ID   CE12C_MAGO7             Reviewed;         309 AA.
AC   G4NBX2;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Endoglucanase cel12C {ECO:0000303|PubMed:20680265};
DE            EC=3.2.1.4 {ECO:0000250|UniProtKB:G4NAZ1};
DE   AltName: Full=Cellulase cel12C {ECO:0000305};
DE   AltName: Full=Endo-1,4-beta-glucanase cel12C {ECO:0000305};
DE   Flags: Precursor;
GN   Name=cel12C {ECO:0000303|PubMed:20680265}; ORFNames=MGG_10972;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=20680265; DOI=10.1007/s00253-010-2781-2;
RA   Takeda T., Takahashi M., Nakanishi-Masuno T., Nakano Y., Saitoh H.,
RA   Hirabuchi A., Fujisawa S., Terauchi R.;
RT   "Characterization of endo-1,3-1,4-beta-glucanases in GH family 12 from
RT   Magnaporthe oryzae.";
RL   Appl. Microbiol. Biotechnol. 88:1113-1123(2010).
CC   -!- FUNCTION: Endoglucanase that hydrolyzes 1,3-1,4-beta-glucan.
CC       {ECO:0000250|UniProtKB:G4NAZ1}.
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:0000250|UniProtKB:G4NAZ1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- MISCELLANEOUS: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the disaccharide cellobiose from the
CC       non-reducing end of the cellulose polymer chain; (3) Beta-1,4-
CC       glucosidases which hydrolyze the cellobiose and other short cello-
CC       oligosaccharides to glucose. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC       {ECO:0000305}.
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DR   EMBL; CM001235; EHA48174.1; -; Genomic_DNA.
DR   RefSeq; XP_003717758.1; XM_003717710.1.
DR   AlphaFoldDB; G4NBX2; -.
DR   SMR; G4NBX2; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH12; Glycoside Hydrolase Family 12.
DR   CLAE; EGL12C_MAGOR; -.
DR   EnsemblFungi; MGG_10972T0; MGG_10972T0; MGG_10972.
DR   GeneID; 2677726; -.
DR   KEGG; mgr:MGG_10972; -.
DR   VEuPathDB; FungiDB:MGG_10972; -.
DR   eggNOG; ENOG502RXZE; Eukaryota.
DR   HOGENOM; CLU_051064_0_0_1; -.
DR   InParanoid; G4NBX2; -.
DR   OMA; KSLPSVW; -.
DR   OrthoDB; 1236368at2759; -.
DR   Proteomes; UP000009058; Chromosome 5.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR002594; GH12.
DR   PANTHER; PTHR34002; PTHR34002; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01670; Glyco_hydro_12; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF49899; SSF49899; 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; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..309
FT                   /note="Endoglucanase cel12C"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432718"
FT   DOMAIN          274..309
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   309 AA;  32098 MW;  938DF82BDB20990C CRC64;
     MIKTLTAAIT LLAAGGVVAV PHPVANEKPT RTQPLSKRAT TVCGQWDSVQ TGGYTVYNNL
     WGKDSGTGSQ CLTVDGVSSG LLSWSTTWSW SGGQYNVKSY PNAVVSAPAA RLSAISSIPT
     RWQWSYTGNS MVANVAYDLF TNSNCGTTPE YEIMVWIGAY GGAGPISQSG QPIASPNIGG
     VTWRLYKGSH SQMTVFSFVS PGQITNYSGD LVNFVRYLTQ SQGMPASQCL YSAGAGTEPF
     TGSNARFTTS GYSMSISTSG SGGGEGGGGP NPPSCAALYG QCGGSGWSGP TCCTQGTCKA
     ANQWYSQCS