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Database: UniProt
Entry: A0A1J7ITD0_9PEZI
LinkDB: A0A1J7ITD0_9PEZI
Original site: A0A1J7ITD0_9PEZI 
ID   A0A1J7ITD0_9PEZI        Unreviewed;       340 AA.
AC   A0A1J7ITD0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Glycoside hydrolase family 61 protein {ECO:0000313|EMBL:OIW30750.1};
GN   ORFNames=CONLIGDRAFT_289742 {ECO:0000313|EMBL:OIW30750.1};
OS   Coniochaeta ligniaria NRRL 30616.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW30750.1, ECO:0000313|Proteomes:UP000182658};
RN   [1] {ECO:0000313|EMBL:OIW30750.1, ECO:0000313|Proteomes:UP000182658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW30750.1,
RC   ECO:0000313|Proteomes:UP000182658};
RG   DOE Joint Genome Institute;
RA   Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA   Van Elsas J.D., Nichols N.N.;
RT   "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT   lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT   hydrolysates.";
RL   Submitted (OCT-2016) 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; KV875096; OIW30750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J7ITD0; -.
DR   STRING; 1408157.A0A1J7ITD0; -.
DR   InParanoid; A0A1J7ITD0; -.
DR   OrthoDB; 2722085at2759; -.
DR   Proteomes; UP000182658; 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:SF9; ENDOGLUCANASE II; 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; 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:OIW30750.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182658};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          301..338
FT                   /note="CBM1"
FT                   /evidence="ECO:0000259|PROSITE:PS51164"
SQ   SEQUENCE   340 AA;  33530 MW;  4E7EB04152418FE3 CRC64;
     MKSVSIILAA LAAKEVAGHA LFQELWVDSV DMGTQCARVP QSNTPVTNVG GTDVRCNVGG
     SRGVSKKCAV KAGSTVTVEM HQQPGDRSCS SEAIGGAHYG PVMVYMSKVS DAATADGSTG
     WFKVFEDGWN KKDGGGAGDN DYWGVKDLNA CCGKMDVKIP ADIAPGDYLL RAEVIALHTA
     GSSGGAQLYM SCYQLTVSGT GTATPATVRF PGAYKASDPG ILVNIHAALS TYVVPGPAVY
     TGGTTKSAGS ACTGCAGSCK AGSGATGTAI AAALPTSAAS AGPDAAGGSA GAAAPGGDAG
     CAVQAFGQCG GNGYTGCTSC GSGATCKAVS PPYYSQCVPS
//
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