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Database: UniProt
Entry: A0A0F8VVW5_9EURO
LinkDB: A0A0F8VVW5_9EURO
Original site: A0A0F8VVW5_9EURO 
ID   A0A0F8VVW5_9EURO        Unreviewed;       992 AA.
AC   A0A0F8VVW5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
GN   ORFNames=ARAM_002293 {ECO:0000313|EMBL:KKK27386.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK27386.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK27386.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK27386.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC         glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00001657};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKK27386.1}.
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DR   EMBL; JZBS01000003; KKK27386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8VVW5; -.
DR   STRING; 308745.A0A0F8VVW5; -.
DR   OrthoDB; 5486960at2759; -.
DR   Proteomes; UP000034291; 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   CDD; cd06595; GH31_u1; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
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:SF89; ALPHA-XYLOSIDASE; 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          378..680
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          690..781
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   992 AA;  113431 MW;  A88A81DFAC96838D CRC64;
     MEFKIEPVVP ADAEEVTDVF LASFSDDFSR RLFPCTEDVR AWWIQKFAAD AEQAHSQHTV
     SFMKMVGTVG SDQRPVIAAF ALWELPKKAP VGEGTEDEHV TWPVGSDSEL CDLFFEGIHK
     ERKSAVKGQP HYYLSMLGTH PSFGRRGLSG RLLKWGLDRA DEEKMEVFIS ASPPGRGFAW
     NSQVVMDKYK FPTHPTPSPG ATVQGPTYRF TLLTDRLIRY EWAEHGQFED RASTFAINRE
     FPVPEFRWVD GEDLEIITEH FHMSYTKKKF SPESLGFQFN GKSVKYGTPW RFGTPVEFNL
     GGTARTLDQV NGRCDMGQGV LSKAGFAVID DSKSMLFDGN GWVAERLPGE RFDGYLFCYG
     RDYKAAMKAF YALSGKQPIL PRYVFGNWWS RYYAYHQDEY IQLIDAFNQH RIPLSVAVVD
     MDWHYVSDDR VPHAGWTGYT WNPSLFPDPG RFRRELNERS LKITLNDHPH SGVYPYEDAY
     KEMSRFLGRD PDEKNPIMFD PANPKFMEAY LEILHRRLER QACDFWWIDW QQGPYSKIPG
     LDPLWLLNHF QYLDSGLDGK TALVFSRFAG PGSHRYPVGF SGDTIVSWAS LAFQPEFTAT
     ASNIGYGWWS HDIGGHIFGG RDDELFARWV QLGVFSPIMR LHSTTSHWMS KEPWLYGQEC
     DSVVSIYMRF RHQLIPYLYT HNVISSIEDE PLVQPLYWRY PYHKKAYEFP NQYFFGQKLM
     VAPIVQPRDP CTHLASVQAW LPPDKRYVDI FTGTVYDGDR ELTFFRPLEG YPVLAHEGSI
     ITLDDDCTGV QNGCFNPDVM QVLVVVGADG QACTVEDPRD SKSQKRDQAV DSEVRQYQLK
     YSQSEGRLTA AGVNGHWRFL FLTLTSIPPD LKVYIDGTNR TEDSTFSIQE FPQTPGLLVS
     CPGDYSVQYS IDVELGPNPQ LDVRDHGPYL ERLIMQYQTD FAVKDRLWKA ISGHKLRPTS
     TTITTLLSFG YDEAVVGPII ELISADSRIG AC
//
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