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
//