ID T0LKJ1_COLGC Unreviewed; 345 AA.
AC T0LKJ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Glycosyl hydrolase family 61 {ECO:0000313|EMBL:EQB52166.1};
GN ORFNames=CGLO_08243 {ECO:0000313|EMBL:EQB52166.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52166.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 61 family.
CC {ECO:0000256|ARBA:ARBA00009585}.
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:EQB52166.1}.
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DR EMBL; AMYD01001646; EQB52166.1; -; Genomic_DNA.
DR AlphaFoldDB; T0LKJ1; -.
DR STRING; 1237896.T0LKJ1; -.
DR HOGENOM; CLU_031730_1_0_1; -.
DR OMA; NDWPSSH; -.
DR OrthoDB; 1887559at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
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, ECO:0000313|EMBL:EQB52166.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
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..345
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004567005"
FT DOMAIN 309..345
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 250..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 35217 MW; D039916A6D1C4D8B CRC64;
MGIITPSSLL 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 GGSGSSPTTA RTTTAAAPAT TTTARTTTTT
AAGGGSGGTT VPKYGQCGGI GYTGSTTCAS GSTCQVLNEY YSQCV
//
