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Protein

Holliday junction ATP-dependent DNA helicase RuvB

Gene

ruvB

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvB is a Mg2+-dependent, DNA-dependent ATPase with an equal preference for supercoiled and linear duplex DNA. It can promote Holliday junction migration alone.

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Enzyme regulationi

The activity of RuvB is enhanced by RuvA.

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi45 – 52ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase
Biological processDNA damage, DNA recombination, DNA repair, SOS response
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Holliday junction ATP-dependent DNA helicase RuvBUniRule annotation (EC:3.6.4.12UniRule annotation)
Gene namesi
Name:ruvBUniRule annotation
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001656201 – 324Holliday junction ATP-dependent DNA helicase RuvBAdd BLAST324

Interactioni

Subunit structurei

Forms a complex with RuvA.

Protein-protein interaction databases

DIPiDIP-41108N

Structurei

3D structure databases

ProteinModelPortaliQ56214
SMRiQ56214
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuvB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CKJ Bacteria
COG2255 LUCA

Family and domain databases

Gene3Di1.10.10.10, 1 hit
HAMAPiMF_00016 DNA_helic_RuvB, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR004605 DNA_helicase_Holl-junc_RuvB
IPR008823 DNA_helicase_Holl-junc_RuvB_C
IPR027417 P-loop_NTPase
IPR008824 RuvB_N
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR42848 PTHR42848, 1 hit
PfamiView protein in Pfam
PF05491 RuvB_C, 1 hit
PF05496 RuvB_N, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005323 DNA_helicase_Holl-junc_RuvB_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00635 ruvB, 1 hit

Sequencei

Sequence statusi: Complete.

Q56214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDLALRPKT LDEYIGQERL KQKLRVYLEA AKARKEPLEH LLLFGPPGLG
60 70 80 90 100
KTTLAHVIAH ELGVNLRVTS GPAIEKPGDL AAILANSLEE GDILFIDEIH
110 120 130 140 150
RLSRQAEEHL YPAMEDFVMD IVIGQGPAAR TIRLELPRFA LIGATTRPGL
160 170 180 190 200
ITAPLLSRFG IVEHLEYYTP EELAQGVMRD ARLLGVRITE EAALEIGRRS
210 220 230 240 250
RGTMRVAKRL FRRVRDFAQV EGEEVITRER ALEALAALGL DELGLEKRDR
260 270 280 290 300
EILEVLILRF GAGPVGLATL ATALSEDPGT LEEVHEPYLI RQGLLKRTPR
310 320
GRVATELAYR HLGYPPPVGP LLEP
Length:324
Mass (Da):36,016
Last modified:November 1, 1997 - v1
Checksum:i1B0DB92F373185CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22817 Genomic DNA Translation: AAB03726.2
PIRiT11851

Similar proteinsi

Entry informationi

Entry nameiRUVB_THETH
AccessioniPrimary (citable) accession number: Q56214
Secondary accession number(s): Q9RA64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 23, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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