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Reviewed, UniProtKB/Swiss-Prot P03880 (ANI1_EMENI)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Intron-encoded DNA endonuclease I-AniI
Alternative name(s):
    mRNA maturase bI1
    COB intron protein
Cleaved into the following 2 chains:
    1- Recommended name:
            Truncated non-functional cytochrome b
    2- Recommended name:
            DNA endonuclease/RNA maturase I-AniI
              EC=3.1.-.-
Gene names
Name: I-AniI
Encoded onMitochondrion
OrganismEmericella nidulans (Aspergillus nidulans)
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Mitochondrial DNA endonuclease and mRNA maturase involved in intron homing and required for splicing of the cytochrome b (cobA) gene intron, containing its own coding sequence. The protein stimulates the intrinsic ribozyme activity of the intron through binding to and stabilizing specific secondary and tertiary structure elements in the RNA. As an endonuclease it introduces a specific double-strand break at the junction of the two exons the cobA gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited specificity and cleaves the sequence 5'-GAGGAGGTTTCTCTGTA-3'. The proteins RNA and DNA recognition and binding surfaces are independent. Ref.3 Ref.4 Ref.5

Cofactor

Magnesium.

Subunit structure

Homodimer.

Subcellular location

Mitochondrion.

Post-translational modification

The mature protein may arise from proteolytic cleavage of an in-frame translation of cobA exon 1 plus intron, containing the I-AniI open reading frame. Cleavage may take place close to Met-213 resulting in an active endonuclease/maturase of about 30 kDa By similarity.

Miscellaneous

Residues 237 to 488 are sufficient for endonuclease, intron homing, and RNA maturase activity.

Sequence similarities

In the C-terminal section; belongs to the LAGLIDADG endonuclease family.

Sequence caution

The sequence AAA31737.1 differs from that shown. Reason: Erroneous gene model prediction. The cobA ORF was not predicted to be expressed alternatively as a fusion with intron 4, and intron 4 CDS was not annotated.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ?Truncated non-functional cytochrome bPRO_0000013491
Chain? – 488DNA endonuclease/RNA maturase I-AniIPRO_0000013492

Regions

Region1 – 169169cobA exon 1 encoded
Region170 – 488319cobA intron encoded

Experimental info

Sequence conflict2951I → R Ref.6

Secondary structure

........................................ 488
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03880-1 [UniParc].

Last modified July 19, 2004. Version 3.
Checksum: 40B106A275535E27

FASTA48855,395
        10         20         30         40         50         60 
MRILKSHPLL KIVNSYIIDS PQPANLSYLW NFGSLLALCL GIQIVTGVTL AMHYTPSVSE 

        70         80         90        100        110        120 
AFNSVEHIMR DVNNGWLVRY LHSNTASAFF FLVYLHIGRG LYYGSYKTPR TLTWAIGTVI 

       130        140        150        160        170        180 
LIVMMATAFL GYVLPYGQMS LWGATVITNL MSAIPWIGQD IVEFIWGGLY TDEPQCGDVL 

       190        200        210        220        230        240 
LKILLNAGKS PILGFAYDLF FIIVLLIGVK IAMTRGKSAG VRSLHTSEAS QRLHAGDLTY 

       250        260        270        280        290        300 
AYLVGLFEGD GYFSITKKGK YLTYELGIEL SIKDVQLIYK IKKILGIGIV SFRKINEIEM 

       310        320        330        340        350        360 
VALRIRDKNH LKSFILPIFE KYPMFSNKQY DYLRFRNALL SGIISLEDLP DYTRSDEPLN 

       370        380        390        400        410        420 
SIESIINTSY FSAWLVGFIE AEGCFSVYKL NKDDDYLIAS FDIAQRDGDI LISAIRKYLS 

       430        440        450        460        470        480 
FTTKVYLDKT NCSKLKVTSV RSVENIIKFL QNAPVKLLGN KKLQYLLWLK QLRKISRYSE 


KIKIPSNY 

« Hide

References

[1]"The mosaic organization of the apocytochrome b gene of Aspergillus nidulans revealed by DNA sequencing."
Waring R.B., Davies R.W., Lee S., Grisi E., Berks M.M., Scazzocchio C.
Cell 27:4-11(1981) [PubMed: 7034966] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Internal structure of a mitochondrial intron of Aspergillus nidulans."
Waring R.B., Davies R.W., Scazzocchio C., Brown T.A.
Proc. Natl. Acad. Sci. U.S.A. 79:6332-6336(1982) [PubMed: 6755468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 170-488.
[3]"A protein encoded by a group I intron in Aspergillus nidulans directly assists RNA splicing and is a DNA endonuclease."
Ho Y., Kim S.-J., Waring R.B.
Proc. Natl. Acad. Sci. U.S.A. 94:8994-8999(1997) [PubMed: 9256423] [Abstract]
Cited for: FUNCTION, RNA SPLICING AND ENDONUCLEASE ACTIVITY.
[4]"The maturase encoded by a group I intron from Aspergillus nidulans stabilizes RNA tertiary structure and promotes rapid splicing."
Ho Y., Waring R.B.
J. Mol. Biol. 292:987-1001(1999) [PubMed: 10512698] [Abstract]
Cited for: FUNCTION, BIOCHEMICAL CHARACTERIZATION OF MATURASE ACTIVITY.
[5]"Functionally distinct nucleic acid binding sites for a group I intron encoded RNA maturase/DNA homing endonuclease."
Chatterjee P., Brady K.L., Solem A., Ho Y., Caprara M.G.
J. Mol. Biol. 329:239-251(2003) [PubMed: 12758073] [Abstract]
Cited for: FUNCTION, RNA AND DNA-BINDING.
[6]"Structural and biochemical analyses of DNA and RNA binding by a bifunctional homing endonuclease and group I intron splicing factor."
Bolduc J.M., Spiegel P.C., Chatterjee P., Brady K.L., Downing M.E., Caprara M.G., Waring R.B., Stoddard B.L.
Genes Dev. 17:2875-2888(2003) [PubMed: 14633971] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 237-488 IN COMPLEX WITH DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

J01388 Genomic DNA. Translation: AAA31737.1. Sequence problems.
J01389 Genomic DNA. No translation available.
J01387 Genomic DNA. No translation available.
PIRQXASBI. A04513.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P8KX-ray2.60Z237-488[»]
2QOJX-ray2.40Z237-488[»]
3EH8X-ray2.70A/D/G237-488[»]
ModBaseSearch...

Family and domain databases

InterProIPR016175. Cyt_b/b6.
IPR005797. Cyt_b/b6_N.
IPR001982. Endonuc_LAG/HNH.
[Graphical view]
Gene3DG3DSA:1.20.810.10. Cytochrome_b/b6. 1 hit.
PANTHERPTHR19271. Cytochrome_b/b6. 1 hit.
PfamPF00033. Cytochrom_B_N. 1 hit.
PF00961. LAGLIDADG_1. 2 hits.
[Graphical view]
PROSITEPS51002. CYTB_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANI1_EMENI
AccessionPrimary (citable) accession number: P03880
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2004
Last modified: June 16, 2009
This is version 65 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents