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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei134 – 1341Proton donorBy similarity

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 nonhomologous end joining Source: PomBase
  • intra-S DNA damage checkpoint Source: PomBase
  • meiotic DNA double-strand break formation Source: PomBase
  • mitotic DNA damage checkpoint Source: PomBase
  • reciprocal meiotic recombination 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
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649DNA repair protein rad32PRO_0000138683Add
BLAST

Proteomic databases

MaxQBiQ09683.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi279207. 133 interactions.
DIPiDIP-52388N.
IntActiQ09683. 2 interactions.

Structurei

Secondary structure

1
649
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 236Combined sources
Turni29 – 335Combined sources
Turni35 – 395Combined sources
Helixi40 – 5415Combined sources
Beta strandi58 – 625Combined sources
Beta strandi67 – 715Combined sources
Helixi74 – 8815Combined sources
Beta strandi89 – 913Combined sources
Beta strandi97 – 1004Combined sources
Helixi115 – 1173Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi127 – 1293Combined sources
Helixi133 – 1353Combined sources
Helixi145 – 1517Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi172 – 1765Combined sources
Beta strandi179 – 1868Combined sources
Helixi191 – 1999Combined sources
Beta strandi203 – 2097Combined sources
Turni210 – 2145Combined sources
Beta strandi215 – 2239Combined sources
Beta strandi228 – 2336Combined sources
Helixi236 – 2383Combined sources
Beta strandi244 – 2507Combined sources
Beta strandi255 – 2617Combined sources
Turni262 – 2654Combined sources
Beta strandi266 – 2705Combined sources
Helixi281 – 2844Combined sources
Beta strandi288 – 2958Combined sources
Beta strandi298 – 3058Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi312 – 3187Combined sources
Helixi319 – 3213Combined sources
Beta strandi327 – 3293Combined sources
Helixi332 – 35827Combined sources
Beta strandi373 – 3797Combined sources
Turni381 – 3833Combined sources
Helixi389 – 3946Combined sources
Turni395 – 3995Combined sources
Beta strandi406 – 4105Combined sources

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the MRE11/RAD32 family.Curated

Phylogenomic databases

HOGENOMiHOG000216581.
InParanoidiQ09683.
KOiK10865.
OMAiRMFVNKQ.
OrthoDBiEOG7J187V.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
4FBKX-ray2.38A/B15-413[»]
4FBQX-ray2.50A/B15-413[»]
4FBWX-ray2.20A/B7-413[»]
4FCXX-ray3.00A/B15-413[»]
ProteinModelPortaliQ09683.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279207. 133 interactions.
DIPiDIP-52388N.
IntActiQ09683. 2 interactions.

Proteomic databases

MaxQBiQ09683.

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.
OMAiRMFVNKQ.
OrthoDBiEOG7J187V.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterisation of the Schizosaccharomyces pombe rad32 gene: a gene required for repair of double strand breaks and recombination."
    Tavassoli M., Shayeghi M., Nasim A., Watts F.Z.
    Nucleic Acids Res. 23:383-388(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "The fission yeast Rad32 (Mre11)-Rad50-Nbs1 complex is required for the S-phase DNA damage checkpoint."
    Chahwan C., Nakamura T.M., Sivakumar S., Russell P., Rhind N.
    Mol. Cell. Biol. 23:6564-6573(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.

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: June 8, 2016
This is version 131 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.