ID A0A436ZYD6_9PEZI Unreviewed; 416 AA.
AC A0A436ZYD6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=CBM1 domain-containing protein {ECO:0000259|PROSITE:PS51164};
GN ORFNames=DFL_005794 {ECO:0000313|EMBL:RVD84027.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD84027.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD84027.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD84027.1,
RC ECO:0000313|Proteomes:UP000283090};
RA Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT "Intercellular communication is required for trap formation in the
RT nematode-trapping fungus Duddingtonia flagrans.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:RVD84027.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; SAEB01000007; RVD84027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZYD6; -.
DR VEuPathDB; FungiDB:DFL_005794; -.
DR Proteomes; UP000283090; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF00734; CBM_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000283090};
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 /note="CBM1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019107396"
FT DOMAIN 18..54
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 42776 MW; 39C85FDD9963F90D CRC64;
MHSLAVITAL LAAVPALAQA PLWGQCGGNG WTGPTTCVSG ACCQYSNEWY SQCVSGTCGG
SNPQTTTRTT TGGNTQPTNS GGCGGGTPDV TVTGSSSSYT TKNKSGTTLY TGNNYLSAIN
AAVNGISSGQ RVSVIASGSI GANTISIGSG KTFEVCGTID VGNRSGRGAI ESTGTTGVTI
PYLTMTGNPY FGLLFYGTRD LTLGQITMNL SGGLGIRFHR DEAANYNVKM DTIRVTGAGS
HAVETWNING LTINQVIARN CGECGLLLQK TNDAKVGLVD GNNVATGTGY ATLRFANENG
RGSGNWNTNI YVDKVVSRGG GRGIFCVSQS GGAEIQTVDL ASNGNNAILI ENCYNVAIKG
GTVNGGGEVR LAARTEFANN RDISITLKVD NTSVRESPCG TNIKWSLSGN GSRNIC
//