ID W3XJB2_PESFW Unreviewed; 319 AA.
AC W3XJB2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=PFICI_04173 {ECO:0000313|EMBL:ETS86148.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS86148.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912110; ETS86148.1; -; Genomic_DNA.
DR RefSeq; XP_007830945.1; XM_007832754.1.
DR AlphaFoldDB; W3XJB2; -.
DR STRING; 1229662.W3XJB2; -.
DR GeneID; 19269186; -.
DR KEGG; pfy:PFICI_04173; -.
DR eggNOG; ENOG502QRTW; Eukaryota.
DR HOGENOM; CLU_031730_0_1_1; -.
DR InParanoid; W3XJB2; -.
DR OMA; INEGCGK; -.
DR OrthoDB; 2722085at2759; -.
DR Proteomes; UP000030651; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030651};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..319
FT /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004834662"
FT DOMAIN 284..319
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 319 AA; 32481 MW; DAD23AFAC0F6BB14 CRC64;
MQSVLVAIAA LAAQQVAAHA TFQDFWINGV DYGAQCIRLP LSNSPVTDVT SNDIRCNAGT
SPVSYKCAVA AGDTVTIEIH QQPGDRTCTT EAIGGAHYGP VQAYLSAVDD SSTADGSDGW
FKIFADTWAK NPSGSSGDDD YWGTKDINTC CGRLDVKIPT DIKAGDYLLR AEALALHTAS
SSGGAQFYMS CIQLTITGSG SASPSTISFP GAYAASDPGI LVDIHAAMTT YIAPGPTVYS
GGSTKSAGAA CEGCETTCTA GAGASGTATS VTLPSSTGGG SDGCTVALYG QCGGIDYTGC
TNCYQGTCTV LSDYYYQCA
//
