y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si002128m |
Family | GT4 |
Protein Properties | Length: 339 Molecular Weight: 37959.1 Isoelectric Point: 10.0199 |
Chromosome | Chromosome/Scaffold: 5 Start: 4731938 End: 4734860 |
Description | UDP-Glycosyltransferase superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT4 | 136 | 301 | 3.3e-23 |
DLLFAIINSVSRGKGQDLFLQAFYQSLQLIQQQKLKVPTMHAVVVGSDMNAQTKFETQLRDFVVKNGIHERVHFVNKTLAVAPYLAAIDVLVQNSQARGE CFGRITIEAMAFKLPVLGTAAGGTTEIILDGLTGLLHPAGKEGVAPLAKNIVRLASHAEQRASMGK |
Full Sequence |
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Protein Sequence Length: 339 Download |
MVLPARGQEA VDTARKADLV VLNTAVAGKW LDPVLKDHVP EVLPKILWWI HEMRGHYFKL 60 EFVKHLPFVA GAMIDSHTTA EYWKSRTSDR LKIQMPQTYV VHLGNSKELM EVAEDNIARR 120 VLREHIRESL GVRSEDLLFA IINSVSRGKG QDLFLQAFYQ SLQLIQQQKL KVPTMHAVVV 180 GSDMNAQTKF ETQLRDFVVK NGIHERVHFV NKTLAVAPYL AAIDVLVQNS QARGECFGRI 240 TIEAMAFKLP VLGTAAGGTT EIILDGLTGL LHPAGKEGVA PLAKNIVRLA SHAEQRASMG 300 KKGYDRVRDR FMEHHMAERI AAVLKEVLKK SQEQHTRS* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0438 | RfaG | 8.0e-17 | 135 | 331 | 199 | + Glycosyltransferase [Cell envelope biogenesis, outer membrane] | ||
cd03795 | GT1_like_4 | 4.0e-18 | 171 | 317 | 151 | + This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes. | ||
cd03798 | GT1_wlbH_like | 4.0e-20 | 149 | 327 | 183 | + This family is most closely related to the GT1 family of glycosyltransferases. wlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS. | ||
cd03808 | GT1_cap1E_like | 1.0e-22 | 202 | 322 | 121 | + This family is most closely related to the GT1 family of glycosyltransferases. cap1E in Streptococcus pneumoniae is required for the synthesis of type 1 capsular polysaccharides. | ||
cd03801 | GT1_YqgM_like | 2.0e-25 | 48 | 325 | 280 | + This family is most closely related to the GT1 family of glycosyltransferases and named after YqgM in Bacillus licheniformis about which little is known. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. |
Gene Ontology | |
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GO Term | Description |
GO:0009058 | biosynthetic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI19755.1 | 0 | 2 | 338 | 128 | 463 | unnamed protein product [Vitis vinifera] |
GenBank | EAY73392.1 | 0 | 2 | 338 | 147 | 482 | hypothetical protein OsI_01273 [Oryza sativa Indica Group] |
RefSeq | NP_001042653.1 | 0 | 2 | 338 | 147 | 482 | Os01g0262600 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001130447.1 | 0 | 2 | 338 | 64 | 399 | hypothetical protein LOC100191545 [Zea mays] |
RefSeq | XP_002281084.1 | 0 | 2 | 332 | 144 | 474 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 2xa1_B | 0.0000000008 | 62 | 324 | 144 | 411 | A Chain A, Crystal Structure Of Trehalose Synthase Tret From P. Horikoshii (Seleno Derivative) |
PDB | 2xa1_A | 0.0000000008 | 62 | 324 | 144 | 411 | A Chain A, Crystal Structure Of Trehalose Synthase Tret From P. Horikoshii (Seleno Derivative) |
PDB | 2x6r_B | 0.0000000008 | 62 | 324 | 144 | 411 | A Chain A, Crystal Structure Of Trehalose Synthase Tret From P. Horikoshii (Seleno Derivative) |
PDB | 2x6r_A | 0.0000000008 | 62 | 324 | 144 | 411 | A Chain A, Crystal Structure Of Trehalose Synthase Tret From P. Horikoshii (Seleno Derivative) |
PDB | 2x6q_B | 0.0000000008 | 62 | 324 | 144 | 411 | A Chain A, Crystal Structure Of Trehalose Synthase Tret From P. Horikoshi |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO780896 | 330 | 4 | 333 | 0 |
HO805639 | 326 | 8 | 333 | 0 |
HO814265 | 299 | 34 | 332 | 0 |
EL684761 | 283 | 10 | 292 | 0 |
EL684785 | 283 | 10 | 292 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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