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Protein

DNA repair protein rad50

Gene

rad50

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

Involved in DNA double-strand break (DSB) repair. Involved in mating type switching and has a role in choosing the sister chromatid for recombinational repair. Also has a role in telomere length maintenance.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per homodimer.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi674 – 6741ZincPROSITE-ProRule annotation
Metal bindingi677 – 6771ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 418ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: PomBase
  • DNA binding Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • DNA duplex unwinding Source: GOC
  • double-strand break repair involved in meiotic recombination Source: PomBase
  • double-strand break repair via homologous recombination Source: PomBase
  • gene conversion at mating-type locus, DNA repair synthesis Source: PomBase
  • homologous recombination-dependent replication fork processing 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
  • telomere maintenance Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Meiosis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-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 rad50 (EC:3.6.-.-)
Gene namesi
Name:rad50
ORF Names:SPAC1556.01c, SPAP4C9.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.01c.
PomBaseiSPAC1556.01c. rad50.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12851285DNA repair protein rad50PRO_0000138647Add
BLAST

Proteomic databases

MaxQBiQ9UTJ8.

Interactioni

Subunit structurei

Heterodimer (By similarity). Interacts with the rad21 cohesin complex. Forms a multisubunit endonuclease complex, MRN, together with nbn and rad32.By similarity2 Publications

Protein-protein interaction databases

BioGridi278131. 26 interactions.
DIPiDIP-52389N.
IntActiQ9UTJ8. 1 interaction.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini630 – 72697Zinc-hookPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili295 – 36571Sequence analysisAdd
BLAST
Coiled coili630 – 66839Sequence analysisAdd
BLAST
Coiled coili698 – 72629Sequence analysisAdd
BLAST
Coiled coili727 – 80983Sequence analysisAdd
BLAST
Coiled coili814 – 90289Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1182 – 121938Ala/Asp-rich (DA-box)Add
BLAST

Domaini

The zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another rad50 molecule, thereby forming a V-shaped homodimer.By similarity

Sequence similaritiesi

Belongs to the SMC family. RAD50 subfamily.Curated
Contains 1 zinc-hook domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000192269.
InParanoidiQ9UTJ8.
KOiK10866.
OrthoDBiEOG74BK1D.
PhylomeDBiQ9UTJ8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
SUPFAMiSSF52540. SSF52540. 5 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UTJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCIDRMSIM GIRSFDNRSR ESIQFFSPLT LIVGQNGSGK TTIIECLKYA
60 70 80 90 100
TTGILPPNTK GGAFIHDPKI CGEKEVLAQV KLAFRNTNQV KMICTRSLQL
110 120 130 140 150
SVKKTTRQQK TLDGQLLILK DNERTTISNR CAELDSQVPL SLGVSKALLD
160 170 180 190 200
YVIFCHQEES FWPLSEPANL KKRFDEIFES LRYAKALDQI KGLKRDQETQ
210 220 230 240 250
VKVDQATLTH YRSDKERAEK IELRVHESLK RISCIRSKVE ELDQEITETA
260 270 280 290 300
RLQDELFKST EEYEQQMITI RHLESQSDII NTTINDLKSQ MTITDESSED
310 320 330 340 350
LEKLHSNFAE KVKEEQELYK SLEKKRSDLE SLLKSRRELL EKLTGDLGKI
360 370 380 390 400
QGEIESLEKL KVKKSTMINE IVHRYNINEI NEEGIMTEVS KYASLVNKNY
410 420 430 440 450
EISSGKLKER QVAVRARIEG IKAHEMFLNN RVSEINSSLE KQLTTQKELR
460 470 480 490 500
SRFEILFPVK LQREDFTKDV EKSDLWIKSL RQEYESKNLL ELLDKHQTAL
510 520 530 540 550
SSVENRLDEI SEIVDSYHKY SGVRTKLQVF EENKTNKSAI LANQLMTLKS
560 570 580 590 600
SFSEVMSYEL KDDDNYNEEL DKLVEDVRKK LQEKEEAESS LRSVRERLEI
610 620 630 640 650
RISLSVQSIN DLTENKKIKT KTLKSYSGTF ASMISEIKAL ESEIEENRKT
660 670 680 690 700
LHSLQFGSTF YEKAIEICVD QHACQLCQRS LDKEEEKLFV EHCHSMIDVI
710 720 730 740 750
PSKSAEVYSH LETLTKTFKN LSEAKPIFDE IELLDKRLSE TKTELSDLQG
760 770 780 790 800
DLQGLDIRKD EIQSELDTLY LRRANLEKLQ LLVKDISNLE EEIRTIDRET
810 820 830 840 850
EVLRIELPSS IAHHNLDEIY AEREKLLEKR GYLRKQIERT KLEETSFKKK
860 870 880 890 900
IDDAVLANNE QKLKLTKLNF QVNELEQLEK DINKSSEDCD LQKKKLLEVS
910 920 930 940 950
SKQGSQAPFL NELESEYEKL EADIQEMAQK SRTEILEANE YLHQLNEWNS
960 970 980 990 1000
ELRIDVSTKF KCIKEKKSNI GEEVRIIASK IESTDDNLRK LQERLADLRT
1010 1020 1030 1040 1050
RERNASDNLR LRALMRQLEE AVTQKNYLLS QQSHDDRESF RERMQILKSK
1060 1070 1080 1090 1100
YGALNAERAG LLGECKQLEN SITKDKEELN MEFKDADERF RRQLIKTKTT
1110 1120 1130 1140 1150
GKANEDLGKY AKALDVAIMQ LHSMKMNEIN RIVDELWKQT YCGTDIDTIL
1160 1170 1180 1190 1200
IRSDSEGKGN RTYNYRVCMV KGDAELDMRG RCSAGQKVLA CIIIRLALAE
1210 1220 1230 1240 1250
CLGVNCGILA LDEPTTNLDE ENICSLAKNL SRIVEFRRKQ ANFQLIVITH
1260 1270 1280
DEQFIRLVNS DAYCSYYYRV KRDTNQKSMI VKEPL
Length:1,285
Mass (Da):149,029
Last modified:September 22, 2009 - v3
Checksum:iDF45B2EAE7097295
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB96041.3.
PIRiT50080.
RefSeqiXP_001713090.2. XM_001713038.3.

Genome annotation databases

EnsemblFungiiSPAC1556.01c.1; SPAC1556.01c.1:pep; SPAC1556.01c.
GeneIDi2541635.
KEGGispo:SPAC1556.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB96041.3.
PIRiT50080.
RefSeqiXP_001713090.2. XM_001713038.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278131. 26 interactions.
DIPiDIP-52389N.
IntActiQ9UTJ8. 1 interaction.

Proteomic databases

MaxQBiQ9UTJ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1556.01c.1; SPAC1556.01c.1:pep; SPAC1556.01c.
GeneIDi2541635.
KEGGispo:SPAC1556.01c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.01c.
PomBaseiSPAC1556.01c. rad50.

Phylogenomic databases

HOGENOMiHOG000192269.
InParanoidiQ9UTJ8.
KOiK10866.
OrthoDBiEOG74BK1D.
PhylomeDBiQ9UTJ8.

Enzyme and pathway databases

ReactomeiR-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

PROiQ9UTJ8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027417. P-loop_NTPase.
IPR004584. Rad50_eukaryotes.
IPR013134. Zn_hook_RAD50.
[Graphical view]
PANTHERiPTHR18867. PTHR18867. 1 hit.
SUPFAMiSSF52540. SSF52540. 5 hits.
TIGRFAMsiTIGR00606. rad50. 1 hit.
PROSITEiPS51131. ZN_HOOK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fission yeast Rad50 stimulates sister chromatid recombination and links cohesion with repair."
    Hartsuiker E., Vaessen E., Carr A.M., Kohli J.
    EMBO J. 20:6660-6671(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RAD21 COHESIN COMPLEX.
  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 nameiRAD50_SCHPO
AccessioniPrimary (citable) accession number: Q9UTJ8
Secondary accession number(s): Q9P3T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.