ID A0A1Y1YTU1_9FUNG Unreviewed; 570 AA.
AC A0A1Y1YTU1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=LY90DRAFT_393333 {ECO:0000313|EMBL:ORY00985.1};
OS Neocallimastix californiae.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Neocallimastix.
OX NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY00985.1, ECO:0000313|Proteomes:UP000193920};
RN [1] {ECO:0000313|EMBL:ORY00985.1, ECO:0000313|Proteomes:UP000193920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:ORY00985.1,
RC ECO:0000313|Proteomes:UP000193920};
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 "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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:ORY00985.1}.
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DR EMBL; MCOG01000513; ORY00985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YTU1; -.
DR STRING; 1754190.A0A1Y1YTU1; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000193920; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1220.10; Cellulose docking domain, dockering; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006970; PT.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF02013; CBM_10; 2.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF04886; PT; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF64571; Cellulose docking domain, dockering; 2.
DR PROSITE; PS51763; CBM10; 2.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 484..520
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 529..565
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT REGION 59..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..472
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 64360 MW; D166D395001E770D CRC64;
MAWLKPYLPG PSELDEVPIY INKKVYCQGC EITATGGDGS LWGMEDGKSC EIDKEICGLN
EQPTEEPTEQ PTEQPTEEPT EEPIKESGKL QYLGTNEAGG EFGDAVLPGV YNEHYIYPNI
NAIEASIEQG MNVFRMGLRW ERFQHELFGD LTEFDLTEYK KIVDATTAKG AVLIIDPHNY
ARYNNNVIGS EEVPIEAFAD FWAKLAEVFK DNEKVWFDLV NEPHDMETDD WFKAARAAVD
AIRTTGAKNN ILISGNGWDG AWSWGKEAWY GESNADVALR YFSSEDENII FEVHQYFDSD
YSGTHDTCVQ RPCQNLLKEF VEWLKTNNLK GWLGETSSTL SEGCKECVQE VLEYLEENRE
HVLGVTWWAA GPWWGHTACA IEPNEEKAFP EQMAWLKPYL PGPSELDEVP IYINKKVYCQ
GCEITATGGD GSLWGMEDGK SCEIDKEICG LNEQPTEEPT EEPTEEPTEE PTEQPVEPVV
EPSTCKFEAL GYKCCSHCIS YIEDEDGSWG VENGKWCGIS DECIKSYNEC WSKKYGYPCC
DTCNVFIIDK YGEWGIKDND WCGIPSTCKA
//
