDLKFIGGQG NYDGWMASDT DANSGVGELG ACCAEIDIWE SNSHSYALTP
HSCETGFNEY HVCETTSCGG TYSDDRYGGK CDADGCDYNP YRLGRTGFYG EGKSVDTSQP
FTSVVTQFEL NGNMRQFFVQ NDNTVEVPTP AFDGLPDSNE INADFCDNVY DVFDTRSRYE
ELGGWSAMQE ALATPLVLVM SIWADNYANM LWLDGLYPRD SDPSQPGNLR GDCPADSGVP
SEVIANYPDS YVTWSNIKFG PIGSTTDDDS NPPPSSTTTA STTSTTTTSE GSGPTNPPGG
CTTPQWAQCG GNGFSGCTTC ASGTTCNYIN DWYSQCY
//
