Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000274007 |
Family | GT2 |
Protein Properties | Length: 315 Molecular Weight: 35444.4 Isoelectric Point: 10.0282 |
Chromosome | Chromosome/Scaffold: 005267153 Start: 13174 End: 15497 |
Description | Nucleotide-diphospho-sugar transferases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT2 | 71 | 266 | 6.8e-32 |
SLIIPAFNEELRLPGALDETMNYLQQRAVKDKSFTYEVVIVDDGSVDGTKRVAFEFIKKYTVDTMRIILLGRNHGKGEAIRKGMLHSRGELLLMLDADGA TKVNDVEKLEKQIHEVAKQDKFRDSSAGNSSFRISDIPIAAFGSRAHLEGKALATRKWYRNFLMKGFHLVVLLAAGPGIRDTQCGFKMFTRAAARK |
Full Sequence |
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Protein Sequence Length: 315 Download |
MEFVIVWTMV ELLLALILVV ATGLASAVFF EAYRRKNNNA HVGAPAIFED PNSLKQVPCP 60 SIFDTAEKYL SLIIPAFNEE LRLPGALDET MNYLQQRAVK DKSFTYEVVI VDDGSVDGTK 120 RVAFEFIKKY TVDTMRIILL GRNHGKGEAI RKGMLHSRGE LLLMLDADGA TKVNDVEKLE 180 KQIHEVAKQD KFRDSSAGNS SFRISDIPIA AFGSRAHLEG KALATRKWYR NFLMKGFHLV 240 VLLAAGPGIR DTQCGFKMFT RAAARKIFTN IRLNSLCCLE VWKLKAVSRH IFGTLRFPGG 300 HSIEFLHLLE RKTRV |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06442 | DPM1_like | 2.0e-17 | 72 | 274 | 204 | + DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily. | ||
pfam00535 | Glycos_transf_2 | 4.0e-21 | 71 | 268 | 199 | + Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. | ||
cd04179 | DPM_DPG-synthase_like | 2.0e-43 | 72 | 274 | 204 | + DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily. | ||
PTZ00260 | PTZ00260 | 7.0e-68 | 62 | 277 | 219 | + dolichyl-phosphate beta-glucosyltransferase; Provisional | ||
cd04188 | DPG_synthase | 3.0e-77 | 72 | 274 | 203 | + DPG_synthase is involved in protein N-linked glycosylation. UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_181493.1 | 0 | 34 | 277 | 32 | 276 | glycosyl transferase family 2 protein [Arabidopsis thaliana] |
RefSeq | XP_002283615.1 | 0 | 32 | 277 | 30 | 277 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002312095.1 | 0 | 32 | 277 | 30 | 276 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315224.1 | 0 | 33 | 277 | 31 | 276 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002530857.1 | 0 | 34 | 277 | 32 | 276 | Dolichyl-phosphate beta-glucosyltransferase, 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 | 3l7l_D | 0.0003 | 70 | 189 | 4 | 124 | A Chain A, Crystal Structure Of A Methyltransferase-Like Protein (Spo2022) From Silicibacter Pomeroyi Dss-3 At 1.80 A Resolution |
PDB | 3l7l_C | 0.0003 | 70 | 189 | 4 | 124 | A Chain A, Crystal Structure Of A Methyltransferase-Like Protein (Spo2022) From Silicibacter Pomeroyi Dss-3 At 1.80 A Resolution |
PDB | 3l7l_B | 0.0003 | 70 | 189 | 4 | 124 | A Chain A, Crystal Structure Of A Methyltransferase-Like Protein (Spo2022) From Silicibacter Pomeroyi Dss-3 At 1.80 A Resolution |
PDB | 3l7l_A | 0.0003 | 70 | 189 | 4 | 124 | A Chain A, Crystal Structure Of A Methyltransferase-Like Protein (Spo2022) From Silicibacter Pomeroyi Dss-3 At 1.80 A Resolution |
PDB | 3l7k_D | 0.0003 | 70 | 189 | 4 | 124 | A Chain A, Crystal Structure Of A Methyltransferase-Like Protein (Spo2022) From Silicibacter Pomeroyi Dss-3 At 1.80 A Resolution |