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Database: UniProt
Entry: H1VGF9_COLHI
LinkDB: H1VGF9_COLHI
Original site: H1VGF9_COLHI 
ID   H1VGF9_COLHI            Unreviewed;      1009 AA.
AC   H1VGF9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE            EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
GN   ORFNames=CH063_10175 {ECO:0000313|EMBL:CCF39312.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF39312.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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}.
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DR   EMBL; CACQ02003427; CCF39312.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1VGF9; -.
DR   STRING; 759273.H1VGF9; -.
DR   EnsemblFungi; CCF39312; CCF39312; CH063_10175.
DR   VEuPathDB; FungiDB:CH63R_06054; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   HOGENOM; CLU_000631_11_0_1; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CCF39312.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1009
FT                   /note="alpha-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003555986"
FT   DOMAIN          341..777
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          785..878
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
SQ   SEQUENCE   1009 AA;  110096 MW;  AED6075C1974BF68 CRC64;
     MFARAPLLLP AAAVMALCTM ARVADLGRPS APQYLASTSI ASSTSQFTVP ASANEGALLI
     PNIEDPESTD PQSVCPGYTA SHIQTTSYGF TADLDLAGSA CNVYGNDVEA LSLVVEYLAT
     DRLHVQVLPR YIGTRNSTWF ILPGELIPKP AADGKASSDG SNSDLEFKWA NEPTFGFNVS
     RKSTGDVLFT TAGTKLVFED QFFEFASPLP KNYNLYGLGE VIHGFKLNNN LTRTLYAADV
     GDPIDGNIYG SHPVYLDTRY YQVNSDTKEA VYVANATDKN AEYTSYTHGV FLRNSHAQEV
     LLRESNITWR GLGGTIDLYF YAGPTADAVM KSYQKTTVGL PAMQQYWTFG FHQCRWGYTS
     WDNLQEVTDD FAKFKIPLET IWADIDYMNQ YRDFENDANS WSYEDAARVL GSLHKNGQHF
     VPIVDSAIYS PNSENASDAY PTYDRGADAD AFMLNPDGSL YIGAVWPGYT VFPDWIGAVL
     NGSRTFEWWK TELVTWFDKV AFDGIWIDMS EVSSFCVGSC GSDNLTLNPA HPPFLLPGEP
     GNEVLEYPEG FDRTNGTEAA SVSSLSSSLA AARTATAAIP SSSLYTTTSY LRTTPTPGVR
     NVNYPPYVIN NIQGDLAVHA VSPNATHHGG TQEYDFHNLF GHQILNATYQ ALLSVLPGKR
     PFIIGRSTFA GSGKWAGHWG GDNASLWAYM FFSIPQALAF SIFGVPMFGV DTCGFSGNTD
     MELCARWMQL SAFFPFYRNH NVIGAIPQEP YRWAAVADAS RAAMAIRYAL LPYVYTAFYR
     AHKQGDTVMK ALAWEFADEP WLAGADRQFL LGPAVMVTPC LEQGASTVDG VFPGVGQGTV
     WYDWYNQSAI TGVSTGQNVT IDAPLGHIPV YVRGGYVIPT QEPGLTTAES RSNPWGLLVA
     LDDKGTAKGS LYVDDGESVE QEATLTVELS ASENSLKATP SGEFRDSNSL GTVTVMGVQG
     DVSAVTLDGR DLDSASWTFN STTRALHIHG LKSRTSEGAW SSARELVWS
//
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