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Q7JQ07 (MOS1T_DROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 30, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mariner Mos1 transposase

EC=3.1.-.-
Alternative name(s):
Transposable element Mos1 transposase
Gene names
Name:mariner\T
OrganismDrosophila mauritiana (Fruit fly)
Taxonomic identifier7226 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates transposition of transposon Mos1 by a 'cut and paste' mechanism. Transposases are sequence-specific nucleases and strand transferases that catalyze transposition through an ordered series of events: sequence-specific binding of transposase to the terminal inverted repeats (IR) present at each end of the transposon, pairing of the transposon IRs in a paired-end complex (PEC), cleavage of one or both DNA strands at each transposon end, capture of target DNA, and strand transfer to insert the transposon at a new site. Ref.3

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese.

Subunit structure

Homodimer. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Ref.3

Subcellular location

Nucleus Probable.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
   Cellular componentNucleus
   LigandDNA-binding
Magnesium
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Transposable element
Gene Ontology (GO)
   Biological processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Mariner Mos1 transposase
PRO_0000386644

Regions

DNA binding24 – 5532H-T-H motif
DNA binding89 – 11022H-T-H motif
Region1 – 112112DNA-binding
Region113 – 12513Linker
Region126 – 345220Catalytic

Sites

Metal binding1561Magnesium 1
Metal binding1561Magnesium 2
Metal binding2491Magnesium 1
Metal binding2841Magnesium 2
Site481Important for base-specific DNA-binding
Site1001Important for base-specific DNA-binding
Site1181Important for base-specific DNA-binding
Site1861Critical for target DNA recognition
Site1861Important for target DNA recognition and for strand transfer activity
Site2931Important for base-specific DNA-binding

Experimental info

Mutagenesis481R → Q: Loss of DNA binding; when associated with R-100.
Mutagenesis1001Q → R: Loss of DNA binding; when associated with Q-48.
Mutagenesis1181R → A: Reduces rate of second strand cleavage; when associated with A-216.
Mutagenesis1191W → P: Alters cleavage sites in second strand cleavage.
Mutagenesis1861R → A: No effect on second strand cleavage. Strongly reduced strand transfer activity.
Mutagenesis2161T → A: Reduces rate of second strand cleavage; when associated with A-118.
Mutagenesis2841D → A: Loss of catalytic activity.
Sequence conflict1521I → L in AAA28701. Ref.2
Sequence conflict1641S → N in AAA28698. Ref.2
Sequence conflict1641S → N in AAA28699. Ref.2
Sequence conflict1641S → N in AAA28700. Ref.2
Sequence conflict1641S → N in AAA28701. Ref.2
Sequence conflict1641S → N in AAA28702. Ref.2
Sequence conflict1641S → N in AAA28703. Ref.2
Sequence conflict2101R → P in AAA28698. Ref.2
Sequence conflict2101R → P in AAA28699. Ref.2
Sequence conflict2101R → P in AAA28700. Ref.2
Sequence conflict2101R → P in AAA28701. Ref.2
Sequence conflict2101R → P in AAA28702. Ref.2
Sequence conflict2101R → P in AAA28703. Ref.2
Sequence conflict2431R → K in AAA28703. Ref.2
Sequence conflict248 – 2492HD → YG in AAA28703. Ref.2
Sequence conflict2601R → C in AAA28703. Ref.2

Secondary structure

.................................................. 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7JQ07 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BC8E59E33B966697

FASTA34540,851
        10         20         30         40         50         60 
MSSFVPNKEQ TRTVLIFCFH LKKTAAESHR MLVEAFGEQV PTVKKCERWF QRFKSGDFDV 

        70         80         90        100        110        120 
DDKEHGKPPK RYEDAELQAL LDEDDAQTQK QLAEQLEVSQ QAVSNRLREM GKIQKVGRWV 

       130        140        150        160        170        180 
PHELNERQME RRKNTCEILL SRYKRKSFLH RIVTGDEKWI FFVSPKRKKS YVDPGQPATS 

       190        200        210        220        230        240 
TARPNRFGKK TMLCVWWDQS GVIYYELLKR GETVNTARYQ QQLINLNRAL QRKRPEYQKR 

       250        260        270        280        290        300 
QHRVIFLHDN APSHTARAVR DTLETLNWEV LPHAAYSPDL APSDYHLFAS MGHALAEQRF 

       310        320        330        340 
DSYESVKKWL DEWFAAKDDE FYWRGIHKLP ERWEKCVASD GKYLE 

« Hide

References

[1]"Molecular structure of a somatically unstable transposable element in Drosophila."
Jacobson J.W., Medhora M.M., Hartl D.L.
Proc. Natl. Acad. Sci. U.S.A. 83:8684-8688(1986) [PubMed: 3022302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The mariner transposable element is widespread in insects."
Robertson H.M.
Nature 362:241-245(1993) [PubMed: 8384700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 125-275.
[3]"Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote."
Richardson J.M., Colloms S.D., Finnegan D.J., Walkinshaw M.D.
Cell 138:1096-1108(2009) [PubMed: 19766564] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF MUTANT ALA-216 IN COMPLEX WITH INVERTED REPEAT DNA; MAGNESIUM AND MANGANESE IONS, FUNCTION, SUBUNIT, METAL-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14653 Genomic DNA. Translation: AAA28678.1.
L10449 Genomic DNA. Translation: AAA28698.1.
L10450 Genomic DNA. Translation: AAA28699.1.
L10451 Genomic DNA. Translation: AAA28700.1.
L10452 Genomic DNA. Translation: AAA28701.1.
L10453 Genomic DNA. Translation: AAA28702.1.
L10454 Genomic DNA. Translation: AAA28703.1.
PIRS36997.
S37002.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HOSX-ray3.50A/B1-343[»]
3HOTX-ray3.25A/B1-343[»]
ProteinModelPortalQ7JQ07.
SMRQ7JQ07. Positions 119-345.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

FlyBaseFBgn0013835. Dmau\mariner\T.

Family and domain databases

InterProIPR001888. Transposase_1.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF01359. Transposase_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMOS1T_DROMA
AccessionPrimary (citable) accession number: Q7JQ07
Secondary accession number(s): Q05407, Q05415, Q05417
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: July 5, 2004
Last modified: November 30, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references