DCW1_CANGA
ID DCW1_CANGA Reviewed; 446 AA.
AC Q6FLP9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=CAGL0L01727g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380958; CAG61815.1; -; Genomic_DNA.
DR RefSeq; XP_448845.1; XM_448845.1.
DR AlphaFoldDB; Q6FLP9; -.
DR SMR; Q6FLP9; -.
DR STRING; 5478.XP_448845.1; -.
DR CAZy; GH76; Glycoside Hydrolase Family 76.
DR EnsemblFungi; CAG61815; CAG61815; CAGL0L01727g.
DR GeneID; 2890890; -.
DR KEGG; cgr:CAGL0L01727g; -.
DR CGD; CAL0136136; CAGL0L01727g.
DR VEuPathDB; FungiDB:CAGL0L01727g; -.
DR eggNOG; ENOG502QSWP; Eukaryota.
DR HOGENOM; CLU_025694_1_2_1; -.
DR InParanoid; Q6FLP9; -.
DR OMA; DGVHFEG; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0046658; C:anchored component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007117; P:budding cell bud growth; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..422
FT /note="Mannan endo-1,6-alpha-mannosidase DCW1"
FT /id="PRO_0000012123"
FT PROPEP 423..446
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012124"
FT REGION 389..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 422
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 49699 MW; A0620B99956608ED CRC64;
MRLVTLLSGL VSLVSVFGLE LDLDDYASLQ NATALVAYGL MDYYTGDQYG KTVGMFSDPY
YWWQAGGAWG CMLDYWYFMQ NDTYNDKIMA ALLHQTGDNN DYVPLNQSTT EGNDDQAFWG
IAVMQAAERK FPNPPDDKPQ WLYLTQAVFN TMALRWDSET CGGGLRWQIF VWNSGYDYKN
TVSNGALFHI AARLARYTGN QSYVDWAERV YDWMEDVHLI DNGTYRYVYD GVSINDNCTT
VTKYQWTYNQ GLMLSGSAYL FNMTGSDLWH ERTHAFLNAS RVFFNNSILY EAACQGPNTC
NTDQRSFKAY FARFLGSTAE LVPETRQQIM TWLNTSALAA AKSCSGGTDG HTCGLNWFRD
DWDGMYGLGE QMAALEVMVN TQALKRAPPY NATNGGNSTG DGAAGTKPHP TNLAPLHITG
GSRAGAGIIT AIIGISIIAC ALWLVY
