ID G8B697_CANPC Unreviewed; 904 AA.
AC G8B697;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Glycoside hydrolase family 5 C-terminal domain-containing protein {ECO:0000259|Pfam:PF18564};
GN OrderedLocusNames=CPAR2_100160 {ECO:0000313|CGD:CAL0000153047,
GN ECO:0000313|EMBL:CCE39978.1};
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:CCE39978.1, 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 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE605203; CCE39978.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B697; -.
DR STRING; 578454.G8B697; -.
DR EnsemblFungi; CPAR2_100160-T; CPAR2_100160-T-p1; CPAR2_100160.
DR CGD; CAL0000153047; CPAR2_100160.
DR VEuPathDB; FungiDB:CPAR2_100160; -.
DR eggNOG; ENOG502QPU8; Eukaryota.
DR Proteomes; UP000005221; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0050295; F:steryl-beta-glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1904462; P:ergosteryl 3-beta-D-glucoside catabolic process; IEA:EnsemblFungi.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR041036; GH5_C.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31308; -; 1.
DR PANTHER; PTHR31308:SF5; ERGOSTERYL-BETA-GLUCOSIDASE; 1.
DR Pfam; PF18564; Glyco_hydro_5_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT DOMAIN 779..858
FT /note="Glycoside hydrolase family 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18564"
FT REGION 674..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..710
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 102803 MW; E32BF9309DD76D78 CRC64;
MFISDALKSA RYAQDAVNEK IRLYSTASSI SPVGVKPLRR SYSISEPIQD AANSGSSILE
CVPLETDKKG NFYDPSTGRI VVLKGINVDA QMKLPTEPYM PSYKGDSTNP DDIFFEGDTV
SFVGRPFPLE EARSHFERIK SWGYNTIRYL LTWEAVEHEG PGKYDQKFAD YTLEMLKIIG
QVGGLYVFLE FHQDVWSRFS GGSGAPMWTF YAAGLDPKKF TLADSAIIHN EPRFRDGTDT
YHKMLWTSNY KRLAPLVMFT MFFAGKYYFP NLIMNGENIQ DFLQNHFLGA VEFIWKQVCE
GVPELINNGT VLGFESMNEP NCGLIGYPDI SQLPDFQQLR VGTTPTAFQS MRLGMGFACE
VDEYRITVTG PRKYGTKIVD PKGTRAWLTP EDAKDIDKNY GFERGEKWEL GTCIFATQGI
WSWPSVARDM ATMTQEQRLD ISSKCKVLEP HFFSKSLPQH KYESDVTKVD THTFVNLHFV
DHIVKFKKLI RKYRSDAFVM LSTPVLEEPP HLKNDKRNVI DDRIIYCPHY YDGLSLMHKS
WNFKFNVDTL GIMRGAYLNP VLGIVFGGRA IRNCFQKQFC EMRRECNEYL GKLPILMSET
GMPFDMDDKR SYRNGKYISQ TAALDALCNA LESANMSHTF WCYDSCNNHK YGDNWNNEDF
SFWSSDDRNL TFEDECETPE IRNETESERN RVKTARAIRK ANRKLKRAAK MGRSGSVDST
ASTTSATSGS STDGYTDMES DSTSSSSVIS STSSNIYRRQ YGKCYPSPDG VRAAGAVIRP
YMMASLGTMV ATEFDVKAVK LSLQIVVDKS DPRVENTPTI IFVPKWHFPF LDYGDVFLTS
GYIKYNEELQ YIEWYHCNDP SLNIKEESTT NEKTSTETII IKNNSGSLED AKTIEDRKLG
CTIS
//
