ID   CEL1_AGABI              Reviewed;         320 AA.
AC   Q00023;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Cellulose-growth-specific protein;
DE   Flags: Precursor;
GN   Name=cel1;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D649;
RX   PubMed=1398098; DOI=10.1016/0378-1119(92)90270-y;
RA   Raguz S., Yaguee E., Wood D.A., Thurston C.F.;
RT   "Isolation and characterization of a cellulose-growth-specific gene from
RT   Agaricus bisporus.";
RL   Gene 119:183-190(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D649;
RX   PubMed=8181702; DOI=10.1111/j.1574-6968.1994.tb06718.x;
RA   Armesilla A.L., Thurston C.F., Yaguee E.;
RT   "CEL1: a novel cellulose binding protein secreted by Agaricus bisporus
RT   during growth on crystalline cellulose.";
RL   FEMS Microbiol. Lett. 116:293-299(1994).
CC   -!- FUNCTION: Probable glycosyl hydrolase active on cellulose.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family. {ECO:0000305}.
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DR   EMBL; M86356; AAA53434.1; -; Genomic_DNA.
DR   PIR; JC1311; JC1311.
DR   AlphaFoldDB; Q00023; -.
DR   SMR; Q00023; -.
DR   CAZy; AA9; Auxiliary Activities 9.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CLAE; PMO9A_AGABI; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005103; AA9.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   Pfam; PF03443; AA9; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..320
FT                   /note="Cellulose-growth-specific protein"
FT                   /id="PRO_0000008031"
FT   DOMAIN          284..320
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          30..261
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          255..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..285
FT                   /note="Linker"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        292..309
FT                   /evidence="ECO:0000250"
FT   DISULFID        303..319
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  33754 MW;  60E2C8080895CA2B CRC64;
     MRLPSRQQVL KMLATFSLAL GLFAAKVQAH GGVIGYSWDG TWYEGWHPYN TPVGQTSIER
     PWATFDPIMD ATASTVGCNN DGNPGPNQLT ATVAAGTAIT AYWNQVWPHP YGPMTTYLGK
     CPGSSCDGVN TNSLKWFKID EAGLLSGTVG KGVWGSGKMI DQNNSWTTTI PSTVPSGAYM
     IRFETIALHS LPAQIYPECA QLTITGGGNR APTSSELVSF PGGYSNSDPG LTVNLYTQEA
     MTDTTYIVPG PPLYGSGGNG GSPTTTPHTT TPITTSPPPT STPGTIPQYG QCGGIGWTGG
     TGCVAPYQCK VINDYYSQCL