ID   M2N0X8_BAUPA            Unreviewed;       429 AA.
AC   M2N0X8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=BAUCODRAFT_27601 {ECO:0000313|EMBL:EMC92290.1};
OS   Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS   (Baudoinia compniacensis (strain UAMH 10762)).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX   NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC92290.1, ECO:0000313|Proteomes:UP000011761};
RN   [1] {ECO:0000313|EMBL:EMC92290.1, ECO:0000313|Proteomes:UP000011761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC92290.1,
RC   ECO:0000313|Proteomes:UP000011761};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB445562; EMC92290.1; -; Genomic_DNA.
DR   RefSeq; XP_007680303.1; XM_007682113.1.
DR   AlphaFoldDB; M2N0X8; -.
DR   STRING; 717646.M2N0X8; -.
DR   GeneID; 19110599; -.
DR   KEGG; bcom:BAUCODRAFT_27601; -.
DR   eggNOG; ENOG502QTP4; Eukaryota.
DR   HOGENOM; CLU_029718_1_0_1; -.
DR   OMA; GYMESNS; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000011761; 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:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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, ECO:0000313|EMBL:EMC92290.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011761};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..429
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004021790"
FT   DOMAIN          17..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
FT   REGION          59..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  44239 MW;  2E1F0825B67579CD CRC64;
     MKTTLLALAA AAGTAVAQNA AYSQCGGQNW TGSTTCVAGY SCVAQNAYYS QCVPSSSSTT
     AATSKTSTSS SSTKASTPAT TSTKATSATT TTTKTTSTAA STPASTGHVQ YAGVNIAGFD
     FGCGTDGTCT TSSVVPPGAN GNGQMNHFVK DDGLNAFRLP VGWQYLVNNN LGGTLDATNF
     ANYDALVQGC LSSGAALCII DVHNYARWNG AIIGQGGPTN AQFVSLWSQL ATKYATNSKI
     AFGIMNEPHD LTISTWAATV QAVVTAIRQA GATSQKILLP GTQYTSAAAF ISDGSAAALN
     TVTNPDGTTT NLIFDVHQYL DSDNSGTHSN CVTNNSASFT TLAQWLRQNG RQAILTETGG
     GPSDSSCLTD VCQELDTLNT NSDVYLGWIG WGAGSFDTSY VLSETPTVSG STYTDQKLVT
     QCIAGKFKK
//