ID C4YD16_CANAW Unreviewed; 946 AA.
AC C4YD16;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Glucoamylase 1 {ECO:0000313|EMBL:EEQ42202.1};
GN ORFNames=CAWG_00404 {ECO:0000313|EMBL:EEQ42202.1};
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ42202.1, ECO:0000313|Proteomes:UP000001429};
RN [1] {ECO:0000313|EMBL:EEQ42202.1, ECO:0000313|Proteomes:UP000001429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1 {ECO:0000313|EMBL:EEQ42202.1,
RC ECO:0000313|Proteomes:UP000001429};
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).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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; CH672346; EEQ42202.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YD16; -.
DR PaxDb; 5476-C4YD16; -.
DR VEuPathDB; FungiDB:CAWG_00404; -.
DR HOGENOM; CLU_000631_11_0_1; -.
DR OMA; PYVINHD; -.
DR Proteomes; UP000001429; Chromosome 1, Supercontig 1.1.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..946
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002946539"
FT DOMAIN 299..723
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 731..821
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
FT REGION 520..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 946 AA; 105778 MW; 05A4E6418FB5CAD4 CRC64;
MKLLSKFIVT ALGLTSIVNA APTSSSSAEE AQKTVPVELS IGVKQLPNIH NDSAVDANAV
AKGYSLVNVS LTARGLTGIL KLKEATNIYG YDFEYLNLSV EYQSDTRLNV HIEPTDLTDV
FVLPEELVVK PKLEGDAKTF NFENSDLVFE YDEEDFGFEV LRSSTREVLF STKGNPLVFS
NQFIQFNTTL PKGHSITGLG ESIHGSLNEP GVVKTLYAND IADPIDGNIY GVHPVYYDQR
YNTNTTHAVY WRTSAIQEVV VGETSLTWRA LSGVIDLYFF SGPDPKDVIQ QYVSEIGLPA
MQPYWALGYH QCRWGYDTVE SLETVVENFK KFDIPLETIW SDIDYMDGYK DFTNDPYRFP
TDKFRKFLDD LHNNSQHYVP IFDAAIYVPN PNNATDDDYE PFHLGNESDV FLKNPDGSLY
IGAVWPGYTV FPDFLANNTQ EYWNKMFKDW YERIPFDGIW TDMNEVSSFC VGSCGTDRYF
DNPVHPPFEV GYSGSDYPLG FDKSNASEWK SISEAAAATK TTTTTSSSAS TSIDGKNTLA
PGKGNINYPP YAINNDQGDH DLATHAISPN ATHADGTVEY DIHNIYGLIQ ERAIYEALLE
IHPNKRPFII GRSSFAGSGK YMGHWGGDNY ADYYMMYFSI PQALSMGLSG IPFFGVDACG
FNGNTDMELC SRWMQLASFF PFYRNHNVLG AIPQEPYVWE AVMKATKTSI NVRYSLLPYY
YTLLHESHVT GIPIMRAFNW QFPYSKELAG VDTQFFVGDA LLVTPVLEPG VNHTKGIFPG
ENAVYYDFYT HKKQKFTAGK NETLAAPLGH IPLHIKGGNI IPTQEPGYTT TESRKNPFGL
LVALDAEGTA SGKLYLDDGE SVDVEEALYV DFVASKNKLV ASVFGEYEAS QPLANVTILG
VDSEPKKVLF NNETVSHKYE NDAVYLTDLE KFTKEGAFAE EFSIQW
//
