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Protein

DNA repair helicase rad15

Gene

rad15

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

ATP-dependent DNA helicase involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents (PubMed:1534406, PubMed:8960127). Necessary for excision of pyrimidine dimers. Also unwinds DNA/RNA duplexes. Plays an essential role in the cell viability (By similarity).By similarity2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.By similarity

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi115 – 1151Iron-sulfur (4Fe-4S)By similarity
Metal bindingi133 – 1331Iron-sulfur (4Fe-4S)By similarity
Metal bindingi154 – 1541Iron-sulfur (4Fe-4S)By similarity
Metal bindingi189 – 1891Iron-sulfur (4Fe-4S)By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 498ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • nucleotide-excision repair, DNA duplex unwinding Source: PomBase
  • transcription initiation from RNA polymerase II promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-113418. Formation of the Early Elongation Complex.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-674695. RNA Polymerase II Pre-transcription Events.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-72086. mRNA Capping.
R-SPO-73776. RNA Polymerase II Promoter Escape.
R-SPO-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SPO-75953. RNA Polymerase II Transcription Initiation.
R-SPO-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-SPO-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair helicase rad151 Publication (EC:3.6.4.12)
Alternative name(s):
DNA repair helicase RAD3 homolog1 Publication
Protein rhp31 Publication
Gene namesi
Name:rad151 Publication
Synonyms:rad51 Publication, rhp31 Publication
ORF Names:SPAC1D4.12Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1D4.12.
PomBaseiSPAC1D4.12. rad15.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: PomBase
  • cytosol Source: PomBase
  • holo TFIIH complex Source: PomBase
  • nucleotide-excision repair factor 3 complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772DNA repair helicase rad15PRO_0000101984Add
BLAST

Proteomic databases

MaxQBiP26659.

Interactioni

Subunit structurei

One of the nine subunits forming the core-TFIIH basal transcription factor.1 Publication

Protein-protein interaction databases

IntActiP26659. 1 interaction.
MINTiMINT-4687938.

Structurei

3D structure databases

ProteinModelPortaliP26659.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 283277Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi233 – 2364DEAH box

Sequence similaritiesi

Belongs to the helicase family. RAD3/XPD subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000205390.
InParanoidiP26659.
KOiK10844.
OMAiDEVWKYK.
OrthoDBiEOG7BKD38.
PhylomeDBiP26659.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR010643. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. RAD3/XPD.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSiPR00852. XRODRMPGMNTD.
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26659-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFYIDDLPI LFPYPRIYPE QYQYMCDLKH SLDAGGIALL EMPSGTGKTI
60 70 80 90 100
SLLSLIVSYQ QHYPEHRKLI YCSRTMSEID KALAELKRLM AYRTSQLGYE
110 120 130 140 150
EPFLGLGLTS RKNLCLHPSV RREKNGNVVD ARCRSLTAGF VREQRLAGMD
160 170 180 190 200
VPTCEFHDNL EDLEPHSLIS NGVWTLDDIT EYGEKTTRCP YFTVRRMLPF
210 220 230 240 250
CNVIIYSYHY LLDPKIAERV SRELSKDCIV VFDEAHNIDN VCIESLSIDL
260 270 280 290 300
TESSLRKASK SILSLEQKVN EVKQSDSKKL QDEYQKLVRG LQDANAANDE
310 320 330 340 350
DQFMANPVLP EDVLKEAVPG NIRRAEHFIA FLKRFVEYLK TRMKVLHVIA
360 370 380 390 400
ETPTSFLQHV KDITFIDKKP LRFCAERLTS LVRALQISLV EDFHSLQQVV
410 420 430 440 450
AFATLVATYE RGFILILEPF ETENATVPNP ILRFSCLDAS IAIKPVFERF
460 470 480 490 500
RSVIITSGTL SPLDMYPKML QFNTVMQESY GMSLARNCFL PMVVTRGSDQ
510 520 530 540 550
VAISSKFEAR NDPSVVRNYG NILVEFSKIT PDGLVAFFPS YLYLESIVSS
560 570 580 590 600
WQSMGILDEV WKYKLILVET PDPHETTLAL ETYRAACSNG RGAVLLSVAR
610 620 630 640 650
GKVSEGVDFD HHYGRAVIMF GIPYQYTESR VLKARLEFLR DTYQIREADF
660 670 680 690 700
LTFDAMRHAA QCLGRVLRGK DDHGIMVLAD KRYGRSDKRT KLPKWIQQYI
710 720 730 740 750
TEGATNLSTD MSLALAKKFL RTMAQPFTAS DQEGISWWSL DDLLIHQKKA
760 770
LKSAAIEQSK HEDEMDIDVV ET
Length:772
Mass (Da):88,149
Last modified:October 1, 1996 - v2
Checksum:iA21025C298A28F08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251S → N in CAA45870 (PubMed:1534406).Curated
Sequence conflicti588 – 5881S → T in CAA43022 (PubMed:1319571).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64583 Genomic DNA. Translation: CAA45870.1.
X60499 Genomic DNA. Translation: CAA43022.1.
CU329670 Genomic DNA. Translation: CAA93221.1.
PIRiS22660.
RefSeqiNP_593025.1. NM_001018424.2.

Genome annotation databases

EnsemblFungiiSPAC1D4.12.1; SPAC1D4.12.1:pep; SPAC1D4.12.
GeneIDi2542203.
KEGGispo:SPAC1D4.12.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64583 Genomic DNA. Translation: CAA45870.1.
X60499 Genomic DNA. Translation: CAA43022.1.
CU329670 Genomic DNA. Translation: CAA93221.1.
PIRiS22660.
RefSeqiNP_593025.1. NM_001018424.2.

3D structure databases

ProteinModelPortaliP26659.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP26659. 1 interaction.
MINTiMINT-4687938.

Proteomic databases

MaxQBiP26659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1D4.12.1; SPAC1D4.12.1:pep; SPAC1D4.12.
GeneIDi2542203.
KEGGispo:SPAC1D4.12.

Organism-specific databases

EuPathDBiFungiDB:SPAC1D4.12.
PomBaseiSPAC1D4.12. rad15.

Phylogenomic databases

HOGENOMiHOG000205390.
InParanoidiP26659.
KOiK10844.
OMAiDEVWKYK.
OrthoDBiEOG7BKD38.
PhylomeDBiP26659.

Enzyme and pathway databases

ReactomeiR-SPO-113418. Formation of the Early Elongation Complex.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-674695. RNA Polymerase II Pre-transcription Events.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-72086. mRNA Capping.
R-SPO-73776. RNA Polymerase II Promoter Escape.
R-SPO-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-SPO-75953. RNA Polymerase II Transcription Initiation.
R-SPO-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-SPO-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

PROiP26659.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR010643. HBB.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR001945. RAD3/XPD.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF06777. HBB. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
PRINTSiPR00852. XRODRMPGMNTD.
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 6 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Schizosaccharomyces pombe rhp3+ gene required for DNA repair and cell viability is functionally interchangeable with the RAD3 gene of Saccharomyces cerevisiae."
    Reynolds P.R., Biggar S., Prakash L., Prakash S.
    Nucleic Acids Res. 20:2327-2334(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Cloning and characterisation of the S. pombe rad15 gene, a homologue to the S. cerevisiae RAD3 and human ERCC2 genes."
    Murray J.M., Doe C., Schenk P., Carr A.M., Lehmann A.R., Watts F.Z.
    Nucleic Acids Res. 20:2673-2678(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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.
  4. "Analysis of spontaneous and double-strand break-induced recombination in rad mutants of S. pombe."
    Fortunato E.A., Osman F., Subramani S.
    Mutat. Res. 364:14-60(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent transcription in vitro."
    Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O., Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.
    J. Biol. Chem. 278:51301-51306(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD15_SCHPO
AccessioniPrimary (citable) accession number: P26659
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 135 of the entry and version 2 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.