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Database: UniProt/TrEMBL
Entry: R8BEZ8_TOGMI
LinkDB: R8BEZ8_TOGMI
Original site: R8BEZ8_TOGMI 
ID   R8BEZ8_TOGMI            Unreviewed;       461 AA.
AC   R8BEZ8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   20-JUN-2018, entry version 28.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=UCRPA7_6639 {ECO:0000313|EMBL:EON97874.1};
OS   Togninia minima (strain UCR-PA7) (Esca disease fungus)
OS   (Phaeoacremonium aleophilum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Togniniales; Togniniaceae;
OC   Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EON97874.1, ECO:0000313|Proteomes:UP000014074};
RN   [1] {ECO:0000313|Proteomes:UP000014074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-PA7 {ECO:0000313|Proteomes:UP000014074};
RX   PubMed=23814032; DOI=10.1128/genomeA.00390-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of the ascomycete Phaeoacremonium aleophilum
RT   strain UCR-PA7, a causal agent of the esca disease complex in
RT   grapevines.";
RL   Genome Announc. 1:E0039013-E0039013(2013).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000256|RuleBase:RU361134}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|RuleBase:RU361134}.
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DR   EMBL; KB933248; EON97874.1; -; Genomic_DNA.
DR   RefSeq; XP_007917367.1; XM_007919176.1.
DR   EnsemblFungi; EON97874; EON97874; UCRPA7_6639.
DR   GeneID; 19327316; -.
DR   KEGG; tmn:UCRPA7_6639; -.
DR   OrthoDB; EOG092C1YBX; -.
DR   Proteomes; UP000014074; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000014074};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014074};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    461       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004452570.
FT   DOMAIN       37    374       Aamy. {ECO:0000259|SMART:SM00642}.
FT   DOMAIN      383    459       Aamy_C. {ECO:0000259|SMART:SM00632}.
SQ   SEQUENCE   461 AA;  49993 MW;  EF376104B584AB81 CRC64;
     MPRTITAGLN AVVALIAAGL TAMAPPVVHA APPGTKDVTA VLFEWNFDSV ARECTQTLGP
     AGYGYVQVSP PAEHIQGSQW WTSYQPVSYQ IAGRLGNRAS FVNMVNTCHG AGVKVIADAV
     INHMSSGSGT GTGGSSYTKY NYPGLYSSYD FDDCTSDINN YGDRWNVQHC ELVGLADLDT
     PEEYPRKAIS GYLNDLLSLG VDGFRIDAAK HMATEDLANI KSRLTNPSTY WKQEVIYGSG
     EAVQPTEYTG NGDVQEFRYA YDLKRVLNSE KLAYLKNYGE GWGYLGNSVA AVFVDNHDTE
     RNGATLNYKD NAKYTLANVF MLAYPYGATD IHSGYEFSDT DAGPPNNGAV SACWQDGWKC
     QHAWPEILRM VAFRNAVRGQ GLTDWWDNGN NAIGFGRGDK GYVAINHESG SVTRTYQTSL
     PAGTYCNVQS NTYVTVDSSG QFTATLGSDI ALAIYAGKTS C
//
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