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Entry version 92 (02 Jun 2021)
Sequence version 1 (06 Dec 2005)
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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.

UniRule annotation2 Publications

Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.

2 Publications

Miscellaneous

RuBisCO folding and assembly commences when the nascent large subunit folds with the help of chaperonin GroEL-GroES. Both RbcX and Raf1 help folded RbcL release from the chaperonin and dimerize; dimeric Raf1 binds to RbcL2 leading to an RbcL8-Raf18 complex. RbcS displaces Raf1, resulting in holoenzyme formation.1 Publication2 Publications
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=58 µM for D-ribulose 1,5-bisphosphate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei120Substrate; in homodimeric partnerUniRule annotation1
    Binding sitei170SubstrateUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei172Proton acceptorUniRule annotation1
    Binding sitei174SubstrateUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi198Magnesium; via carbamate groupUniRule annotation1
    Metal bindingi200MagnesiumUniRule annotation1
    Metal bindingi201MagnesiumUniRule annotation1
    Active sitei291Proton acceptorUniRule annotation1
    Binding sitei292SubstrateUniRule annotation1
    Binding sitei324SubstrateUniRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei331Transition state stabilizerUniRule annotation1
    Binding sitei376SubstrateUniRule annotation1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionLyase, Monooxygenase, Oxidoreductase
    Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    SYNEL:SYNPCC7942_1426-MONOMER

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation1 Publication)
    Short name:
    RuBisCO large subunitUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:cbbLUniRule annotation
    Synonyms:rbcL1 PublicationUniRule annotation
    Ordered Locus Names:Synpcc7942_1426
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSynechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans R2)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1140 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000002717 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Keywords - Cellular componenti

    Bacterial microcompartment, Carboxysome

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Heterologous expression of 12 carboxysomal genes in E.coli (ccaA, ccmK2, ccmK3, ccmK4, ccmL, ccmM, ccmN, ccmO, ccmP, rbcL, rbcS, rbcX) leads to the formation of bodies that resemble carboxysomes, have densely packed paracrystalline arrays and RuBisCO activity. These structures open the door to generating carboxysomes in plant cells to increase their photosynthesis and productivity, as well as tailoring bacterial microcompartments to specific metabolic needs and molecule delivery.1 Publication

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002514631 – 472Ribulose bisphosphate carboxylase large chainAdd BLAST472

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei198N6-carboxylysineUniRule annotation1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi244Interchain; in linked formUniRule annotation

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q31NB3

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Carboxysome size and components vary with growth conditions. When grown in ambient air at medium light (50 uE meter(-2) second(-1)) there are 853 RuBisCO complexes (RbcL8S8) per carboxysome (measured using the small subunit), the numbers decrease under low light and high CO2, and increase under high light (at protein level).1 Publication

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked (Probable). The disulfide link is formed within the large subunit homodimers (Probable). Isolated reduced and oxidized M35 binds holo-RuBisCO (RbcL8-RbcS8) but neither subunit octamer alone; RuBisCO has a higher affinity for reduced M35. M35 binds RuBisCO via its SSUL domains; the SSUL domain binds close to the equitorial domain of RuBisCO between RbcL dimers, with 1 M35 protein per dimer (PubMed:30675061). Colocalizes with RbcX throughout carboxysome formation (PubMed:30389782).

    3 Publications3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    1140.Synpcc7942_1426

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1472
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q31NB3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG1850, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_031450_2_0_3

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    IHGHPDG

    Database of Orthologous Groups

    More...
    OrthoDBi
    848380at2

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd08212, RuBisCO_large_I, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.110, 1 hit
    3.30.70.150, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_01338, RuBisCO_L_type1, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR033966, RuBisCO
    IPR020878, RuBisCo_large_chain_AS
    IPR000685, RuBisCO_lsu_C
    IPR036376, RuBisCO_lsu_C_sf
    IPR017443, RuBisCO_lsu_fd_N
    IPR036422, RuBisCO_lsu_N_sf
    IPR020888, RuBisCO_lsuI

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR42704, PTHR42704, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00016, RuBisCO_large, 1 hit
    PF02788, RuBisCO_large_N, 1 hit

    Structure-Function Linkage Database

    More...
    SFLDi
    SFLDS00014, RuBisCO, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51649, SSF51649, 1 hit
    SSF54966, SSF54966, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00157, RUBISCO_LARGE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q31NB3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA
    60 70 80 90 100
    GAAIAAESST GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY
    110 120 130 140 150
    PLDLFEEGSV TNILTSIVGN VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH
    160 170 180 190 200
    GIQVERDLLN KYGRPMLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
    210 220 230 240 250
    ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT APTCEEMMKR
    260 270 280 290 300
    AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
    310 320 330 340 350
    QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH
    360 370 380 390 400
    IEADRSRGVF FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG
    410 420 430 440 450
    GGTLGHPWGN APGATANRVA LEACVQARNE GRDLYREGGD ILREAGKWSP
    460 470
    ELAAALDLWK EIKFEFETMD KL
    Length:472
    Mass (Da):52,448
    Last modified:December 6, 2005 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCDD8519AA9D493C9
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    CP000100 Genomic DNA Translation: ABB57456.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_011242444.1, NC_007604.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    ABB57456; ABB57456; Synpcc7942_1426

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    syf:Synpcc7942_1426

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000100 Genomic DNA Translation: ABB57456.1
    RefSeqiWP_011242444.1, NC_007604.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    6HBCelectron microscopy2.78B/C1-472[»]
    6SMHelectron microscopy4.30A/B/C/D/E/F/G/H19-465[»]
    SMRiQ31NB3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi1140.Synpcc7942_1426

    Proteomic databases

    PRIDEiQ31NB3

    Genome annotation databases

    EnsemblBacteriaiABB57456; ABB57456; Synpcc7942_1426
    KEGGisyf:Synpcc7942_1426

    Phylogenomic databases

    eggNOGiCOG1850, Bacteria
    HOGENOMiCLU_031450_2_0_3
    OMAiIHGHPDG
    OrthoDBi848380at2

    Enzyme and pathway databases

    BioCyciSYNEL:SYNPCC7942_1426-MONOMER

    Family and domain databases

    CDDicd08212, RuBisCO_large_I, 1 hit
    Gene3Di3.20.20.110, 1 hit
    3.30.70.150, 1 hit
    HAMAPiMF_01338, RuBisCO_L_type1, 1 hit
    InterProiView protein in InterPro
    IPR033966, RuBisCO
    IPR020878, RuBisCo_large_chain_AS
    IPR000685, RuBisCO_lsu_C
    IPR036376, RuBisCO_lsu_C_sf
    IPR017443, RuBisCO_lsu_fd_N
    IPR036422, RuBisCO_lsu_N_sf
    IPR020888, RuBisCO_lsuI
    PANTHERiPTHR42704, PTHR42704, 1 hit
    PfamiView protein in Pfam
    PF00016, RuBisCO_large, 1 hit
    PF02788, RuBisCO_large_N, 1 hit
    SFLDiSFLDS00014, RuBisCO, 1 hit
    SUPFAMiSSF51649, SSF51649, 1 hit
    SSF54966, SSF54966, 1 hit
    PROSITEiView protein in PROSITE
    PS00157, RUBISCO_LARGE, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBL_SYNE7
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q31NB3
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: December 6, 2005
    Last modified: June 2, 2021
    This is version 92 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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