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Database: UniProt
Entry: A0A409VDF6_9AGAR
LinkDB: A0A409VDF6_9AGAR
Original site: A0A409VDF6_9AGAR 
ID   A0A409VDF6_9AGAR        Unreviewed;       429 AA.
AC   A0A409VDF6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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=CVT24_006308 {ECO:0000313|EMBL:PPQ62910.1};
OS   Panaeolus cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Galeropsidaceae; Panaeolus.
OX   NCBI_TaxID=181874 {ECO:0000313|EMBL:PPQ62910.1, ECO:0000313|Proteomes:UP000284842};
RN   [1] {ECO:0000313|EMBL:PPQ62910.1, ECO:0000313|Proteomes:UP000284842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2629 {ECO:0000313|EMBL:PPQ62910.1,
RC   ECO:0000313|Proteomes:UP000284842};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
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:PPQ62910.1}.
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DR   EMBL; NHTK01006136; PPQ62910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409VDF6; -.
DR   STRING; 181874.A0A409VDF6; -.
DR   InParanoid; A0A409VDF6; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000284842; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF5; CBM1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
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|RuleBase:RU361153};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284842};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..429
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019043131"
FT   DOMAIN          16..52
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          55..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  45082 MW;  22C7F046D3F8CF36 CRC64;
     MKSAFFILLT AVLVHAEQPL YGQCGGIGWS GETTCVSGAT CTVLNDYYSQ CLPGSGSSTT
     EVPAPTTTSE TVTPTPTTTT GTDTPPTTTT EVPSPTTTTE TDSPAPTTTG TPGAGGLPFL
     GGVNLAGYDF SVYTNGSFSG TGVDPPVSQV SHFAGQGVNA FRIPFAWQLM TPSLGGDIDA
     TFFSRYDATV QAALGASTQP YVILDLHNYA RWNGQIISQG GPTNEQYASL WSQVAAKYMD
     NPKIIFGIMN EPHDLQSVPT WVESVQAAVN AIRDAGATTQ YILIPGSSWS SAEAFPNEAG
     PLLLQVTDPA GGTDKLIFDV HKYLDVDNSG THTECTTDNV AVFTTLANFL RENGNRQALL
     SETGGGNTQS CVTAMGAQLA YIKANSDVLT GFTIWSAGSF DTTYELTVTP NPDGSDQMLW
     AQAVIPNLP
//
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