ID A0A2T4B876_9HYPO Unreviewed; 412 AA.
AC A0A2T4B876;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:PTB65510.1};
GN ORFNames=BBK36DRAFT_1169225 {ECO:0000313|EMBL:PTB65510.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB65510.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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DR EMBL; KZ680214; PTB65510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4B876; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 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; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000241546};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015538057"
FT DOMAIN 32..339
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 376..412
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 347..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 42739 MW; 051702A1E5034F17 CRC64;
MFFTKVVGSL SLLAGLASAA PNPIARRQAA GAQNVVYWGQ NGGGTIENND LSAYCTPTSG
IDIIVLSFLY QWAEGSSVLG GTIGQSCGIS NSGEPQNCDA LTAAITKCKA AGVKMILSLG
GASAFSSFQT ADQAANAGQY LWNAYGGGSG VTRPLGNNVM DGWDLDIESN PGTNENYAAL
VSALRSNFPS DPSRQYVISG APQCPLPEPN MGVIIQNAQF DYLWVQFYNN NDYPGDPCSL
GLPGDAPFNF NNWTTFIQST PSKNAKVFVG VPAAPLAANG APSGEVYYAT PAQLAEIVND
VKSNPAFGGV MMWSAGFSDS NVNNGCNYAQ EAKNILLTGS PCSSGPVTIS PPPVTTPITI
SSPPTSSQTP PPSSGGSVPQ WGQCGGNGYT GPTQCVAPFK CVATSEWWSQ CE
//
