ID A0A1Y1VJ66_9FUNG Unreviewed; 784 AA.
AC A0A1Y1VJ66;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN ORFNames=BCR36DRAFT_580333 {ECO:0000313|EMBL:ORX57760.1};
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:ORX57760.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX57760.1, 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:ORX57760.1, 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:ORX57760.1}.
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DR EMBL; MCFH01000005; ORX57760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VJ66; -.
DR STRING; 1754191.A0A1Y1VJ66; -.
DR EnsemblFungi; ORX57760; ORX57760; BCR36DRAFT_580333.
DR OrthoDB; 121538at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 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; 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..23
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 24..784
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5011826191"
FT DOMAIN 654..691
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 698..734
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 745..781
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT ACT_SITE 437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 784 AA; 86217 MW; 969278D0AE422AC8 CRC64;
MKFQKIVSAI AALVAPMAVV AKSQDYARHI ELSLLFYEAQ RSGKLPENNR VYWRHDSLLD
AGADNGVDLT GGYYDAGDNV KFNFPGAAAL TLLAWSGIDY ADGYKEAGQW DYILDAVRWG
ADYFVKCHTG KNELYVQVGK GATDHGFWYP PEYVQYDHPS YKITAAAPGS EVAGDTASFL
AAASILFKDI DSSYSSNLLK HAIEIYDFAD SYRGEYIKAV PDAQGFYSNW SGYNDELAFG
ALWLYRATGE SKYMDKFSKI ADASYGEQDT KAYGTCTGPI SWDDKRPGAY ILAAIITGDE
KRMKQASWYC DNVLTQPKTP GGLWYDANLS KWASNRYASN AAAMVAMYAN YLPSSDSKRS
KYVDFVKKQT DYILGDNPAK INYVVGAEAN SPKAVHHRGA SGTYDSQDTN AKPTDYNIFT
LWGALAGGPG PDDEYTDSRK NYEMNEVALD YNAAFQMNLA FLVKEGFNKP DPDSVKIHDR
SFPKKADTPD VKVEVTEKTI EISTGSNMMC SSWCIEFTTD YKIEAVHDCI MHQSGPDYII
CNRRESNFLD GKGTPQIIKY QGSNGQDPLT INESVVMCDG WHAPQSSHKP VYRPENGRRY
KVTGSGGVGN TTPLFEQSEC WPAFLCGGSN TTPKTTIKKT TTTTKKSEPT SSSSCFAKSM
GYACCSVGTE VVYTDNDGQW GIENGQWCGI GGGQQQQQQE EKCGDYACCS GCESVYVDND
GKWGVENGNW CLIKESKCGG SSAVTCTGMN SGYQCCDTCN VVYTDNDGKW GIMNGEWCGI
KSSC
//
