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Search results 701 to 800 out of 878 for Sf1

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 1138  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1525  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 733  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2544  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1601  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 869  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 725  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1025  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 840  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 763  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1617  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1187  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1214  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1244  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 763  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1583  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1239  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1165  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2021  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1174  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 672  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1383  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1384  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1848  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1848  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1264  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 862  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 990  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1173  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 978  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1510  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1025  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 735  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1239  
Fragment?: false
Publication
First Author: Singleton MR
Year: 2004
Journal: Nature
Title: Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks.
Volume: 432
Issue: 7014
Pages: 187-93
Publication
First Author: Tanner NK
Year: 2003
Journal: Mol Cell
Title: The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis.
Volume: 11
Issue: 1
Pages: 127-38
Publication
First Author: Yeeles JT
Year: 2011
Journal: Nucleic Acids Res
Title: The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain.
Volume: 39
Issue: 6
Pages: 2271-85
Protein Domain
Type: Domain
Description: Helicases have been classified in 5 superfamilies (SF1-SF5). All of theproteins bind ATP and, consequently, all of them carry the classical Walker A(phosphate-binding loop or P-loop) and Walker B(Mg2+-binding aspartic acid) motifs. For the two largest groups, commonlyreferred to as SF1 and SF2, a total of seven characteristic motifs have beenidentified []which are distributed over two structural domains, anN-terminal ATP-binding domain and a C-terminal domain. UvrD-like DNA helicasesbelong toSF1, but they differ from classical SF1/SF2 by alarge insertion in each domain. UvrD-like DNA helicases unwind DNA with a3'-5' polarity [].Crystal structures of several uvrD-like DNA helicases have been solved [, , ]. They are monomeric enzymes consisting of twodomains with a common α-β RecA-like core. The ATP-binding site issituated in a cleft between the N terminus of the ATP-binding domain and thebeginning of the C-terminal domain. The enzyme crystallizes in two differentconformations (open and closed). The conformational difference between the twoforms comprises a large rotation of the end of the C-terminal domain byapproximately 130 degrees. This "domain swiveling"was proposed to be an importantaspect of the mechanism of the enzyme [].Some proteins that belong to the UvrD-like DNA helicase family are listedbelow:Bacterial UvrD helicase. It is involved in the post-incision events ofnucleotide excision repair and methyl-directed mismatch repair. It unwindsDNA duplexes with 3'-5' polarity with respect to the bound strand andinitiates unwinding most effectively when a single-stranded region ispresent.Gram-positive bacterial pcrA helicase, an essential enzyme involved in DNArepair and rolling circle replication. The Staphylococcus aureus pcrAhelicase has both 5'-3' and 3'-5' helicase activities.Bacterial rep proteins, a single-stranded DNA-dependent ATPase involved inDNA replication which can initiate unwinding at a nick in the DNA. It bindsto the single-stranded DNA and acts in a progressive fashion along the DNAin the 3' to 5' direction.Bacterial helicase IV (helD gene product). It catalyzes the unwinding ofduplex DNA in the 3'-5' direction.Bacterial recB protein. RecBCD is a multi-functional enzyme complex thatprocesses DNA ends resulting from a double-strand break. RecB is a helicasewith a 3'-5' directionality.Fungal srs2 proteins, an ATP-dependent DNA helicase involved in DNA repair. The polarity of the helicase activity was determined to be 3'-5'.This domain is also found bacterial helicase-nuclease complex AddAB, both in subunit AddA and AddB. The AddA subunit is responsable for the helicase activity. AddB also harbors a putative ATP-binding domain which does not play a role as a secondary DNA motor, but that it may instead facilitate the recognition of the recombination hotspot sequences [].This entry represents the ATP-binding domain found in AddA, AddB and UvrD-like helicases.
Protein Domain
Type: Domain
Description: Helicases have been classified in 5 superfamilies (SF1-SF5) []. All of the proteins bind ATP and, consequently, all of them carry the classical Walker A (phosphate-binding loop or P-loop), and Walker B (Mg2+-binding aspartic acid) motifs []. For the two largest groups, commonly referred to as SF1 and SF2, a total of seven characteristic motifs have been identified []which are distributed over two structural domains, an N-terminal ATP-binding domain and a C-terminal domain.This entry represents the C-terminal domain.UvrD-like DNA helicases belong to SF1, but they differ from classical SF1/SF2 by a large insertion in each domain. UvrD-like DNA helicases unwind DNA with a 3'-5' polarity []. Crystal structures of several uvrD-like DNA helicases have been solved [, , ]. They are monomeric enzymes consisting of two domains with a common α-β RecA-like core. The ATP-binding site is situated in a cleft between the N terminus of the ATP-binding domain and the beginning of the C-terminal domain. The enzyme crystallizes in two different conformations (open and closed). The conformational difference between the two forms comprises a large rotation of the end of the C-terminal domain by approximately 130 degrees. This "domain swiveling"was proposed to be an important aspect of the mechanism of the enzyme [].Some proteins that belong to the uvrD-like DNA helicase family are listed below:Bacterial UvrD helicase. It is involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair. It unwinds DNA duplexes with 3'-5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present.Gram-positive bacterial pcrA helicase, an essential enzyme involved in DNA repair and rolling circle replication. The Staphylococcus aureus pcrA helicase has both 5'-3' and 3'-5' helicase activities. Bacterial rep proteins, a single-stranded DNA-dependent ATPase involved in DNA replication which can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction.Bacterial helicase IV (helD gene product). It catalyzes the unwinding of duplex DNA in the 3'-5' direction.Bacterial recB protein. RecBCD is a multi-functional enzyme complex that processes DNA ends resulting from a double-strand break. RecB is a helicase with a 3'-5' directionality.Fungal srs2 proteins, an ATP-dependent DNA helicase involved in DNA repair. The polarity of the helicase activity was determined to be 3'-5'.
Protein
Organism: Mus musculus/domesticus
Length: 1062  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1863  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1124  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1622  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1843  
Fragment?: false
Publication
First Author: Korolev S
Year: 1997
Journal: Cell
Title: Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP.
Volume: 90
Issue: 4
Pages: 635-47
Publication
First Author: Schmid SR
Year: 1992
Journal: Mol Microbiol
Title: D-E-A-D protein family of putative RNA helicases.
Volume: 6
Issue: 3
Pages: 283-91
Publication
First Author: Velankar SS
Year: 1999
Journal: Cell
Title: Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism.
Volume: 97
Issue: 1
Pages: 75-84
Publication
First Author: Soultanas P
Year: 2000
Journal: Curr Opin Struct Biol
Title: DNA helicases: 'inching forward'.
Volume: 10
Issue: 1
Pages: 124-8
Publication
First Author: Hao W
Year: 2017
Journal: PLoS Pathog
Title: Crystal structure of Middle East respiratory syndrome coronavirus helicase.
Volume: 13
Issue: 6
Pages: e1006474
Protein
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 646  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 740  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2711  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1711  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1916  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2476  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2198  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 926  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1003  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1827  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2885  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1416  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2582  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 900  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2986  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1388  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1401  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 779  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1046  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1100  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1445  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1100  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 139  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1692  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1032  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 924  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 885  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true