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Protein

DNA repair and recombination protein RadA

Gene

radA

Organism
Methanococcus voltae
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1128ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.B7. 3268.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair and recombination protein RadA
Gene namesi
Name:radA
OrganismiMethanococcus voltae
Taxonomic identifieri2188 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322DNA repair and recombination protein RadAPRO_0000150099Add
BLAST

Interactioni

Protein-protein interaction databases

DIPiDIP-29120N.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Helixi13 – 2210Combined sources
Helixi27 – 315Combined sources
Helixi35 – 395Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 5914Combined sources
Turni61 – 633Combined sources
Helixi68 – 747Combined sources
Helixi85 – 906Combined sources
Beta strandi93 – 964Combined sources
Beta strandi99 – 1068Combined sources
Helixi111 – 12111Combined sources
Helixi125 – 1273Combined sources
Turni132 – 1343Combined sources
Turni137 – 1404Combined sources
Beta strandi141 – 15212Combined sources
Helixi156 – 16611Combined sources
Helixi170 – 1756Combined sources
Beta strandi177 – 1815Combined sources
Helixi185 – 1939Combined sources
Helixi195 – 2006Combined sources
Beta strandi204 – 2118Combined sources
Helixi215 – 2206Combined sources
Turni224 – 2263Combined sources
Helixi227 – 24721Combined sources
Beta strandi251 – 2566Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi271 – 2744Combined sources
Helixi275 – 2817Combined sources
Beta strandi283 – 2908Combined sources
Beta strandi295 – 3028Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi309 – 3168Combined sources
Beta strandi319 – 3213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T4GX-ray2.00A1-322[»]
1XU4X-ray2.40A1-322[»]
2B21X-ray2.40A1-322[»]
2F1HX-ray2.70A1-322[»]
2F1IX-ray2.90A1-322[»]
2F1JX-ray2.30A1-322[»]
2FPKX-ray2.10A1-322[»]
2FPLX-ray2.30A1-322[»]
2FPMX-ray2.00A1-322[»]
2GDJX-ray2.50A63-322[»]
2I1QX-ray1.90A1-322[»]
3FYHX-ray1.90A1-322[»]
3NTUX-ray1.90A4-322[»]
4DC9X-ray2.60A/B/C/D/E/F61-322[»]
4QKQX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L61-322[»]
ProteinModelPortaliO73948.
SMRiO73948. Positions 5-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO73948.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00348. RadA_arch.
InterProiIPR003593. AAA+_ATPase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR011938. DNA_recomb/repair_RadA.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02236. recomb_radA. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O73948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNLTDLPG VGPSTAEKLV EAGYIDFMKI ATATVGELTD IEGISEKAAA
60 70 80 90 100
KMIMGARDLC DLGFKSGIDL LKQRSTVWKL STSSSELDSV LGGGLESQSV
110 120 130 140 150
TEFAGVFGSG KTQIMHQSCV NLQNPEFLFY DEEAVSKGEV AQPKAVYIDT
160 170 180 190 200
EGTFRPERIM QMAEHAGIDG QTVLDNTFVA RAYNSDMQML FAEKIEDLIQ
210 220 230 240 250
EGNNIKLVVI DSLTSTFRNE YTGRGKLAER QQKLGRHMAT LNKLADLFNC
260 270 280 290 300
VVLVTNQVSA KPDAFFGMAE QAIGGHIVGH AATFRFFVRK GKGDKRVAKL
310 320
YDSPHLPDAE AIFRITEKGI QD
Length:322
Mass (Da):35,189
Last modified:November 1, 1998 - v1
Checksum:i8A9F5EFB927344B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008421 Genomic DNA. Translation: AAC23499.1.
AF090200 Genomic DNA. Translation: AAD16066.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008421 Genomic DNA. Translation: AAC23499.1.
AF090200 Genomic DNA. Translation: AAD16066.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T4GX-ray2.00A1-322[»]
1XU4X-ray2.40A1-322[»]
2B21X-ray2.40A1-322[»]
2F1HX-ray2.70A1-322[»]
2F1IX-ray2.90A1-322[»]
2F1JX-ray2.30A1-322[»]
2FPKX-ray2.10A1-322[»]
2FPLX-ray2.30A1-322[»]
2FPMX-ray2.00A1-322[»]
2GDJX-ray2.50A63-322[»]
2I1QX-ray1.90A1-322[»]
3FYHX-ray1.90A1-322[»]
3NTUX-ray1.90A4-322[»]
4DC9X-ray2.60A/B/C/D/E/F61-322[»]
4QKQX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L61-322[»]
ProteinModelPortaliO73948.
SMRiO73948. Positions 5-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29120N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.6.4.B7. 3268.

Miscellaneous databases

EvolutionaryTraceiO73948.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00348. RadA_arch.
InterProiIPR003593. AAA+_ATPase.
IPR013632. DNA_recomb/repair_Rad51_C.
IPR011938. DNA_recomb/repair_RadA.
IPR016467. DNA_recomb/repair_RecA-like.
IPR010995. DNA_repair_Rad51/TF_NusA_a-hlx.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR027417. P-loop_NTPase.
IPR020588. RecA_ATP-bd.
IPR020587. RecA_monomer-monomer_interface.
[Graphical view]
PfamiPF08423. Rad51. 1 hit.
[Graphical view]
PIRSFiPIRSF005856. Rad51. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00278. HhH1. 2 hits.
[Graphical view]
SUPFAMiSSF47794. SSF47794. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR02236. recomb_radA. 1 hit.
PROSITEiPS50162. RECA_2. 1 hit.
PS50163. RECA_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The RadA protein from the archaeon Methanococcus voltae: a functional homolog of eukaryotic Rad51."
    Reich C.I., Buldak G.L., McNeil L.K.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 33273 / DSM 1537 / NBRC 100457 / OCM 70 / PS.
  2. "Diversity of radA genes from cultured and uncultured archaea: comparative analysis of putative RadA proteins and their use as a phylogenetic marker."
    Sandler S.J., Hugenholtz P., Schleper C., DeLong E.F., Pace N.R., Clark A.J.
    J. Bacteriol. 181:907-915(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 112-254.

Entry informationi

Entry nameiRADA_METVO
AccessioniPrimary (citable) accession number: O73948
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1998
Last modified: April 13, 2016
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.