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Entry version 100 (18 Sep 2019)
Sequence version 2 (27 Jul 2011)
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Protein

DNA endonuclease I-CreI

Gene
N/A
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
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

Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site.

<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+3 Publications, Mn2+3 Publications, Co2+3 Publications, Ni2+3 Publications, Zn2+3 PublicationsNote: Binds 3 Mg2+ ions per homodimer. The enzyme can also utilize Mn2+ or Co2+, but has lower cleavage activity with Ni2+ or Zn2+. Ca2+ Co2+ give no enzyme activity.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi19Magnesium 1; via carbonyl oxygen1
Metal bindingi20Magnesium 11
Metal bindingi20Magnesium 2; shared with dimeric partner1

<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 functionEndonuclease, Hydrolase, Nuclease
Biological processIntron homing
LigandMagnesium, Metal-binding

Protein family/group databases

Restriction enzymes and methylases database

More...
REBASEi
2540 I-CreI

<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_and_taxonomy_section">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:
DNA endonuclease I-CreI (EC:3.1.-.-)
Alternative name(s):
23S rRNA intron protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlastid; Chloroplast
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri3055 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi20D → A, L or N: Loss of catalytic activity. Reduced affinity for DNA. 1 Publication1
Mutagenesisi26Q → A or C: Alters the specificity of the endonuclease. 1 Publication1
Mutagenesisi33Y → C, H or R: Alters the specificity of the endonuclease. 2 Publications1
Mutagenesisi44Q → A, C, T, V or W: Alters the specificity of the endonuclease. 1 Publication1
Mutagenesisi47Q → A, E or M: Loss of catalytic activity. 1 Publication1
Mutagenesisi47Q → N: Strongly reduced affinity for DNA. No effect on catalytic activity. 1 Publication1
Mutagenesisi68R → A: Loss of activity. 1 Publication1
Mutagenesisi98K → A: Strongly reduced affinity for DNA. Increased catalytic activity. 1 Publication1
Mutagenesisi98K → R: Strongly reduced affinity for DNA. No effect on catalytic activity. 1 Publication1
Mutagenesisi138S → A: Reduced affinity for DNA. No effect on catalytic activity. Reduced cleavage; when associated with M-139. 1 Publication1
Mutagenesisi139K → M: Reduced affinity for DNA. No effect on catalytic activity. Reduced cleavage; when associated with A-138. 1 Publication1
Mutagenesisi142K → G: Reduced affinity for DNA. No effect on catalytic activity. Reduced cleavage; when associated with G-143. 1 Publication1
Mutagenesisi143T → G: Reduced affinity for DNA. No effect on catalytic activity. Reduced cleavage; when associated with G-142. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001927831 – 163DNA endonuclease I-CreIAdd BLAST163

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-15738760,EBI-15738760

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-59771N

<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

1163
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

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SMRi
P05725

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P05725

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 38Interaction with DNAAdd BLAST13
Regioni44 – 47Interaction with DNA4
Regioni68 – 70Interaction with DNA3
Regioni138 – 143Interaction with DNA6

<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 LAGLIDADG endonuclease family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.28.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027434 Homing_endonucl
IPR004860 LAGLIDADG_2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00961 LAGLIDADG_1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55608 SSF55608, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P05725-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNTKYNKEFL LYLAGFVDGD GSIIAQIKPN QSYKFKHQLS LTFQVTQKTQ
60 70 80 90 100
RRWFLDKLVD EIGVGYVRDR GSVSDYILSE IKPLHNFLTQ LQPFLKLKQK
110 120 130 140 150
QANLVLKIIE QLPSAKESPD KFLEVCTWVD QIAALNDSKT RKTTSETVRA
160
VLDSLSEKKK SSP
Length:163
Mass (Da):18,696
Last modified:July 27, 2011 - v2
<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:i22B625C0CD72F575
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X01977 Genomic DNA Translation: CAA26008.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A23091

<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
X01977 Genomic DNA Translation: CAA26008.2
PIRiA23091

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
1AF5X-ray3.00A4-138[»]
1BP7X-ray3.00A/B/C/D2-153[»]
1G9YX-ray2.05A/B2-153[»]
1G9ZX-ray1.80A/B2-153[»]
1MOWX-ray2.40A/D/G/J17-163[»]
1N3EX-ray2.50A/B/G/H1-163[»]
1N3FX-ray2.00A/B/G/H1-163[»]
1T9IX-ray1.60A/B1-163[»]
1T9JX-ray2.00A/B1-163[»]
1U0CX-ray2.50A/B1-163[»]
1U0DX-ray2.90A/B1-163[»]
2I3PX-ray2.30A/B1-153[»]
2I3QX-ray2.30A/B1-153[»]
2O7MX-ray2.00A/B1-156[»]
2VBJX-ray1.95A/B2-153[»]
2VBLX-ray1.80A/B1-153[»]
2VBNX-ray1.90A/B1-153[»]
2VBOX-ray1.80A/B1-153[»]
4AABX-ray2.50A/B2-153[»]
4AADX-ray3.10A/B2-153[»]
4AAEX-ray2.60A/B2-154[»]
4AAFX-ray2.50A/B2-153[»]
4AAGX-ray2.80A/B2-153[»]
4AQUX-ray2.30A/B2-153[»]
4AQXX-ray2.20A/B2-153[»]
6FB0X-ray2.15A2-154[»]
B2-155[»]
6FB1X-ray3.02A/B2-155[»]
6FB2X-ray2.95A2-154[»]
B2-155[»]
6FB5X-ray2.20A2-154[»]
B2-155[»]
6FB6X-ray2.60A2-154[»]
B2-155[»]
6FB7X-ray2.69A/B2-153[»]
6FB8X-ray2.45A/B2-153[»]
6FB9X-ray2.95A/B2-153[»]
SMRiP05725
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-59771N

Protein family/group databases

REBASEi2540 I-CreI

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP05725

Family and domain databases

Gene3Di3.10.28.10, 1 hit
InterProiView protein in InterPro
IPR027434 Homing_endonucl
IPR004860 LAGLIDADG_2
PfamiView protein in Pfam
PF00961 LAGLIDADG_1, 1 hit
SUPFAMiSSF55608 SSF55608, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiDNE1_CHLRE
<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: P05725
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: September 18, 2019
This is version 100 of the entry and version 2 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 programPlant 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

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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