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Database: UniProt/TrEMBL
Entry: K5W345_PHACS
LinkDB: K5W345_PHACS
Original site: K5W345_PHACS 
ID   K5W345_PHACS            Unreviewed;       577 AA.
AC   K5W345;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   18-JUL-2018, entry version 30.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=PHACADRAFT_259591 {ECO:0000313|EMBL:EKM53319.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus)
OS   (Peniophora carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM53319.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM53319.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM53319.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa
RT   and P. chrysosporium, to elucidate the genetic basis of the distinct
RT   wood types they colonize.";
RL   BMC Genomics 13:444-444(2012).
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:RU003615}.
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DR   EMBL; JH930474; EKM53319.1; -; Genomic_DNA.
DR   RefSeq; XP_007398011.1; XM_007397949.1.
DR   EnsemblFungi; EKM53319; EKM53319; PHACADRAFT_259591.
DR   GeneID; 18917463; -.
DR   KEGG; pco:PHACADRAFT_259591; -.
DR   InParanoid; K5W345; -.
DR   OrthoDB; EOG092C1YBX; -.
DR   Proteomes; UP000008370; 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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
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; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008370};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134,
KW   ECO:0000313|EMBL:EKM53319.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    577       Alpha-amylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003885279.
FT   DOMAIN      477    577       CBM20. {ECO:0000259|PROSITE:PS51166}.
SQ   SEQUENCE   577 AA;  61621 MW;  4759E3247F762FC2 CRC64;
     MARSSLACLL ISLLTFVAGS TSSPAQFPVQ APEALKNVIV QMFEWTWDSV AAECYNFIGP
     AGYGFVQVSP AQEHVQGSQW WTDYQPVSYT LTSKRGDRDQ YTNMINTCHA AGVGVIADTL
     LNHMSGSDDG GVGVGGSSFQ HYVYPGIYEY QDFHHCGLEP DDNIVDYSNA VEVQTCQLDN
     LADLFTESEY VRSRLAAYVN DLLSLGVDGL RLDAAKHINA NDIANITSRL RRAPYITQEV
     IFGTGEPITP IQYVNIGDVQ EFRYTTAVQN AFSGSGISGL QSFDNLGWVP GTSANVFVSN
     HDTERNGNSL NANSPSNIYV TAMVFSLAHP YGMPTILSSY SDFTDYDAGA PNGGAGTCTT
     GGGTNGWLCQ HRWNAIAGMV GFHNQVGTAA MNNWVSPQSE QIAFGRGSLG FVAINNADAV
     WTTTFATSLP DGTYCDVISG ISSSGVCTGT AFTVSDGKFT AGVQARNAIA IHSGATGTAG
     ATITVNFAEN ANTTWGENIF LVGSVPQLGS WSPNSALPLS PASYPTWTVS VSLPPNTAFE
     YKFIRKETNG TVVWESDPNR SATTPGSGSL DLTESWR
//
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