UniProtKB - P58301 (RAD50_PYRFU)
DNA double-strand break repair Rad50 ATPase
rad50
Functioni
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair (PubMed:11029422, PubMed:18957200).
The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200).
Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex (PubMed:24493214).
The ATP-bound conformation promotes DNA end binding and end tethering, and alters Mre11 nuclease activity (PubMed:24493214).
ATP hydrolysis promotes both Mre11 activity as well as HerA/NurA activity (PubMed:24493214).
Has also reversible adenylate kinase activity (PubMed:17349953).
4 PublicationsCofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 12 | ATPCombined sources3 Publications | 1 | |
Binding sitei | 140 | ATPCombined sources2 Publications | 1 | |
Metal bindingi | 444 | ZincUniRule annotation1 Publication | 1 | |
Metal bindingi | 447 | ZincUniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 32 – 38 | ATPCombined sources3 Publications | 7 | |
Nucleotide bindingi | 60 – 64 | ATPCombined sources3 Publications | 5 | |
Nucleotide bindingi | 763 – 764 | ATPCombined sources2 Publications | 2 | |
Nucleotide bindingi | 791 – 796 | ATPCombined sources2 Publications | 6 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-UniRule
- ATP hydrolysis activity Source: UniProtKB-UniRule
- identical protein binding Source: IntAct
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- double-strand break repair Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase |
Biological process | DNA damage, DNA repair |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: DNA double-strand break repair Rad50 ATPaseUniRule annotationCuratedAlternative name(s): pfRad501 Publication |
Gene namesi | Name:rad501 PublicationUniRule annotation Ordered Locus Names:PF1167 |
Organismi | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
Taxonomic identifieri | 186497 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 793 | S → R: Prevents ATP binding and disrupts the communication among the other ATP-binding loops. Prevents also Rad50 dimerization. Decreases both ATPase and adenylate kinase activities. 3 Publications | 1 | |
Mutagenesisi | 797 | R → G: Decreases ATP-induced dimerization. Increases DNA end tethering. 1 Publication | 1 | |
Mutagenesisi | 802 | L → W: Destabilizes the ATP-dimerized state. Promotes HerA/NurA activity. 1 Publication | 1 | |
Mutagenesisi | 805 | R → E: Increases ATP-induced dimerization. Increases DNA end tethering. Fails to promote HerA/NurA activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000138661 | 1 – 882 | DNA double-strand break repair Rad50 ATPaseAdd BLAST | 882 |
Proteomic databases
PRIDEi | P58301 |
Interactioni
Subunit structurei
Binary interactionsi
P58301
With | #Exp. | IntAct |
---|---|---|
mre11 [Q8U1N9] | 11 | EBI-2505704,EBI-2014945 |
itself | 4 | EBI-2505704,EBI-2505704 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
DIPi | DIP-54373N |
IntActi | P58301, 2 interactors |
MINTi | P58301 |
STRINGi | 186497.PF1167 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P58301 |
SMRi | P58301 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P58301 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 399 – 496 | Zinc-hookUniRule annotationAdd BLAST | 98 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 257 – 588 | UniRule annotationAdd BLAST | 332 | |
Coiled coili | 629 – 735 | UniRule annotationAdd BLAST | 107 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | arCOG00368, Archaea |
HOGENOMi | CLU_004785_0_2_2 |
OMAi | VNFIYGP |
OrthoDBi | 1771at2157 |
PhylomeDBi | P58301 |
Family and domain databases
CDDi | cd03240, ABC_Rad50, 1 hit |
Gene3Di | 3.40.50.300, 2 hits |
HAMAPi | MF_00449, RAD50, 1 hit |
InterProi | View protein in InterPro IPR045171, ABC_Rad50 IPR003959, ATPase_AAA_core IPR027417, P-loop_NTPase IPR038729, Rad50/SbcC_AAA IPR022982, Rad50_ATPase_archaeal IPR013134, Zn_hook_RAD50 |
Pfami | View protein in Pfam PF13304, AAA_21, 1 hit PF13476, AAA_23, 1 hit PF04423, Rad50_zn_hook, 1 hit |
SUPFAMi | SSF52540, SSF52540, 2 hits |
PROSITEi | View protein in PROSITE PS51131, ZN_HOOK, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MKLERVTVKN FRSHSDTVVE FKEGINLIIG QNGSGKSSLL DAILVGLYWP
60 70 80 90 100
LRIKDIKKDE FTKVGARDTY IDLIFEKDGT KYRITRRFLK GYSSGEIHAM
110 120 130 140 150
KRLVGNEWKH VTEPSSKAIS AFMEKLIPYN IFLNAIYIRQ GQIDAILESD
160 170 180 190 200
EAREKVVREV LNLDKFETAY KKLSELKKTI NNRIKEYRDI LARTENIEEL
210 220 230 240 250
IKENEQELIQ VLQEISKIEE VLPSKRSKVD MLRKEVLRLE ETKVEIENSE
260 270 280 290 300
RLLEKRRGDK RTLEERIKNT EEYLEKLKEK EKELEEQVKE ITSIKKDVDA
310 320 330 340 350
YLALKEFKNE YLDKKYKIEK ELTRVEELIN EIQKRIEELN EKESEKEKLE
360 370 380 390 400
NEKKEILNKL AILEKDHQLY EEIKAKKENL RQLKEKLGDK SPEDIKKLLE
410 420 430 440 450
ELETKKTTIE EERNEITQRI GELKNKIGDL KTAIEELKKA KGKCPVCGRE
460 470 480 490 500
LTDEHREELL SKYHLDLNNS KNTLAKLIDR KSELERELRR IDMEIKRLTP
510 520 530 540 550
LLTVAEQIRS IEEELNVVNL EKIEKNATEY EKLLEELRTL EGRIRGLAED
560 570 580 590 600
LKKLAPLEKK LAALIHKKQE LEKELKELNT KLESFGFKSV EDLDSKLREL
610 620 630 640 650
EEIYKRYLTL LNSKKELEIT QREIAKAKET LEMSFEELAE VEADIERIEK
660 670 680 690 700
KLSQLKQKYN EEEYKKKREE KEELEKELAR LEAQKKELEK RRDTIKSTLE
710 720 730 740 750
KLKAEKENRE RVKKEIKDLE KAKDFTEELI EKVKKYKALA REAALSKIGE
760 770 780 790 800
LASEIFAEFT EGKYSEVVVR AEENKVRLFV VWEGKERPLT FLSGGERIAL
810 820 830 840 850
GLAFRLAMSL YLAGEISLLI LDEPTPYLDE ERRRKLITIM ERYLKKIPQV
860 870 880
ILVSHDEELK DAADHVIRIS LENGSSKVEV VS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE009950 Genomic DNA Translation: AAL81291.1 |
RefSeqi | WP_011012307.1, NZ_CP023154.1 |
Genome annotation databases
EnsemblBacteriai | AAL81291; AAL81291; PF1167 |
GeneIDi | 41712975 |
KEGGi | pfu:PF1167 |
PATRICi | fig|186497.12.peg.1227 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE009950 Genomic DNA Translation: AAL81291.1 |
RefSeqi | WP_011012307.1, NZ_CP023154.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1F2T | X-ray | 1.60 | A | 1-149 | [»] | |
B | 735-882 | [»] | ||||
1F2U | X-ray | 1.60 | A/C | 1-149 | [»] | |
B/D | 735-882 | [»] | ||||
1II8 | X-ray | 3.02 | A | 1-195 | [»] | |
B | 709-882 | [»] | ||||
1L8D | X-ray | 2.20 | A/B | 396-506 | [»] | |
1US8 | X-ray | 2.10 | A | 1-147 | [»] | |
B | 739-882 | [»] | ||||
3QKR | X-ray | 3.40 | A | 1-195 | [»] | |
B | 704-882 | [»] | ||||
3QKS | X-ray | 2.10 | A | 1-195 | [»] | |
B | 704-882 | [»] | ||||
3QKT | X-ray | 1.90 | A/B/C/D | 1-177 | [»] | |
A/B/C/D | 726-882 | [»] | ||||
3QKU | X-ray | 3.30 | A/B | 1-187 | [»] | |
A/B | 716-882 | [»] | ||||
4NCH | X-ray | 2.30 | A/B | 1-177 | [»] | |
A/B | 726-882 | [»] | ||||
4NCI | X-ray | 2.30 | A | 1-177 | [»] | |
A | 726-882 | [»] | ||||
4NCJ | X-ray | 2.00 | A/B/C/D | 1-177 | [»] | |
A/B/C/D | 726-882 | [»] | ||||
4NCK | X-ray | 1.99 | A/B | 1-177 | [»] | |
A/B | 726-882 | [»] | ||||
6ZFF | X-ray | 3.00 | A/B | 378-516 | [»] | |
AlphaFoldDBi | P58301 | |||||
SMRi | P58301 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-54373N |
IntActi | P58301, 2 interactors |
MINTi | P58301 |
STRINGi | 186497.PF1167 |
Proteomic databases
PRIDEi | P58301 |
Genome annotation databases
EnsemblBacteriai | AAL81291; AAL81291; PF1167 |
GeneIDi | 41712975 |
KEGGi | pfu:PF1167 |
PATRICi | fig|186497.12.peg.1227 |
Phylogenomic databases
eggNOGi | arCOG00368, Archaea |
HOGENOMi | CLU_004785_0_2_2 |
OMAi | VNFIYGP |
OrthoDBi | 1771at2157 |
PhylomeDBi | P58301 |
Miscellaneous databases
EvolutionaryTracei | P58301 |
Family and domain databases
CDDi | cd03240, ABC_Rad50, 1 hit |
Gene3Di | 3.40.50.300, 2 hits |
HAMAPi | MF_00449, RAD50, 1 hit |
InterProi | View protein in InterPro IPR045171, ABC_Rad50 IPR003959, ATPase_AAA_core IPR027417, P-loop_NTPase IPR038729, Rad50/SbcC_AAA IPR022982, Rad50_ATPase_archaeal IPR013134, Zn_hook_RAD50 |
Pfami | View protein in Pfam PF13304, AAA_21, 1 hit PF13476, AAA_23, 1 hit PF04423, Rad50_zn_hook, 1 hit |
SUPFAMi | SSF52540, SSF52540, 2 hits |
PROSITEi | View protein in PROSITE PS51131, ZN_HOOK, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RAD50_PYRFU | |
Accessioni | P58301Primary (citable) accession number: P58301 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 26, 2001 |
Last sequence update: | September 26, 2001 | |
Last modified: | May 25, 2022 | |
This is version 151 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families