Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna30233.1-v1.0-hybrid |
Family | GH13 |
Protein Properties | Length: 1190 Molecular Weight: 134737 Isoelectric Point: 5.2202 |
Chromosome | Chromosome/Scaffold: 6 Start: 12554211 End: 12568767 |
Description | starch branching enzyme 2.2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 691 | 1011 | 1.1e-28 |
LPRIKKLGYNAVQLMAIQEHAYYASFGYHVTNFFAPSSRCGTPDDLKSLIDRAHELGLLVLMDIVHSHASNNTLDGLNMFDGTDSHYFHSGPRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLEEFKFDGFRFDGVTSMMYTHHGLQVAFTGNYSEYFGLATDVDAVTYLMLVNDLIHGLYPEAISIGEDVSGMPAFCIP VADGGVGFDYRLHMAIADKWIELLQKMDEYWQMGDIVHTLTNRRWGEKCVAYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPTIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 1190 Download |
MSDPKPRLVC CIGDIHGFHT KLQNLWSNLE SSTPSSDFAT ALIIFLGDYC DRGPETNKVL 60 DFLISLPSRY PRQKHVFIAG NHDFAFAAFL GVVPPPLDGS EFREGWREFE DNEEREGWFK 120 GEGYEGMHLQ GRRWAGRMTG FNKAKGTEYQ GSIYDAGPTF ESYGVPHGSA DLVKAVPDDH 180 KKFLANVVWV HEEDDVCVEI EGETKYYKLI AVHAGLEKDK DVKQQLEFLK ARDTRIPKIA 240 ALSGRKDVWN IPEELKNTPT VIVSGHHGKL HIEGLRLIID EGGGFAKNPV AAILLPSMKI 300 VHSANRDLDL ITNPTRKLKE EEEEEDGLDS LGDTLPSRPF RFQVLLAFQW RQSALHQPLP 360 VARQLLLFLS WDTMAFMLGV IPNMCLIRGK IFAGKSSYDS DSASSLTVAA SKKILVPGGP 420 SDGSPPLTEE LEAPDTDSED PQVLEDVDSV TMEDEKIEDE AISSLDVGSV DDETPSPLKA 480 TASTATKTIP PPGTGQKIYE IDPLLKGFRD HLDYRYGQYK RLREEIDKYE GGLEVFSRGY 540 EKFGFTRSAT GITYREWAPG AKSASLIGDF NNWNMNADVM TRNEFGVWEI FLPNNADGSP 600 AIPHGSRVKI RMDTPSGIKD SIPAWIKFSV QAPNEIPYNG IYYDPPEEEK YVFQHPQPNR 660 PQSLRIYEAH VGMSSTEPKI NSYAEFRDDV LPRIKKLGYN AVQLMAIQEH AYYASFGYHV 720 TNFFAPSSRC GTPDDLKSLI DRAHELGLLV LMDIVHSHAS NNTLDGLNMF DGTDSHYFHS 780 GPRGYHWMWD SRLFNYGSWE VLRYLLSNAR WWLEEFKFDG FRFDGVTSMM YTHHGLQVAF 840 TGNYSEYFGL ATDVDAVTYL MLVNDLIHGL YPEAISIGED VSGMPAFCIP VADGGVGFDY 900 RLHMAIADKW IELLQKMDEY WQMGDIVHTL TNRRWGEKCV AYAESHDQAL VGDKTIAFWL 960 MDKDMYDFMA LDRPSTPTID RGIALHKMIR LITMGLGGEG YLNFMGNEFG HPEWIDFPRG 1020 VQKLPNGKIV PGNNNSFDKC RRRFDLADAD YLRYHGLQEF DRAMHHLEET YSFMTSEHQY 1080 ISRKDEGDKV IVFERGNLVF VFNFHWSKSY SDYRVGCLKP GKYKIVLDSD ESIFGGFNRI 1140 DHTADYFTVD GWYDERPNSF QLYAPCRTAV VYALVESKET SKEKKPIKG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 6.0e-9 | 506 | 592 | 93 | + alpha-amylase | ||
cd07421 | MPP_Rhilphs | 3.0e-178 | 6 | 309 | 305 | + Rhilph phosphatases, metallophosphatase domain. Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination. | ||
PLN02447 | PLN02447 | 0 | 425 | 1187 | 767 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 647 | 1062 | 417 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic 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. | ||
PLN02960 | PLN02960 | 0 | 600 | 1175 | 580 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0016787 | hydrolase activity |
GO:0043169 | cation binding |
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 | 3amk_A | 0 | 498 | 1176 | 13 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 498 | 1176 | 13 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 498 | 1176 | 13 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 498 | 1176 | 13 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3k1d_A | 0 | 492 | 1170 | 88 | 717 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
Sequence Alignments (This image is cropped. Click for full image.) |
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