ID   A0A0P1BMF4_9BASI        Unreviewed;       494 AA.
AC   A0A0P1BMF4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=chitin deacetylase {ECO:0000256|ARBA:ARBA00024056};
DE            EC=3.5.1.41 {ECO:0000256|ARBA:ARBA00024056};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17887.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH17887.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + n H2O = n acetate +
CC         chitosan; Xref=Rhea:RHEA:10464, Rhea:RHEA-COMP:9593, Rhea:RHEA-
CC         COMP:9597, ChEBI:CHEBI:15377, ChEBI:CHEBI:17029, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57704; EC=3.5.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10465;
CC         Evidence={ECO:0000256|ARBA:ARBA00023996};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; CCYA01000265; CEH17887.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BMF4; -.
DR   STRING; 401625.A0A0P1BMF4; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF138; CHITIN DEACETYLASE; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Hydrolase {ECO:0000313|EMBL:CEH17887.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT   DOMAIN          229..429
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          63..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  51898 MW;  1710D44300312124 CRC64;
     MSAQSSRPRF ADTVQVRHGV SFSLFPTQIP YPLILTMVRT SLFVAAAAAM ALPMAVADLR
     PERRQAESSS SRRHRSSATA TASAGSGSGA VSSPPAFTGS LPASISSIVA TLTPGTRSPE
     PTYPLPTTFQ AGATNTYISG APPLPSAPTI ANYPPLDEPP LRSFQGSEQL LAGIDLSGVK
     DVPLNQGSAG CGEAGNEANL ANAGASGNCW WTCGGCTRDT DIVQCPDKNT WGLSYDDGPS
     PYTPLLLDYL EKNNLKTTFF VVGSRALSRP DMLAYEYMTG HQLSVHTWSH TSLTTQTNEA
     IALELLWTKK IIHDITGVTP NTMRPPYGDI DDRVRGVSKA VGLTPIIWTS ANGGNYDTND
     WKIGSGVVSA GEVVSVFDGI IANASTLDHG YIVLAHDLYE QSVKLATEIV LPQALSQSPK
     QNIVPIITCL KKPLGDSYVE TNRNTSDSAP ATNGNNENTS SGSGSGSGAG LNMELSKAHL
     TIVGAVLFGA ATLL
//