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Protein

Intron-encoded endonuclease I-PpoI

Gene
N/A
Organism
Physarum polycephalum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Mediates the homing of a group I intron in the ribosomal DNA. Makes a four-base staggered cut in its ribosomal DNA target sequence.

Cofactori

GO - Molecular functioni

  1. endonuclease activity Source: UniProtKB-KW

GO - Biological processi

  1. intron homing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Intron homing

Keywords - Ligandi

Zinc

Protein family/group databases

REBASEi2469. I-PpoI.

Names & Taxonomyi

Protein namesi
Recommended name:
Intron-encoded endonuclease I-PpoI (EC:3.1.-.-)
Short name:
I-Ppo
OrganismiPhysarum polycephalum (Slime mold)
Taxonomic identifieri5791 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaMyxogastriaMyxogastromycetidaePhysariidaPhysaraceaePhysarum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Intron-encoded endonuclease I-PpoIPRO_0000192788Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1915Combined sources
Beta strandi24 – 329Combined sources
Beta strandi35 – 439Combined sources
Beta strandi46 – 483Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 688Combined sources
Beta strandi71 – 766Combined sources
Turni77 – 793Combined sources
Helixi80 – 823Combined sources
Beta strandi83 – 853Combined sources
Beta strandi87 – 893Combined sources
Beta strandi92 – 987Combined sources
Helixi108 – 1103Combined sources
Beta strandi111 – 1155Combined sources
Helixi116 – 1216Combined sources
Helixi122 – 1243Combined sources
Turni128 – 1314Combined sources
Beta strandi157 – 1604Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A73X-ray1.80A/B1-163[»]
1A74X-ray2.20A/B1-163[»]
1CYQX-ray1.93A/B2-163[»]
1CZ0X-ray2.10A/B2-163[»]
1EVWX-ray3.10A/B/C/D1-163[»]
1EVXX-ray2.00A/B2-163[»]
1IPPX-ray2.20A/B1-163[»]
2O6MX-ray2.30A/B1-163[»]
ProteinModelPortaliQ94702.
SMRiQ94702. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ94702.

Family & Domainsi

Family and domain databases

InterProiIPR008704. Endonuclease_Zinc-binding_loop.
[Graphical view]
PfamiPF05551. zf-His_Me_endon. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q94702-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALTNAQILA VIDSWEETVG QFPVITHHVP LGGGLQGTLH CYEIPLAAPY
60 70 80 90 100
GVGFAKNGPT RWQYKRTINQ VVHRWGSHTV PFLLEPDNIN GKTCTASHLC
110 120 130 140 150
HNTRCHNPLH LCWESLDDNK GRNWCPGPNG GCVHAVVCLR QGPLYGPGAT
160
VAGPQQRGSH FVV
Length:163
Mass (Da):17,789
Last modified:December 15, 1998 - v3
Checksum:iA193B6F06B0D8EEF
GO

Sequence cautioni

The sequence AAB65764.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38131 Genomic DNA. Translation: AAB65765.1.
M38131 Genomic DNA. Translation: AAB65764.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38131 Genomic DNA. Translation: AAB65765.1.
M38131 Genomic DNA. Translation: AAB65764.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A73X-ray1.80A/B1-163[»]
1A74X-ray2.20A/B1-163[»]
1CYQX-ray1.93A/B2-163[»]
1CZ0X-ray2.10A/B2-163[»]
1EVWX-ray3.10A/B/C/D1-163[»]
1EVXX-ray2.00A/B2-163[»]
1IPPX-ray2.20A/B1-163[»]
2O6MX-ray2.30A/B1-163[»]
ProteinModelPortaliQ94702.
SMRiQ94702. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

REBASEi2469. I-PpoI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ94702.

Family and domain databases

InterProiIPR008704. Endonuclease_Zinc-binding_loop.
[Graphical view]
PfamiPF05551. zf-His_Me_endon. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of I-Ppo, an intron-encoded endonuclease that mediates homing of a group I intron in the ribosomal DNA of Physarum polycephalum."
    Muscarella D.E., Ellison E.L., Ruoff B.M., Vogt V.M.
    Mol. Cell. Biol. 10:3386-3396(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Vogt V.M.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI."
    Flick K.E., Jurica M.S., Monnat R.J. Jr., Stoddard B.L.
    Nature 394:96-101(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
  5. "Conformational changes and cleavage by the homing endonuclease I-PpoI: a critical role for a leucine residue in the active site."
    Galburt E.A., Chadsey M.S., Jurica M.S., Chevalier B.S., Erho D., Tang W., Monnat R.J. Jr., Stoddard B.L.
    J. Mol. Biol. 300:877-887(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiPPO1_PHYPO
AccessioniPrimary (citable) accession number: Q94702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: November 26, 2014
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.