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Database: UniProt
Entry: A0A2J6PDX7_9HELO
LinkDB: A0A2J6PDX7_9HELO
Original site: A0A2J6PDX7_9HELO 
ID   A0A2J6PDX7_9HELO        Unreviewed;       345 AA.
AC   A0A2J6PDX7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=NA56DRAFT_756799 {ECO:0000313|EMBL:PMD12199.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD12199.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD12199.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD12199.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-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}.
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DR   EMBL; KZ613561; PMD12199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6PDX7; -.
DR   STRING; 1745343.A0A2J6PDX7; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000235672; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:PMD12199.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..345
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014428086"
FT   DOMAIN          47..314
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   345 AA;  37205 MW;  ABE0FC2F3B3970AA CRC64;
     MRLGNLVLIF TSFSGALAAP AANADPAPNE RSVSTNKKRS NFWFAGVNES GAEFGSNNIP
     GKLGTDYTWP LTSSVDTLMG KGFNIFRIPF LMERLVPGGL YNSADATYLS GLTNLVNHIT
     NKGGYAAICA QNFGRYNGNI ITDTAGFQAF WKTIASHFSG NSHVIFDTNN EYHDMDNSLV
     GNLNQAAING IRAAGATSQT IFVEGNSYTG AWTWVSSGTD TAMGALTDPH DNIIYEMHQY
     LDSDGSGTHS TCVSTTIGQQ RLVAATNWCR SNKKNCIIGE TAAGSNSVCL SAIEGMLSYM
     KANNDVWRGW LLWGGGPWWG DYMFSVEPPS GTQYVGVVPS ILQYI
//
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