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Protein

DNA endonuclease I-CreI

Gene
N/A
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

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
Metal bindingi19Magnesium 1; via carbonyl oxygen1
Metal bindingi20Magnesium 11
Metal bindingi20Magnesium 2; shared with dimeric partner1

GO - Molecular functioni

  • endonuclease activity Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

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

Protein family/group databases

REBASEi2540 I-CreI

Names & Taxonomyi

Protein namesi
Recommended name:
DNA endonuclease I-CreI (EC:3.1.-.-)
Alternative name(s):
23S rRNA intron protein
Encoded oniPlastid; Chloroplast
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001927831 – 163DNA endonuclease I-CreIAdd BLAST163

Interactioni

Subunit structurei

Homodimer.7 Publications

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

DIPiDIP-59771N

Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 20Combined sources14
Beta strandi22 – 29Combined sources8
Beta strandi31 – 33Combined sources3
Beta strandi36 – 48Combined sources13
Helixi49 – 51Combined sources3
Helixi52 – 62Combined sources11
Beta strandi66 – 70Combined sources5
Beta strandi73 – 78Combined sources6
Helixi81 – 91Combined sources11
Helixi92 – 94Combined sources3
Beta strandi96 – 98Combined sources3
Helixi99 – 115Combined sources17
Helixi119 – 135Combined sources17
Helixi145 – 153Combined sources9

3D structure databases

SMRiP05725
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05725

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni26 – 38Interaction with DNAAdd BLAST13
Regioni44 – 47Interaction with DNA4
Regioni68 – 70Interaction with DNA3
Regioni138 – 143Interaction with DNA6

Sequence similaritiesi

Belongs to the LAGLIDADG endonuclease family.Curated

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

Sequencei

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
Checksum:i22B625C0CD72F575
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01977 Genomic DNA Translation: CAA26008.2
PIRiA23091

Similar proteinsi

Entry informationi

Entry nameiDNE1_CHLRE
AccessioniPrimary (citable) accession number: P05725
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: July 27, 2011
Last modified: October 25, 2017
This is version 97 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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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