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Protein

DNA repair protein rad32

Gene

rad32

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the repair of double strand breaks (DSB) caused by gamma and UV radiation. May work in conjunction with rhp51.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei134Proton donorBy similarity1

GO - Molecular functioni

  • double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: PomBase
  • manganese ion binding Source: PomBase
  • nuclease activity Source: PomBase
  • single-stranded DNA 3'-5' exodeoxyribonuclease activity Source: PomBase
  • single-stranded DNA endodeoxyribonuclease activity Source: PomBase

GO - Biological processi

  • cellular protein localization Source: PomBase
  • DNA double-strand break processing Source: PomBase
  • double-strand break repair Source: PomBase
  • double-strand break repair involved in meiotic recombination Source: PomBase
  • double-strand break repair via homologous recombination Source: PomBase
  • double-strand break repair via nonhomologous end joining Source: PomBase
  • intra-S DNA damage checkpoint Source: PomBase
  • meiotic DNA double-strand break formation Source: PomBase
  • reciprocal meiotic recombination Source: PomBase
  • telomere maintenance Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair, Meiosis

Keywords - Ligandi

Manganese

Enzyme and pathway databases

ReactomeiR-SPO-1834949. Cytosolic sensors of pathogen-associated DNA.
R-SPO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SPO-5693548. Sensing of DNA Double Strand Breaks.
R-SPO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein rad32
Gene namesi
Name:rad32
ORF Names:SPAC13C5.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC13C5.07.
PomBaseiSPAC13C5.07.

Subcellular locationi

GO - Cellular componenti

  • Mre11 complex Source: PomBase
  • nuclear chromosome, telomeric region Source: PomBase
  • site of double-strand break Source: PomBase
  • subtelomeric heterochromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001386831 – 649DNA repair protein rad32Add BLAST649

Proteomic databases

MaxQBiQ09683.
PRIDEiQ09683.

Interactioni

Subunit structurei

Associates with nbn. Forms a multisubunit endonuclease complex, MRN, together with nbn and rad50.1 Publication

Protein-protein interaction databases

BioGridi279207. 134 interactors.
DIPiDIP-52388N.
IntActiQ09683. 2 interactors.

Structurei

Secondary structure

1649
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 23Combined sources6
Turni29 – 33Combined sources5
Turni35 – 39Combined sources5
Helixi40 – 54Combined sources15
Beta strandi58 – 62Combined sources5
Beta strandi67 – 71Combined sources5
Helixi74 – 88Combined sources15
Beta strandi89 – 91Combined sources3
Beta strandi97 – 100Combined sources4
Helixi115 – 117Combined sources3
Beta strandi123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Helixi133 – 135Combined sources3
Helixi145 – 151Combined sources7
Beta strandi154 – 157Combined sources4
Beta strandi167 – 169Combined sources3
Beta strandi172 – 176Combined sources5
Beta strandi179 – 186Combined sources8
Helixi191 – 199Combined sources9
Beta strandi203 – 209Combined sources7
Turni210 – 214Combined sources5
Beta strandi215 – 223Combined sources9
Beta strandi228 – 233Combined sources6
Helixi236 – 238Combined sources3
Beta strandi244 – 250Combined sources7
Beta strandi255 – 261Combined sources7
Turni262 – 265Combined sources4
Beta strandi266 – 270Combined sources5
Helixi281 – 284Combined sources4
Beta strandi288 – 295Combined sources8
Beta strandi298 – 305Combined sources8
Beta strandi307 – 309Combined sources3
Beta strandi312 – 318Combined sources7
Helixi319 – 321Combined sources3
Beta strandi327 – 329Combined sources3
Helixi332 – 358Combined sources27
Beta strandi373 – 379Combined sources7
Turni381 – 383Combined sources3
Helixi389 – 394Combined sources6
Turni395 – 399Combined sources5
Beta strandi406 – 410Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FBKX-ray2.38A/B15-413[»]
4FBQX-ray2.50A/B15-413[»]
4FBWX-ray2.20A/B7-413[»]
4FCXX-ray3.00A/B15-413[»]
ProteinModelPortaliQ09683.
SMRiQ09683.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MRE11/RAD32 family.Curated

Phylogenomic databases

HOGENOMiHOG000216581.
InParanoidiQ09683.
KOiK10865.
OMAiNSRQPEK.
OrthoDBiEOG092C2IFF.
PhylomeDBiQ09683.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR003701. Mre11.
IPR007281. Mre11_DNA-bd.
[Graphical view]
PANTHERiPTHR10139:SF1. PTHR10139:SF1. 1 hit.
PfamiPF00149. Metallophos. 1 hit.
PF04152. Mre11_DNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF000882. DSB_repair_MRE11. 1 hit.
SMARTiSM01347. Mre11_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
TIGRFAMsiTIGR00583. mre11. 1 hit.

Sequencei

Sequence statusi: Complete.

Q09683-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNDPSDMNN ELHNENTIRI LISSDPHVGY GEKDPVRGND SFVSFNEILE
60 70 80 90 100
IARERDVDMI LLGGDIFHDN KPSRKALYQA LRSLRLNCLG DKPCELELLS
110 120 130 140 150
DTSLTTGDTA VCNINYLDPN INVAIPVFSI HGNHDDPSGD GRYSALDILQ
160 170 180 190 200
VTGLVNYFGR VPENDNIVVS PILLQKGFTK LALYGISNVR DERLYHSFRE
210 220 230 240 250
NKVKFLRPDL YRDEWFNLLT VHQNHSAHTP TSYLPESFIQ DFYDFVLWGH
260 270 280 290 300
EHECLIDGSY NPTQKFTVVQ PGSTIATSLS PGETAPKHCG ILNITGKDFH
310 320 330 340 350
LEKIRLRTVR PFIMKDIILS EVSSIPPMVE NKKEVLTYLI SKVEEAITEA
360 370 380 390 400
NAQWYEAQGT VPVVENEKPP LPLIRLRVDY TGGYQTENPQ RFSNRFVGRV
410 420 430 440 450
ANATDVVQFY LKKKYTRSKR NDGLYTSAVE DIKINSLRVE SLVNEYLKTN
460 470 480 490 500
RLECLPEDSL GEAVVNFVEK DDRDAIKECV ETQLNKQINL LVKKRVTEEN
510 520 530 540 550
LEQEISSIIN DLPKISTTKR KDYEELPEEV SETSINIAEH TPVLKHTSSL
560 570 580 590 600
LDHHSPLATS SSEHEMEATP SPALLKKTNK RRELPSSLTK KNTRTPQRSK
610 620 630 640
EVKKVPARKL SQSTKKSDKN TQSTLLFYDP SSTTEAQYLD NEDDEILDD
Length:649
Mass (Da):73,689
Last modified:November 1, 1995 - v1
Checksum:i400B349EF4FA3428
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82322 Genomic DNA. Translation: CAA57765.1. Different termination.
CU329670 Genomic DNA. Translation: CAA90458.1.
PIRiS58097.
RefSeqiNP_592935.1. NM_001018336.2.

Genome annotation databases

EnsemblFungiiSPAC13C5.07.1; SPAC13C5.07.1:pep; SPAC13C5.07.
GeneIDi2542757.
KEGGispo:SPAC13C5.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82322 Genomic DNA. Translation: CAA57765.1. Different termination.
CU329670 Genomic DNA. Translation: CAA90458.1.
PIRiS58097.
RefSeqiNP_592935.1. NM_001018336.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4FBKX-ray2.38A/B15-413[»]
4FBQX-ray2.50A/B15-413[»]
4FBWX-ray2.20A/B7-413[»]
4FCXX-ray3.00A/B15-413[»]
ProteinModelPortaliQ09683.
SMRiQ09683.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279207. 134 interactors.
DIPiDIP-52388N.
IntActiQ09683. 2 interactors.

Proteomic databases

MaxQBiQ09683.
PRIDEiQ09683.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC13C5.07.1; SPAC13C5.07.1:pep; SPAC13C5.07.
GeneIDi2542757.
KEGGispo:SPAC13C5.07.

Organism-specific databases

EuPathDBiFungiDB:SPAC13C5.07.
PomBaseiSPAC13C5.07.

Phylogenomic databases

HOGENOMiHOG000216581.
InParanoidiQ09683.
KOiK10865.
OMAiNSRQPEK.
OrthoDBiEOG092C2IFF.
PhylomeDBiQ09683.

Enzyme and pathway databases

ReactomeiR-SPO-1834949. Cytosolic sensors of pathogen-associated DNA.
R-SPO-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SPO-5693548. Sensing of DNA Double Strand Breaks.
R-SPO-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Miscellaneous databases

PROiQ09683.

Family and domain databases

Gene3Di3.60.21.10. 2 hits.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
IPR003701. Mre11.
IPR007281. Mre11_DNA-bd.
[Graphical view]
PANTHERiPTHR10139:SF1. PTHR10139:SF1. 1 hit.
PfamiPF00149. Metallophos. 1 hit.
PF04152. Mre11_DNA_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF000882. DSB_repair_MRE11. 1 hit.
SMARTiSM01347. Mre11_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 2 hits.
TIGRFAMsiTIGR00583. mre11. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRAD32_SCHPO
AccessioniPrimary (citable) accession number: Q09683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.