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Database: UniProt
Entry: A0A0C4E9R3_MAGP6
LinkDB: A0A0C4E9R3_MAGP6
Original site: A0A0C4E9R3_MAGP6 
ID   A0A0C4E9R3_MAGP6        Unreviewed;       592 AA.
AC   A0A0C4E9R3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:KLU90835.1};
GN   ORFNames=MAPG_09361 {ECO:0000313|EMBL:KLU90835.1};
OS   Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS   fungus) (Magnaporthe poae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX   NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_09361T0, ECO:0000313|Proteomes:UP000011715};
RN   [1] {ECO:0000313|Proteomes:UP000011715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KLU90835.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU90835.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KLU90835.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU90835.1};
RA   Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of Magnaporthe poae ATCC 64411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblFungi:MAPG_09361T0}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_09361T0};
RX   PubMed=26416668; DOI=10.1534/g3.115.020057;
RA   Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA   Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA   Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA   Ma L.-J., Dean R.A.;
RT   "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT   family of fungi.";
RL   G3 (Bethesda) 5:2539-2545(2015).
RN   [5] {ECO:0000313|EnsemblFungi:MAPG_09361T0}
RP   IDENTIFICATION.
RC   STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_09361T0};
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; ADBL01002393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL876976; KLU90835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C4E9R3; -.
DR   STRING; 644358.A0A0C4E9R3; -.
DR   EnsemblFungi; MAPG_09361T0; MAPG_09361T0; MAPG_09361.
DR   VEuPathDB; FungiDB:MAPG_09361; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   OMA; PNGEKWA; -.
DR   OrthoDB; 3680211at2759; -.
DR   Proteomes; UP000011715; Unassembled WGS sequence.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011715}.
FT   DOMAIN          22..447
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   592 AA;  66911 MW;  7C6CFFF08B485C98 CRC64;
     MADLGLSHAH SKKWWKEAVV YQVYPSSFKD TNGDGVGDLP GIIEKLDHIQ SLGATVIWVC
     PMYDSPQVDL GYDIRDYEKV YPPYGTMQDM QNLIDSCHAR GMRIILDLVI NHTSDQHAWF
     QESRASKASP KRDWYIWRPA RRGPAGERLP PNNWRSNFGS SVWTWDDASQ EYYLHLFAPE
     QPDLNWENAE TRRAIYASAM ESWLRRGVDG FRVDTVNMYS KAPGLPDAPV VNPAQEWQFA
     AGQFCNGPRM FEYLDEMNKV MEGYDTMTVG ELPHTPDLGR VLKYVSAAEK KLDMVFQFDV
     VDTGFGKDVK YDTTPFNWTL PEFKRRVLRT QSLISGTDAW TTSFLENHDQ ARSISRFASD
     VPEHRVQSGK LLCLLSCTLS GTLFVYQGQE IGMVNMSKDW PMDEYKDIES GNYYREVQAK
     VAGTPDEASA MAAAKASLQH LARDHARVPM CWDDSPQGGF STNPATWMRT HHLAGEINVA
     FQTGDPASVL GFWRKTLRLR REYADVLVYG DFEIDDIEDP STFVYTKSNG AETALVMLNF
     TAVHVDAKVP TRLAGASFQL VASTYEDTGT DDGLGKLRPF EGRFYVAQSG LK
//
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