ID L2FU09_COLFN Unreviewed; 313 AA.
AC L2FU09;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Endo-1,4-beta-glucanase {ECO:0000313|EMBL:ELA29827.1};
GN ORFNames=CGGC5_9811 {ECO:0000313|EMBL:ELA29827.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA29827.1};
RN [1] {ECO:0000313|EMBL:ELA29827.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA29827.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC {ECO:0000256|ARBA:ARBA00009585}.
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DR EMBL; KB020829; ELA29827.1; -; Genomic_DNA.
DR RefSeq; XP_007281146.1; XM_007281084.1.
DR AlphaFoldDB; L2FU09; -.
DR STRING; 1213859.L2FU09; -.
DR EnsemblFungi; ELA29827; ELA29827; CGGC5_9811.
DR HOGENOM; CLU_031730_1_0_1; -.
DR OrthoDB; 1887559at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd21175; LPMO_AA9; 1.
DR Gene3D; 2.70.50.70; -; 1.
DR InterPro; IPR005103; AA9.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR PANTHER; PTHR33353:SF10; ENDO-BETA-1,4-GLUCANASE D; 1.
DR PANTHER; PTHR33353; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12560)-RELATED; 1.
DR Pfam; PF03443; AA9; 1.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..313
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003958609"
FT DOMAIN 277..313
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 256..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 32250 MW; DEC9FF28F63C1B92 CRC64;
MGIIAPSSLL LSLATLVASH GHVDWLVADN VAYRGWDSPA FTYSPPTYPV VGWKIDAPDN
GFVEPVNFGT GDIICHKNGS PAGGHATVPA GAKIQLVWNT WPESHKGPVI DYLAKCSGNC
ESVDKTSLNF FKISAGGLID MSLSNGKWAD DVLMANNFTW TVQIPSNLAP GNYVLRHEII
ALHSGGNVNG AQAYPQCFNL QVTGGGSLAP AGVKGTALYK SDDPGILFNL YTSPLVYPIP
GPTLAAGISS STAAQSTARP TATSSATAPG GGGSGGSTVP KYGQCGGIGY TGSTTCASGS
TCQVLNEYYS QCV
//
