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Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51198 Retrieve the sequence logo from the alignment.Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits: Domain architecture view of Swiss-Prot proteins matching PS51198.Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51198: Undetected by PS51198: 8 ( 8 false negatives and 0 ' partial') Sequences in UniProtKB/Swiss-Prot known to belong to this class: 267ĭetected by PS51198: 259 (true positives) PROSITE methods (with tools and information) covered by this documentation: UVRD_HELICASE_ATP_BIND, PS51198 UvrD-like DNA helicase ATP-binding domain profile (MATRIX) One recognizes the ATP-binding domain, whereas the second one is directed To recognize uvrD-like DNA helicases we have developed two profiles. The polarity of the helicase activity was determined to be 3'-5'. Fungal srs2 proteins, an ATP-dependent DNA helicase involved in DNA repair.Processes DNA ends resulting from a double-strand break. RecBCD is a multi-functional enzyme complex that Bacterial helicase IV (helD gene product).To the single-stranded DNA and acts in a progressive fashion along the DNA Bacterial rep proteins, a single-stranded DNA-dependent ATPase involved inĭNA replication which can initiate unwinding at a nick in the DNA.Helicase has both 5'-3' and 3'-5' helicase activities. Gram-positive bacterial pcrA helicase, an essential enzyme involved in DNA.Initiates unwinding most effectively when a single-stranded region is It unwindsĭNA duplexes with 3'-5' polarity with respect to the bound strand and
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Nucleotide excision repair and methyl-directed mismatch repair. It is involved in the post-incision events of
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Some proteins that belong to the uvrD-like DNA helicase family are listed This "domain swiveling" was proposed to be an importantĪspect of the mechanism of the enzyme. The conformational difference between the twoįorms comprises a large rotation of the end of the C-terminal domain byĪpproximately 130°. The enzyme crystallizes in two differentĬonformations (open and closed). Situated in a cleft between the N-terminus of the ATP-binding domain and theīeginning of the C-terminal domain. They are monomeric enzymes consisting of twoĭomains with a common α-β RecA-like core. UvrD-like DNA helicases unwind DNA with aĬrystal structures of several uvrD-like DNA helicases have been solved (seeįor example ). UvrD-like DNA helicasesīelong to SF1, but they differ from classical SF1/SF2 (see ) by a N-terminal ATP-binding domain and a C-terminal domain. Identified which are distributed over two structural domains, an Referred to as SF1 and SF2, a total of seven characteristic motifs have been (phosphate-binding loop or P-loop) (see ) and Walker B Proteins bind ATP and, consequently, all of them carry the classical Walker A Helicases have been classified in 5 superfamilies (SF1-SF5).