General information | DisProt: | DP00684 | Name: | DNA helicase II | Synonym(s): | UVRD_ECOLI
DNA helicase II
| First appeared in release: | Release 5.2 (08/07/2010) | UniProt: | P03018 | UniGene: | | SwissProt: | UVRD_ECOLI | TrEMBL: | | NCBI (GI): | 137194 | Source organism: | Escherichia coli (strain K12) | Sequence length: | 720 | Percent disordered: | 10% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MDVSYLLDSL NDKQREAVAA PRSNLLVLAG AGSGKTRVLV HRIAWLMSVE NCSPYSIMAV - 60 TFTNKAAAEM RHRIGQLMGT SQGGMWVGTF HGLAHRLLRA HHMDANLPQD FQILDSEDQL - 120 RLLKRLIKAM NLDEKQWPPR QAMWYINSQK DEGLRPHHIQ SYGNPVEQTW QKVYQAYQEA - 180 CDRAGLVDFA ELLLRAHELW LNKPHILQHY RERFTNILVD EFQDTNNIQY AWIRLLAGDT - 240 GKVMIVGDDD QSIYGWRGAQ VENIQRFLND FPGAETIRLE QNYRSTSNIL SAANALIENN - 300 NGRLGKKLWT DGADGEPISL YCAFNELDEA RFVVNRIKTW QDNGGALAEC AILYRSNAQS - 360 RVLEEALLQA SMPYRIYGGM RFFERQEIKD ALSYLRLIAN RNDDAAFERV VNTPTRGIGD - 420 RTLDVVRQTS RDRQLTLWQA CRELLQEKAL AGRAASALQR FMELIDALAQ ETADMPLHVQ - 480 TDRVIKDSGL RTMYEQEKGE KGQTRIENLE ELVTATRQFS YNEEDEDLMP LQAFLSHAAL - 540 EAGEGQADTW QDAVQLMTLH SAKGLEFPQV FIVGMEEGMF PSQMSLDEGG RLEEERRLAY - 600 VGVTRAMQKL TLTYAETRRL YGKEVYHRPS RFIGELPEEC VEEVRLRATV SRPVSHQRMG - 660 TPMVENDSGY KLGQRVRHAK FGEGTIVNME GSGEHSRLQV AFQGQGIKWL VAAYARLESV - 720
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Functional narrative |
Has both ATPase and helicase activities. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand and initiates unwinding most effectively when a single-stranded region is present. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair. Belongs to the helicase family. UvrD subfamily
Contains 1 uvrD-like helicase ATP-binding domain.
Contains 1 uvrD-like helicase C-terminal domain.
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Map of ordered and disordered regions |
![](regions/DP00684.gif)
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Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | C-terminal | Location: | 495 - 564 | Length: | 70 | Region sequence: |
EQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAV QLMTLHSAKG | Modification type: | Native
| PDB: | 2IS2:A, 2IS2:B | Structural/functional type: | Relationship to function unknown | Functional classes: | | Functional subclasses: | Intraprotein interaction
Protein-DNA binding
| Detection methods:
- X-ray crystallography (277 K; pH: 8; DTT (buffer) 1 mM; EDTA (buffer) 0.1 mM; ethylmercury phosphate 0.6 mM; glycerol (buffer) 5 %; KCl (buffer) 150 mM; MgCl2 (buffer) 5 mM; protein 6 mg/mL; Tris (buffer) 20 mM)
| References:
- Lee, J.Y. and W. Yang. "UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke." Cell. 2006; 127(7): 13491360. PubMed: 17190599
- Manelytea, Laura, Colin P. Guyb, Rachel M. Smitha, Mark S. Dillinghama, Peter McGlynnb and Nigel J. Savery. "The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair." DNA Repair (Amst). 2009; 8: 1300-1310. PubMed: 19762288
| Comments:
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References |
- Manelytea, Laura, Colin P. Guyb, Rachel M. Smitha, Mark S. Dillinghama, Peter McGlynnb and Nigel J. Savery. "The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair." DNA Repair (Amst). 2009; 8: 1300-1310. PubMed: 19762288
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Comments |
AV (8-3-2010) PubMed: 19762288
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