y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_004613m |
Family | CBM45 |
Protein Properties | Length: 566 Molecular Weight: 63879.9 Isoelectric Point: 7.0323 |
Chromosome | Chromosome/Scaffold: 11495 Start: 471330 End: 475879 |
Description | alpha-amylase-like 3 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 310 | 386 | 6.4e-23 |
LHWGVCRNDAKNWEIPAGPYPSETTVFKDKALRTLLQPTDGGNGCSGLFTIDQEFVGFLFVLKLNEKTWLKCKENDF | |||
CBM45 | 121 | 204 | 1.4e-29 |
LHWGVSYVDDVGSEWDQPPKNMRPPGSVPIKDYAIETPLKKSSEEEIFHEVKINFDPKSSIAAINFVLKDEETGAWYQHRGRDF |
Full Sequence |
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Protein Sequence Length: 566 Download |
MSTISIEPLL RYSRRETPLC RCRTKMLMPF SLNFSPKLLF NGATTSFCNF KPQHFLTIQA 60 SSTDSALLET FKSTDVFFKE IFPLTRTQTV EGKIFIRLDK GENQQRWQLS VGCSLPGKWI 120 LHWGVSYVDD VGSEWDQPPK NMRPPGSVPI KDYAIETPLK KSSEEEIFHE VKINFDPKSS 180 IAAINFVLKD EETGAWYQHR GRDFKVPLVD YLLNDSNVVG AKRGFNIWPG AFLRKMLLKA 240 KELPSKDQES SSGSKDVKQE SRQVEGFYEE QPITKQVVIQ NLITVSVTKC PKTAKNLLYL 300 ETDISGEVVL HWGVCRNDAK NWEIPAGPYP SETTVFKDKA LRTLLQPTDG GNGCSGLFTI 360 DQEFVGFLFV LKLNEKTWLK CKENDFHIPL SSSSSMHAQP GQGQYEGQLV SEKTLEENQA 420 VPRTPHSKGI INEMRNLVSD ISSSRKTKTK EAQEGILHEI EKLAAEAYSM FRSSIPTLTL 480 TEKAVSESEP PETPKICSGT GTGFEILFQG FNWESHKSGR WYMELKEKVL EISSLGFTVI 540 WLPPPTESVS PEGYMPKDLY NLNSR* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00642 | Aamy | 3.0e-8 | 505 | 565 | 65 | + Alpha-amylase domain. | ||
PLN00196 | PLN00196 | 3.0e-16 | 505 | 564 | 61 | + alpha-amylase; Provisional | ||
PLN02361 | PLN02361 | 2.0e-23 | 503 | 564 | 62 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-25 | 506 | 565 | 62 | + 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. | ||
PLN02784 | PLN02784 | 0 | 1 | 565 | 574 | + alpha-amylase |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAX33231.1 | 0 | 1 | 565 | 1 | 570 | plastid alpha-amylase [Malus x domestica] |
EMBL | CAN69906.1 | 0 | 1 | 565 | 1 | 549 | hypothetical protein [Vitis vinifera] |
EMBL | CBI32016.1 | 0 | 1 | 565 | 1 | 554 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 565 | 1 | 570 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 565 | 1 | 570 | alpha-amylase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3bsh_A | 0.00000000000003 | 505 | 564 | 2 | 62 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
PDB | 3bsg_A | 0.00000000000003 | 505 | 564 | 2 | 62 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0.00000000000003 | 505 | 564 | 2 | 62 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0.00000000000003 | 505 | 564 | 2 | 62 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0.00000000000003 | 505 | 564 | 2 | 62 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 577 | 1 | 565 | 0 |
HO782468 | 237 | 85 | 316 | 0 |
HO782468 | 245 | 317 | 547 | 0 |
HO782468 | 74 | 135 | 208 | 0.007 |
HO782468 | 49 | 77 | 125 | 0.007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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