ID A0A1Y1VJ65_9FUNG Unreviewed; 779 AA.
AC A0A1Y1VJ65;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
DE Flags: Fragment;
GN ORFNames=BCR36DRAFT_318558 {ECO:0000313|EMBL:ORX57763.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX57763.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX57763.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX57763.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORX57763.1}.
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DR EMBL; MCFH01000005; ORX57763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VJ65; -.
DR STRING; 1754191.A0A1Y1VJ65; -.
DR EnsemblFungi; ORX57763; ORX57763; BCR36DRAFT_318558.
DR OrthoDB; 121538at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.90.1220.10; Cellulose docking domain, dockering; 3.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR009034; Dockerin_dom_fun_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; PF02013; CBM_10; 3.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF64571; Cellulose docking domain, dockering; 3.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51763; CBM10; 3.
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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10060};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 22..779
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5011809952"
FT DOMAIN 646..682
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 690..728
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 740..776
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT ACT_SITE 436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT NON_TER 779
FT /evidence="ECO:0000313|EMBL:ORX57763.1"
SQ SEQUENCE 779 AA; 85614 MW; DC9BACB10287172D CRC64;
MKFSTIITAI AALVAPMTAV AKSQDYARHL ELSLLFYEAQ RSGKLPENNR IYWRHDSLVD
AGADNGVDLS GGYYDAGDNA KFNFPGAATM TLLAWSGIDY AEGYKSAGQW EYILDAVRWG
ADYFMKCHTG KNELYAQVGD GNTDHGFWYP PEYVKYDYPS FKVTAEKPGS EVAGETAAFL
AAASILFKDE DSSYSAKLLK HAKEIYEFAD TYRGDYTGAI PGVVSFYSTY SGYNDELAWG
AAWLLRATGD ESYLNKYNVI ANKKYESYDP KKFSGATGPI SWDDKRPGCY ILIAMVTGDE
NRIKEAYNYC DAVLTQPKTP GGLWYDDGLS MWGSNRYASN AASMLAMFAN YLPKSDPKRA
KYVEFVQQQT NYILGDNPAK INYVVGAEAN SPKAVHHRGS SGVFDSQDKA AKPDENIYTL
WGALAGGPDE TDSYIDTRSN FRTNEVALDY NAAFQMNLAF LTQEGLSKPD PDSVKIHERS
WPKKAETPDI RLKFSDGELS IATGSGMRCS GWCVSFTSSS YKITQTSDGN IVNSGPEYTI
CNKRENNALD GKGTAHIVTF QASGSSLPTE FTVLCDGFHA PLNHQKYSYI PEWGRQYKVV
NGGGVENTTP LFEETECWPG FICDGSAPSP STTKTKTPVQ TSVSNDCFAI AQGYECCNDN
EVVYTDESGQ WGIKDGQWCG IGGASTPEPT PEPQPDCGAY PCCNECEVIY TDNDGDWGVE
NNEWCLINKL VCGGNPKPKT CTGQDSGFPC CNHCEVIYND NDGPWGIENG EWCGISSEC
//
