CAZyme Information: mRNA_M_BR32_EuGene_00110691-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00110691-p1
• CAZy Family: GH47
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
535	BR32_scaffold00016|CGC4	59793.56	6.5017

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PoryzaeBR32	14781	N/A	432	14349

• Gene Location: location=BR32_scaffold00016:205916-207936(+)

Full Sequence      

MHPPAPRNGHQPHHPNGDATSNGHPAPNMEQVYVVPDHGPCPPNRTLFEAFEWYLPAQQN
HWRRLADRIPSLAALGVTDLWIPPACKGAWYTSNGYDVYDLYDLGEFDQRGARQTKWGSK
EELLRLVDVANRHGVGVLFDAVLNHMTGADETERVLAVNVDPNDRRQEISTPHQIEAWTK
FNFPGRGDTYSPLRWTAEHFTGVDYDQASKTNGIWKFLGKEWAPDVDGEFGNYDFLMCTD
IDHSHPEVRRNFFHWVQWLASQMRLGGLRLDAVKHISASFMRDFVGLVQNTVGRDWLLLG
EYWSGDVKALLGYLEQLDHRISLVDVPLVESFSRISRGEQPDLRRVFENTLAATKPNNAV
QTGQTLETPVEPFFIPIAYALILLRANHGTPCVFWCDLYGTLLPSRPGPAPLGGLLTARL
MLARKLWAYGTEAAYFCGKGAETCVGFTRFGHPARSGGAGLAVVANTGFERAARRMCVGS
RHAGERWTDLLRQVWGVVVVDAAGYAEFPVGPRGVSVWVHEMAEGRDVVEGLTSL

Enzyme Prediction     

EC	3.2.1.1:2	3.2.1.116:1	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	72	401	5e-122	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	44	426	1	391	Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
236518	PRK09441	0.0	44	519	3	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	1.02e-36	47	399	2	276	Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
223443	AmyA	1.15e-21	62	400	28	321	Glycosidase [Carbohydrate transport and metabolism].
214758	Aamy	2.03e-20	46	148	2	97	Alpha-amylase domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QBZ66474.1|GH13_5	0.0	1	535	1	543
QBZ65510.1|GH13_5	6.76e-195	36	519	26	510
EAQ71557.1|GH13_5	6.78e-194	36	518	26	509
AEO58507.1|GH13_5	8.27e-182	69	530	1	466
VBB80949.1|GH13_5	1.02e-180	32	532	53	573

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4UZU_A	2.08e-127	41	534	2	494	Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]
1BLI_A	1.29e-126	44	519	4	481	Bacillus Licheniformis Alpha-Amylase [Bacillus licheniformis]
1VJS_A	1.64e-124	44	519	4	481	Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
1OB0_A	6.55e-124	44	519	4	481	Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface [Bacillus licheniformis]
1HVX_A	8.90e-124	41	519	2	481	BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06278|AMY_BACLI	7.41e-124	44	519	33	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P06279|AMY_GEOSE	2.58e-122	36	519	31	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P19571|AMT6_BACS7	2.82e-119	44	521	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P00692|AMY_BACAM	1.97e-115	44	521	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P26613|AMY2_SALTY	1.27e-104	44	521	3	492	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000001

TMHMM  Annotations     

There is no transmembrane helices in mRNA_M_BR32_EuGene_00110691-p1.