The domain within your query sequence starts at position 862 and ends at position 935; the E-value for the UvrD_C domain shown below is 1.7e-12.

DFAEYILGTVHKAKGLEFDTVHVLDDFVKVPCARHNLAQLPHFRVESFSEDEWNLLYVAV
TRAKKRLIMTKSLE

UvrD_C

UvrD_C
PFAM accession number:PF13361
Interpro abstract (IPR014017):

Helicases have been classified in 5 superfamilies (SF1-SF5) [(PUBMED:2546125)]. 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 [(PUBMED:2546125)]. For the two largest groups, commonly referred to as SF1 and SF2, a total of seven characteristic motifs have been identified [(PUBMED:2546125)] 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 [(PUBMED:10679457)]. Crystal structures of several uvrD-like DNA helicases have been solved [(PUBMED:9288744), (PUBMED:10199404), (PUBMED:15538360)]. They are monomeric enzymes consisting of two domains with a common alpha-beta 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 [(PUBMED:10199404)].

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'.

GO function:hydrolase activity (GO:0016787), ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry UvrD_C