ID A0A436ZXF2_9PEZI Unreviewed; 556 AA.
AC A0A436ZXF2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=CBM6 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DFL_007802 {ECO:0000313|EMBL:RVD83416.1};
OS Arthrobotrys flagrans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Arthrobotrys.
OX NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD83416.1, ECO:0000313|Proteomes:UP000283090};
RN [1] {ECO:0000313|EMBL:RVD83416.1, ECO:0000313|Proteomes:UP000283090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD83416.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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:RVD83416.1}.
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DR EMBL; SAEB01000009; RVD83416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A436ZXF2; -.
DR VEuPathDB; FungiDB:DFL_007802; -.
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:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR CDD; cd04086; CBM35_mannanase-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS51764; GH26; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01100}; 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..556
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019488747"
FT DOMAIN 21..139
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 160..454
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT DOMAIN 313..328
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 520..556
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 462..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 556 AA; 60140 MW; 7350CE5D786B95EF CRC64;
MLGLVPFILA ILAGSSSAQT VTYQAESATL TGVTVGTDVA GFTGTGYVEG FDTSGDEIKF
TVTSTSQGLY DLKIIYNGPY GDKYTTVVLN GAGGGQVFLP ATTSWVTVSA GQVLLDAGSN
TIQIQNNWGW YLIDAITLTP STPRGPHQIS TTPANPAANS DAKALLKYLG SIYGKNILSG
QQDQDSLDWV TSNVGKTPAI LGLDLMDYTD SRTSRGASST DVDKAIAFAA RGGIVTFCWH
WGAPVGLYDT PEQRWWSGFY TEATDFNVAT ALADTTNANY TLLIHDIDTI AVQLKKLETA
GVPVLFRPLH EAEGGWFWWG AQGPEPCKKL WNLVHDRLTN YHGINNLIWI WNSVAADWYP
GDATIDIVSA DVYTQGDHGP ISATYNSLLD LVDDKKIIAA SEIGSIMDPV QLQLYQADWV
YFCVWSGDFI SGGQWNSLDF IKSVYNHDYV LNLDEIQGWK NPTTTTTTTS VRPTSTTTSR
RTTTPVTTTA SSRTTTPRTT TTTRATTTPS TTTTSATPTA VAGHWQQCGG IGYTGPTVCE
SPYTCTVLNP YYYQCL
//
