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Database: UniProt
Entry: C5DDS2_LACTC
LinkDB: C5DDS2_LACTC
Original site: C5DDS2_LACTC 
ID   C5DDS2_LACTC            Unreviewed;       467 AA.
AC   C5DDS2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   OrderedLocusNames=KLTH0C03344g {ECO:0000313|EMBL:CAR21933.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21933.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21933.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|PIRNR:PIRNR037299}.
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DR   EMBL; CU928167; CAR21933.1; -; Genomic_DNA.
DR   RefSeq; XP_002552371.1; XM_002552325.1.
DR   AlphaFoldDB; C5DDS2; -.
DR   STRING; 559295.C5DDS2; -.
DR   GeneID; 8291235; -.
DR   KEGG; lth:KLTH0C03344g; -.
DR   eggNOG; ENOG502QVQI; Eukaryota.
DR   HOGENOM; CLU_040459_0_0_1; -.
DR   InParanoid; C5DDS2; -.
DR   OMA; WNATANQ; -.
DR   OrthoDB; 337487at2759; -.
DR   Proteomes; UP000002036; Chromosome C.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProt.
DR   CDD; cd06923; ChtBD1_GH16; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR   PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..467
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002947794"
FT   DOMAIN          67..299
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          343..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
SQ   SEQUENCE   467 AA;  49866 MW;  50A61747606CA193 CRC64;
     MAGSKLFFLS AISALTSVVA AATTEKVVYC NETLAACPED KPCCSQYGVC GSGSYCLGGC
     NPRYSHNITA CMPMPVCKDF QTVFSNYSGD LQSQYTYLGD AEKHDWIYEG YTMDYDKEDA
     LVLAMPKNSG GTVLSSTRYV WYGKVGARLK TSHDAGVVTA FIMFSSVQDE IDYEYVGNNL
     TQVQTNYYFE GVQNWTHSTN VSTTDTFDNY HLYEVDWHED HIDWLIDGEV SRTLLKNSTF
     NATSGEYMFP QTPARIQISI WPGGNATNPV GTRSWAGGEI NWDSSDIQDY GYYYALLQGV
     NVTCYDPPAG TVKNGSVSYE YISSENFTQN YVAITNGTTV MGSADDTGYN PEDGKSSSSS
     SSSSSSSPAA SKSTQKGSSS TDKSSSTESG LKVATGSSSV SSAKQSGFVQ NINSASSSAT
     GKSSATSTGS SATSTGGAAG LSYAPISNNG LMHIAMGLFG AAFAFLY
//
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