ID A0A0P7BWU7_9HYPO Unreviewed; 470 AA.
AC A0A0P7BWU7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=AK830_g194 {ECO:0000313|EMBL:KPM46495.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM46495.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM46495.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM46495.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) 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:KPM46495.1}.
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DR EMBL; LKCW01000001; KPM46495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7BWU7; -.
DR STRING; 78410.A0A0P7BWU7; -.
DR OrthoDB; 1638835at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..470
FT /note="cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006136299"
FT DOMAIN 172..439
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 129..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 49199 MW; C53E7C409E555C88 CRC64;
MRPSFLLVVA GASLAACRPC KPRTSSSTNT PLETLVETPV ASSTATLVAP VVSSVATSVP
LNATQTVFTP TRAQTSALDT AISSASLDAT PVVSTQVSAG TSTAAAVASS VVSSASLDAS
LAVSTLPGVE TSTPATTATP VASSAPSSQT SSAAPSKATN GSSSGFLFTG INEAGAEFGT
GNIPGTEGTD YTFPNTSAID ILFDAGMNAF RVGFLMERMV PDELTGTLDS DYFDGINTVV
THVTGKGAYA ILDPHNYGRY YSNIITDVDA FGSFWTTLAT KFADNELVVF DTNNEYHDME
NSLVAELNQA AITAIRGAGA TSQYIFVEGN SYSGAWTWVS SGNGDSLVDL TDPQDKLIYE
MHQYLDSDGS GTAEACVDST IGATRLEAAT AWLKENGKLG IIGETAGANN DVCQTAIKGE
LQHLQDNSDV WVGFLWWAAG PWWDDYMFSM EPSNGIAYEN YLSIIQEFLV
//
