ID A0A2T3ZG28_9HYPO Unreviewed; 416 AA.
AC A0A2T3ZG28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:PTB43739.1};
GN ORFNames=M441DRAFT_190018 {ECO:0000313|EMBL:PTB43739.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB43739.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB43739.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB43739.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA 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.
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DR EMBL; KZ679259; PTB43739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ZG28; -.
DR STRING; 1042311.A0A2T3ZG28; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000240493; 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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
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; PS51164; CBM1_2; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..416
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015560906"
FT DOMAIN 35..340
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 380..416
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 345..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 43146 MW; 287010FED797D513 CRC64;
MHLAAFFAGL GLAGLVAGAP PSAPHKVKAR QASGAQNVVY WGGTNNESDD LSTYCTPTAG
IDILVLSFLD IYGATGNIPA GNIGNSCYIG TNGAPQLCDD LAASIASCQA AGIKIILSLG
GAAGSYSLQS QSQAVAIGQY LWEAYGNSGS TSVQRPFGSI FVNGWDFDLE LNAGNQYYQY
LISTLRSNFA SDPKNTYYIT GAPQCPLPEP NMGEIISTSQ FDYLWIQFYN NNAYAPDPCS
LGLPGDAPFN YNNWTSFIAT TPSKNAKLFI GVPANTLAAN GNSGGAVYYA SPSQLASIVA
NTKSSPDFGG IMMWDAGYSD ANVNNGCNYA QEAKNILLTG APCGGSPPPV SSSTPTSTAR
TTKPATSTSS ASGTGPTGGG TVPQWGQCGG EGYTGPTQCV SPYKCIESSQ WWSSCQ
//
