Detailed Peptide Information
This page shows detailed information of individual peptides present in PlantPepDB database. The page is majorly divided into 3 sections. The first sections contains primary information like peptide activity, source, sequence, etc. In the secondary information section user can access the tertiary structure as well as the physico-chemical properties by clicking the respective links. Further there is also link of the source database and research article from which the peptide data is retrieved. Download the information by clicking
| Primary Information |
|---|
| PPepDB ID | PPepDB_4460 |
| Peptide Name | RBL2_HETTR |
| PMID(s) | --NA-- |
| Plant Source (Scientific Name) | Heterocapsa triquetra |
| Plant Source (Common Name) | Dinoflagellate |
| Plant Family | Heterocapsaceae |
| Peptide Family | --NA-- |
| Peptide Function | Signaling-peptide |
| Peptide Function Description | Calvin cycle; Carbon dioxide fixation; Chloroplast; Lyase; Magnesium; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Photorespiration; Photosynthesis; Plastid; Signal; Transit peptide; Transmembrane | Ribulose bisphosphate carboxylase, chloroplast precursor (EC 4.1.1.39),(RuBisCO).Plastid, chloroplast (Probable). Note=In this organism the plastid is the result |
| Activity Against | --NA-- |
| IC50 value | --NA-- |
| Sequence | AMMCSVLTLTIGNNQGMGDVEYGKIYDIYFPPSYLRLFDGPSCNIIDMWRAQFGPLSENCAFLVDGYVAGGTAVTVARRNFPKQFLHYHRAGHGSVTSPQDGPYYHQTWEGMAETTPIISGGMNALRLPAFFENLGHSNVILTAGGGAFGEQPAPSTSALPWAFGAGACLALAAGGQRKQRSAIAQGRATVLPTASPVVRGPDLHMAGSPLPPPLKGYLNDIGYLSDGTPMATAGNLSNHHKDGPKQGATSCRQGEEAWKLWKAGVYGSVSLSDGVIEYAKTHEEIKGAFILGRGTTDGGLVVGTIIKPKLGLQPKPFGEACYAFWQGGDFIKNDEPQGNLTFQKDADQIYPGWKEKLGYTGESSVQAASFDWKKKAAAAAFAGSSTQARLTNHPETIGPDPHINGSELPQAVFVNSIGYLPDGTAMNQAGNAVNHPETMMPSSSFTTGLALGAGALVGANAFVAPTAKTTNLRAPTQEASLQVAASQQTQPFCQMNEVIPEVVKAMRAAIKETGVAKLFSANITADDPAEMIARGKYVLRALDQSSRYADLSLSEEQLIANGKHVLVSYIMKPKAGYDYLATAAHFAAESSTGTNVNVCTTDDFTKSVDALVYYIDPENEECKIAYPNLLFDRNIIDGRTQRGYTAFVHTKLSRVQGASGIHVGTMSFGKMEGDASDKNIAFMLQDDAATVGVQMRHGYDDVATNTFYYDKRLESFGQQEFFNQVGYLPDGTPMNTAGN |
| Sequence Length | 740 |
| Validation | Experimental evidence at transcript level |
| Average Molecular Weight (Da) | 79148.06 |
| Monoisotopic Molecular Weight (Da) | 79097.96 |
| Isoelectric Point (pI) | 5.82 |
| Method / Extraction | --NA-- |
| External links (Uniprot, PDB and Source Information Database) |
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| Uniprot | Q5ENN5 |
| NCBI | --NA-- |
| EMBL | AY826897 |
| Link to Source Databases | SPdb213870 |
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| Addtional Information | FUNCTION:RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site (By similarity).CATALYTIC ACTIVITY:2 3-phospho-D-glycerate 2 H() = D-ribulose 1,5-bisphosphate CO(2) H(2)O.CATALYTIC ACTIVITY:3-phospho-D-glycerate 2-phosphoglycolate = D-ribulose 1,5-bisphosphate O(2).COFACTOR:Binds 1 magnesium ion per subunit (By similarity).SUBUNIT:Homodimer (By similarity).MISCELLANEOUS:The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits (By similarity).MISCELLANEOUS:This protein is suggested in Ref.1 to be first co- translationally imported into the ER up to the stop-transfer signal, so that the N-terminal region of the transit peptide is in the lumen of the ER while the rest of the protein remains in the cytoplasm. Maintaining this topology, proteins are directed to the Golgi and sorted into vesicles that will fuse with the outermost plastid membrane, exposing the transit peptide to the Toc/Tic apparatus, which draws the entire protein across the remaining membranes.SIMILARITY:Belongs to the RuBisCO large chain family. Type II subfamily.CAUTION:Note that unlike other eukaryotes, peridinin-containing dinoflagellates have a nuclear-encoded chloroplast-targeted form II RuBisCO. |
