ID   DCW1_ASHGO              Reviewed;         451 AA.
AC   Q75DG6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Mannan endo-1,6-alpha-mannosidase DCW1;
DE            EC=3.2.1.101;
DE   AltName: Full=Defective cell wall 1;
DE   AltName: Full=Endo-alpha-1->6-D-mannanase DCW1;
DE   Flags: Precursor;
GN   Name=DCW1; OrderedLocusNames=ABR060W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 128; 133-134 AND 144.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Required for normal synthesis of the cell wall.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in
CC         unbranched (1->6)-mannans.; EC=3.2.1.101;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR   EMBL; AE016815; AAS50830.2; -; Genomic_DNA.
DR   RefSeq; NP_983006.2; NM_208359.2.
DR   AlphaFoldDB; Q75DG6; -.
DR   SMR; Q75DG6; -.
DR   STRING; 33169.AAS50830; -.
DR   CAZy; GH76; Glycoside Hydrolase Family 76.
DR   EnsemblFungi; AAS50830; AAS50830; AGOS_ABR060W.
DR   GeneID; 4619110; -.
DR   KEGG; ago:AGOS_ABR060W; -.
DR   eggNOG; ENOG502QSWP; Eukaryota.
DR   HOGENOM; CLU_025694_1_2_1; -.
DR   InParanoid; Q75DG6; -.
DR   OMA; DGVHFEG; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007117; P:budding cell bud growth; IBA:GO_Central.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IBA:GO_Central.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR005198; Glyco_hydro_76.
DR   InterPro; IPR014480; Mannan-1_6-alpha_mannosidase.
DR   PANTHER; PTHR12145; PTHR12145; 1.
DR   Pfam; PF03663; Glyco_hydro_76; 1.
DR   PIRSF; PIRSF016302; Man_a_manosd; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW   Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..427
FT                   /note="Mannan endo-1,6-alpha-mannosidase DCW1"
FT                   /id="PRO_0000012121"
FT   PROPEP          428..451
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000012122"
FT   REGION          397..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           427
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  50371 MW;  E76E888B0F3D2DD9 CRC64;
     MLAVTFTAAA VLSLLAASGR TLNLDVDDLQ SIREATSLLA TGLMDYYHGH DYGETVGKFS
     DPYYWWEAGG AWGSILDYWY YMENSTYNDL LTDSLLHQAG EDLSYTPWNE TTTEGNDDQF
     FWGMAVMAAA ERNFPNPPAD QPQWLALAQA VFNTMALRWD METCNGGLRW QIFRWNDGYH
     YKNSVSNGAL FHMAARLTRY TGNATYLEWA ERVYDWMYGV GLISIVQPNW HVVYDGTDIN
     DNCTNLNKLQ WTYNHGLIMA GCAFIYNHTQ DELWHQRTLR FLDSARIFLS NDTLYEAGCQ
     GGDNCNIDQR SFKAYFSRFL GLTAQLVPES RETIVRWIRA SAQGAAASCS GGRDGHTCGL
     NWLINGWDGK WGLGEQMAAL EIIQNLRCLE RPAPYTAMNG GTSPGDPAAG TKTKAENLPP
     LDIKAGDRAG AGIITALIGS SFLACTLWLI I