ID G1XCM6_ARTOA Unreviewed; 212 AA.
AC G1XCM6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=AOL_s00079g61 {ECO:0000313|EMBL:EGX49107.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49107.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX49107.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.
CC {ECO:0000256|ARBA:ARBA00025221}.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGX49107.1}.
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DR EMBL; ADOT01000137; EGX49107.1; -; Genomic_DNA.
DR RefSeq; XP_011122238.1; XM_011123936.1.
DR AlphaFoldDB; G1XCM6; -.
DR STRING; 756982.G1XCM6; -.
DR GeneID; 22893621; -.
DR eggNOG; ENOG502QTQG; Eukaryota.
DR HOGENOM; CLU_1299439_0_0_1; -.
DR InParanoid; G1XCM6; -.
DR OMA; MNFGSFY; -.
DR OrthoDB; 2655644at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF7; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE C; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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 Reference proteome {ECO:0000313|Proteomes:UP000008784};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 177..212
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
SQ SEQUENCE 212 AA; 22534 MW; D68B2546BF9ACB02 CRC64;
MDSGLLKTAG TSSYQIAWTS FGNGAMEGAF IYYRSGYYYL FTSWGNCCQL VPRPAAGTEY
HMRVCRSTSA TGGFKDKNGV DCKSSGGTTI LESHDYVYAP GHGGVIDVPG VGSVLYYHYV
NNNQGTNQAA TYFGWNVLDW PSDWPVISTG TSTPTTTTKT TTSRAAQTTT TAATSGNCAS
LYGQCGGQGF TGAACCSSGT CKYSNDWYSQ CL
//
