ID A0A2T4AJJ3_TRIHA Unreviewed; 412 AA.
AC A0A2T4AJJ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Carbohydrate-binding module family 1 protein {ECO:0000313|EMBL:PTB57202.1};
GN ORFNames=M431DRAFT_112925 {ECO:0000313|EMBL:PTB57202.1};
OS Trichoderma harzianum CBS 226.95.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB57202.1, ECO:0000313|Proteomes:UP000241690};
RN [1] {ECO:0000313|EMBL:PTB57202.1, ECO:0000313|Proteomes:UP000241690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB57202.1,
RC ECO:0000313|Proteomes:UP000241690};
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; KZ679678; PTB57202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AJJ3; -.
DR STRING; 983964.A0A2T4AJJ3; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000241690; 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:UP000241690};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015585983"
FT DOMAIN 34..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 348..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 42958 MW; ABB59043A3F18B6E CRC64;
MLSTSLILGL GLVGFGVAAP SYPQSIKARQ APGAQNVVYW GGNNNENDNL ATYCKPGAGI
DILVLSFLDI YGTTGNIPYG NIGNSCYIGS TGVPQQCDNL AASIATCQAA GIKIILSLGG
AAGSYSLQSQ SQAVAIGQYL WEAYGNSGST SVVRPFGNVI VDGWDFDLEL NLGNQYYQYL
ISTLRSNFPS DPTKTYYITG APQCPIPEPN MGEIISTSVF DYLWIQFYNN NGYGPDPCSL
GLPGDAPFNF NNWTSFIATT PSKNAKLFIG VPANTLAANG NAGGAVYYAT PAQLATIVQN
TKSNPAFGGI MMWAAGYSDA NVNNGCTYAQ EAKNILLTGA PCGGSQPVSS SLPTTTAKPT
KSATSTSSAT GSGPTGTVPQ WGQCGGEGYT GPTQCIAPYK CVAQGEWWSS CQ
//
