tr A9W9N7 A9W9N7_CHLAA Putative uncharacterized protein

tr B3KYW5 B3KYW5_PLAKH SICA antigen Fragment OS

Structures of UvrD-like SF1 helicase solved so far share a four-subdomain tertiary arrangement (1A/2A/1B/2B) (Singleton et al., 2007), including two RecA-like domains (1A/2A) which contain the ATP binding site and are proposed to function as the translocase (Dillingham et al., 2001; Lee and Yang, 2006), and a flexible domain (2B) which is believed to play a regulatory role in helicase activity #=GF ID UvrD-helicase #=GF AC PF00580.22 #=GF DE UvrD/REP helicase N-terminal domain #=GF AU Bateman A;0000-0002-6982-4660 #=GF SE MRC-LMB Genome group. #=GF GA 23.00 23.00; #=GF TC 23.00 23.00; #=GF NC 22.90 22.90; #=GF BM hmmbuild HMM.ann SEED.ann #=GF SM hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq #=GF TP Domain #=GF RC Structure of Swiss:P09980 #=GF RN [1] #=GF RM 9288744 #=GF RT Major domain swiveling revealed by the crystal structures of #=GF RT complexes of E. coli Rep helicase 2009-04-03 · The stimulation is specific for UvrD, as UvrAB failed to stimulate Rep helicase, a UvrD homologue. Moreover, although UvrAB can promote limited strand displacement, stimulation of UvrD did not require the strand displacement function of UvrAB. We conclude that UvrAB, like MutL, modulate UvrD helicase activity. Escherichia coli UvrD is a superfamily 1 DNA helicase and single-stranded DNA (ssDNA) translocase that functions in DNA repair and plasmid replication and as an anti-recombinase by removing RecA protein from ssDNA. UvrD couples ATP binding and hydrolysis to unwind double-stranded DNA and translocate along ssDNA with 3'-to-5' directionality. However, there have been conflicting reports about the oligomeric state of the active helicase in vitro, some claiming that a UvrD monomer can function as a processive helicase 36,37, whereas Inactivation of the helicase function of UvrD.

We report here a series of crystal structures of the UvrD helicase complexed with DNA and ATP hydrolysis UvrD-like DNA helicase C-terminal domain profile. IPR014017: UvrD-like DNA helicase, C-terminal 289 566 25.557 Pfam PF00580 UvrD/REP helicase N-terminal domain IPR034739: UvrD/AddA helicase, N-terminal 12 273 6.4E-74 Gene3D G3DSA:1.10.486.10 384 UvrD, a highly conserved helicase involved in mismatch repair, nucleotide excision repair (NER), and recombinational repair, plays a critical role in maintaining genomic stability and facilitating DNA lesion repair in many prokaryotic species. Get the latest issue of Science delivered right to you! DNA helicases are motor proteins that function to unwind duplex (ds) DNA during DNA replication, recombination, and repair and are also UvrD is a helicase that is widely conserved in gram-negative bacteria. A uvrD homologue was identified in Mycobacterium tuberculosis on the basis of the homology of its encoded protein with Escherichia coli UvrD, with which it shares 39% amino acid identity, distributed throughout the protein. The gene was cloned, and a histidine-tagged form of the protein was expressed and purified to The PcrA/UvrD helicase functions in multiple path-ways that promote bacterial genome stability includ-ing the suppression of conﬂicts between replication and transcription and facilitating the repair of tran-scribed DNA. The reported ability of PcrA/UvrD to bind and backtrack RNA polymerase (1,2) might be UvrD-like helicase ATP-binding PROSITE-ProRule annotation.

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UvrD is a helicase and translocase that functions in excision repair to remove the damaged segment of DNA so that DNA polymerase can fill in the gap. Separation of the UvrD helicase and translocase activities is possible in vitro.

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UvrD is an abundant helicase in Escherichia coli with well characterized functions in mismatch and nucleotide excision repair and a possible role in displacement of proteins such as RecA from UvrD exhibits modest processivity as a DNA helicase (40–50 bp) (53– 55) making this protein an interesting choice for the helicase responsible for the unwinding event in MMR. UvrD is also the helicase responsible for the unwinding event associated with excision repair ( 56 – 59 ), which requires unwinding of a short 12–13 base long oligonucleotide well within the limits of the The closed conformation activates the helicase, but it can also generate super-helicases capable of unzipping long stretches of DNA at high speed and with considerable force. Comstock et al.

Although a UvrD monomer can translocate along single-stranded DNA, self UvrD, a ubiquitous bacterial helicase that plays important roles in multiple DNA metabolic pathways, is essential for genome stability and might, therefore, be crucial in bacterial physiology and pathogenesis. In this study, the functional characterization of UvrD helicase from Haemophilus influenzae and Helicobacter pylori is reported. Abstract. The PcrA/UvrD helicase functions in multiple pathways that promote bacterial genome stability including the suppression of conflicts between replication and transcription and facilitating the repair of transcribed DNA. 2012-05-09 · Translocation of UvrD. UvrD is a helicase and translocase that functions in excision repair to remove the damaged segment of DNA so that DNA polymerase can fill in the gap.
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Adding recF mutations almost completely suppresses AZT and partially suppresses UV and CFX sensitivity, suggesting RadA processes a class of intermediates that accumulate in uvrD mutants (PubMed: 25484163 ). 1 Publication 2018-10-19 · MutL functions as a processivity factor for UvrD helicase activity. UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair. The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination.

The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase: Authors: Sanders, K Lin, C-L Smith, AJ Cronin, N Fisher, G Eftychidis, V McGlynn, P Savery, NJ Wigley, DB Dillingham, MS: Item Type: Journal Article: Abstract: The structure and function of an RNA polymerase interaction domain in the PcrA/UvrD helicase Kelly Sanders, Chia Liang Lin, Abigail J. Smith , Nora Cronin, Gemma Fisher, Vasileios Eftychidis, Peter McGlynn, Nigel J. Savery , Dale B. Wigley, Mark S. Dillingham * The polarity of the helicase activity was determined to be 3'-5'. This domain is also found in subunit AddA of bacterial helicase-nuclease complex AddAB. The AddA subunit is the one responsible for the helicase activity [ (PUBMED:21071401) ].
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In this study, the functional characterization of UvrD helicase from Haemophilus influenzae and Helicobacter pylori is reported. UvrD, a ubiquitous bacterial helicase that plays important roles in multiple DNA metabolic pathways, is essential for genome stability and might, therefore, be crucial in bacterial physiology and pathogenesis. In this study, the func-tional characterization of UvrD helicase from Haemophilus inﬂuenzae and Helicobacter pylori is reported.

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1 Publication 2018-10-19 · MutL functions as a processivity factor for UvrD helicase activity. UvrD (DNA helicase II) has been implicated in DNA replication, DNA recombination, nucleotide excision repair, and methyl-directed mismatch repair. The enzymatic function of UvrD is to translocate along a DNA strand in a 3' to 5' direction and unwind duplex DNA utilizing a DNA-dependent ATPase activity. In addition, UvrD interacts with many other UvrD is a DNA helicase that participates in nucleotide excision repair and several replication-associated processes, including methyl-directed mismatch repair and recombination.