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Database: UniProt
Entry: G8BI19_CANPC
LinkDB: G8BI19_CANPC
Original site: G8BI19_CANPC 
ID   G8BI19_CANPC            Unreviewed;       490 AA.
AC   G8BI19;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Glycosidase {ECO:0000256|PIRNR:PIRNR037299};
DE            EC=3.2.-.- {ECO:0000256|PIRNR:PIRNR037299};
GN   Name=CRH11 {ECO:0000313|CGD:CAL0000156447};
GN   OrderedLocusNames=CPAR2_400860 {ECO:0000313|CGD:CAL0000156447,
GN   ECO:0000313|EMBL:CCE44284.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE44284.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC       subfamily. {ECO:0000256|ARBA:ARBA00038074}.
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DR   EMBL; HE605208; CCE44284.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8BI19; -.
DR   STRING; 578454.G8BI19; -.
DR   EnsemblFungi; CPAR2_400860-T; CPAR2_400860-T-p1; CPAR2_400860.
DR   CGD; CAL0000156447; CRH11.
DR   VEuPathDB; FungiDB:CPAR2_400860; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 4.
DR   GO; GO:0009986; C:cell surface; IDA:CGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
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; cd02183; GH16_fungal_CRH1_transglycosylase; 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:SF27; GLYCOSIDASE CRH1-RELATED; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037299-2};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037299};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037299};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..490
FT                   /note="Glycosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003508567"
FT   DOMAIN          30..237
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          284..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        121
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-1"
FT   DISULFID        26..34
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037299-2"
SQ   SEQUENCE   490 AA;  51869 MW;  12EA5B58C36E1959 CRC64;
     MLISRAFSLA SILITTVSAA TSTASCNPIK SSSCSPNPAL GGSMQENFQN GLGSYFTNSG
     NQGDVKTGDE GLSLTVNKRF DNPSIHSDFY LMFGYVEVEL KAGEGKGIVS SFFLQSDDLD
     EIDIELFGGD EYEWQSNYFV QGNTSTYDRG GYHSINPSPL TNYHKYAINW TKDSLDWIVD
     GSVIRSLHIT NSQGYPQSPM RIYAGIWAGG DPSNEEGTIL WAGGETDYSQ APFTMHIKSI
     TAIDYSTGSE YSYSDQSGYW QSIDAKDGEV NGRYSDAQSD VNKAVNGDSI ENSGSSDSPS
     TTQSSSESSS TTESSSESSS TTESSSESSS TTESSSESSS TTESSSESSS TTESSSESSS
     TTESSSESSS TTENSSSFSE STQESQSSSE PNSSASSAET TETSESTQTT RGGANKVETD
     ASSFSSSVAT TSAETDSSEQ ETTTSSSSSS DETHSVSSSS ENSACRFTSP RSMQFVTVLV
     SFVSFGFVLV
//
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