ID   A0A1Y2ERV6_9FUNG        Unreviewed;       536 AA.
AC   A0A1Y2ERV6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Arabinanase/levansucrase/invertase {ECO:0000313|EMBL:ORY74004.1};
GN   ORFNames=LY90DRAFT_699456 {ECO:0000313|EMBL:ORY74004.1};
OS   Neocallimastix californiae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Neocallimastix.
OX   NCBI_TaxID=1754190 {ECO:0000313|EMBL:ORY74004.1, ECO:0000313|Proteomes:UP000193920};
RN   [1] {ECO:0000313|EMBL:ORY74004.1, ECO:0000313|Proteomes:UP000193920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:ORY74004.1,
RC   ECO:0000313|Proteomes:UP000193920};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:ORY74004.1}.
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; MCOG01000031; ORY74004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2ERV6; -.
DR   STRING; 1754190.A0A1Y2ERV6; -.
DR   OrthoDB; 5470935at2759; -.
DR   Proteomes; UP000193920; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate 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:UniProtKB-KW.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd09003; GH43_XynD-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193920};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..536
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013005629"
FT   DOMAIN          394..488
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|Pfam:PF03422"
FT   REGION          488..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..536
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            182
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   536 AA;  58671 MW;  7EE1BFD31BCDDD30 CRC64;
     MKSVFFSTIL AIAGALVSAN DAFKDVVPKE TKKPIPDHNP INVIKYTADP GVMVYDDTVY
     VYGTNDGITE IMGENPESND YALIHTINVM SSKDLVNWVD HGTIPSAGKD GAAKWAQNSW
     APTAAHKKIN GKEKFFLYFA NSGNGIGVLT SDSPTGPFED PIGDYLISHD TPNCADITWL
     FDPAVFVDDD GSAYIYFGGG VPGEYDNHPL YKDAPLFERP RTLRVAKLGD DMISLATEPV
     LLDAPWPYED SGIHKADGIY YYTYCTSWNE KSPFGAARIG MMASKNPLGP FEFVDTIFNN
     PGDFFVVTGN NHHTVIPFHD KWYIFYHSEW LNLQNFGEAK GYRTTHVNEL PYVDGKFLNA
     TGTLEGVPQL FNVDAFETQT AALMAWEAGC STNGLGHTTV TYQKGEWSGV SGVDFDEGAD
     TIEIVAQSKN GAVIQVSVDS VEGEVLGYVE IPASDKMETV YTEIAPVKGV KNIFFLASDE
     VTVDTWEFGN TSDESDEEES ADAGADAEDV ESDDEENVEA DADEAEVEEE DSADEE
//