ID A0A1X6ML84_9APHY Unreviewed; 501 AA.
AC A0A1X6ML84;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Glycoside hydrolase family 1 protein {ECO:0000313|EMBL:OSX56833.1};
GN ORFNames=POSPLADRAFT_1186390 {ECO:0000313|EMBL:OSX56833.1};
OS Postia placenta MAD-698-R-SB12.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=670580 {ECO:0000313|EMBL:OSX56833.1, ECO:0000313|Proteomes:UP000194127};
RN [1] {ECO:0000313|EMBL:OSX56833.1, ECO:0000313|Proteomes:UP000194127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAD-698-R-SB12 {ECO:0000313|EMBL:OSX56833.1,
RC ECO:0000313|Proteomes:UP000194127};
RG DOE Joint Genome Institute;
RA Gaskell J., Kersten P., Larrondo L.F., Canessa P., Martinez D., Hibbett D.,
RA Schmoll M., Kubicek C.P., Martinez A.T., Yadav J., Master E.,
RA Magnuson J.K., James T., Yaver D., Berka R., Labutti K., Lipzen A.,
RA Aerts A., Barry K., Henrissat B., Blanchette R., Grigoriev I., Cullen D.;
RT "Genome Sequence of the Model Brown-Rot Fungus Postia placenta SB12.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family.
CC {ECO:0000256|RuleBase:RU003690}.
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DR EMBL; KZ110611; OSX56833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6ML84; -.
DR STRING; 670580.A0A1X6ML84; -.
DR OrthoDB; 3373839at2759; -.
DR Proteomes; UP000194127; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU004468};
KW Hydrolase {ECO:0000256|RuleBase:RU004468, ECO:0000313|EMBL:OSX56833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194127}.
FT ACT_SITE 375
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10055"
SQ SEQUENCE 501 AA; 56806 MW; 9F3EF43BA376F1DB CRC64;
MANKISSRLP KDFLWGFATA SFQIEGSTQV DGRGKSIWDD FSKKPGKTLD GRDGDVATDS
YRLWKDDLDL LVSYGVKSYR FSIAWSRIIP LGGRNDPVNE AGIRFYSNLI DNLLARGIIP
FVTLYHWDLP QGLEDRYGGW LNKEEIVKDY VNYAKICFER FGNRVKNWLT FNEPWCISVH
GYGHGVFAPG RSSDRTRCPE GDTSTEPWLV GHNVILAHAY ASKLYREEFK QAQGGQIGIT
LNGDWALPYD DSPESASRGS DADLLTFADP IYLGHYPEYL KEMLGSRLPT FTAEELHVVK
GSSEFYGMNT YTTNLCMAGG DNEFQGKVKY TFTRPDGTQL GTQAHCAWLQ DYAPGFRQLL
NYLYKRYRKP IYVTENGFAV KDENNKPVEE ALSDYDRVHY FQGTTSSLLS AVVEDGVDIR
GYFAWSLMDN FEWADGYVTR FGVTYVDYET QKRYPKDSAR FVCQWFKENI EKDESSESAA
GPSAPVSKLA DDAHLIDAVR A
//