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Protein

DNA polymerase eta

Gene

RAD30

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.34 Publications

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi30 – 301MagnesiumPROSITE-ProRule annotation
Metal bindingi155 – 1551MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • chromosome segregation Source: SGD
  • DNA replication Source: UniProtKB-KW
  • error-free translesion synthesis Source: SGD
  • error-prone translesion synthesis Source: SGD
  • mitotic sister chromatid cohesion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA repair, DNA replication, DNA synthesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29960-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase eta (EC:2.7.7.7)
Alternative name(s):
Radiation-sensitive protein 30
Gene namesi
Name:RAD30
Synonyms:DBH1
Ordered Locus Names:YDR419W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR419W.
SGDiS000002827. RAD30.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: SGD
  • nucleus Source: SGD
  • replication fork Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301D → A: Abolishes DNA polymerase activity. 1 Publication
Mutagenesisi34 – 341F → L: Alters translesion activity. 1 Publication
Mutagenesisi39 – 391E → A: Abolishes DNA polymerase activity. 1 Publication
Mutagenesisi64 – 641Y → F or A: Decreases efficiency of nucleotide incorporation. 1 Publication
Mutagenesisi67 – 671R → A: Decreases efficiency of nucleotide incorporation. 1 Publication
Mutagenesisi155 – 1551D → A: Abolishes DNA polymerase activity and increases UV-induced mutations. 1 Publication
Mutagenesisi156 – 1561E → A: Decreases efficiency of nucleotide incorporation. 1 Publication
Mutagenesisi279 – 2791K → A: Decreases efficiency of nucleotide incorporation. 1 Publication
Mutagenesisi627 – 6271F → A: Abolishes POL30-binding; when associated with A-628.
Mutagenesisi628 – 6281F → A: Abolishes POL30-binding; when associated with A-627.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632DNA polymerase etaPRO_0000268698Add
BLAST

Proteomic databases

MaxQBiQ04049.
PRIDEiQ04049.

Expressioni

Inductioni

By UV radiation and heat shock. The mRNA is stabilized during stationary phase.2 Publications

Interactioni

Subunit structurei

Interacts with POL30. This interaction is essential for the polymerase eta function.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POL30P158733EBI-36214,EBI-12993

Protein-protein interaction databases

BioGridi32477. 90 interactions.
DIPiDIP-6500N.
IntActiQ04049. 8 interactions.
MINTiMINT-708283.

Structurei

Secondary structure

632
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 55Combined sources
Helixi6 – 105Combined sources
Helixi11 – 133Combined sources
Turni15 – 173Combined sources
Helixi18 – 203Combined sources
Beta strandi21 – 233Combined sources
Beta strandi26 – 316Combined sources
Helixi34 – 429Combined sources
Beta strandi51 – 555Combined sources
Beta strandi58 – 625Combined sources
Helixi64 – 674Combined sources
Turni68 – 703Combined sources
Helixi77 – 815Combined sources
Beta strandi88 – 914Combined sources
Beta strandi93 – 964Combined sources
Beta strandi100 – 1034Combined sources
Helixi115 – 1173Combined sources
Beta strandi123 – 1275Combined sources
Helixi129 – 14517Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi156 – 1605Combined sources
Helixi162 – 17110Combined sources
Beta strandi176 – 1783Combined sources
Helixi183 – 1864Combined sources
Helixi188 – 1969Combined sources
Beta strandi203 – 2064Combined sources
Helixi210 – 2145Combined sources
Beta strandi219 – 2213Combined sources
Helixi233 – 25624Combined sources
Beta strandi260 – 2678Combined sources
Helixi268 – 2758Combined sources
Turni276 – 2783Combined sources
Beta strandi280 – 2856Combined sources
Helixi288 – 2903Combined sources
Helixi291 – 2955Combined sources
Beta strandi297 – 2993Combined sources
Helixi302 – 3043Combined sources
Helixi306 – 3083Combined sources
Helixi311 – 3199Combined sources
Beta strandi324 – 3263Combined sources
Helixi327 – 3348Combined sources
Helixi339 – 35113Combined sources
Beta strandi352 – 3554Combined sources
Turni357 – 3593Combined sources
Helixi364 – 3663Combined sources
Helixi367 – 37711Combined sources
Turni378 – 3803Combined sources
Beta strandi395 – 4006Combined sources
Turni403 – 4064Combined sources
Helixi409 – 43426Combined sources
Beta strandi436 – 44813Combined sources
Beta strandi454 – 4607Combined sources
Helixi466 – 4683Combined sources
Helixi469 – 48719Combined sources
Turni488 – 4903Combined sources
Beta strandi497 – 51014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIHX-ray2.25A/B1-513[»]
2R8JX-ray3.10A/B1-531[»]
2R8KX-ray3.30A/B1-531[»]
2WTFX-ray2.50A/B1-513[»]
2XGPX-ray2.70A/B1-513[»]
2XGQX-ray2.70A/B1-513[»]
3MFHX-ray2.00A1-513[»]
3MFIX-ray1.76A1-513[»]
3OHAX-ray2.00A1-513[»]
3OHBX-ray2.00A1-513[»]
ProteinModelPortaliQ04049.
SMRiQ04049. Positions 1-512.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04049.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 309284UmuCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni625 – 6328POL30-binding

Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated
Contains 1 umuC domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000065930.
InParanoidiQ04049.
KOiK03509.
OMAiGYTTSCG.
OrthoDBiEOG092C18P5.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. UmuC.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04049-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKFTWKELI QLGSPSKAYE SSLACIAHID MNAFFAQVEQ MRCGLSKEDP
60 70 80 90 100
VVCVQWNSII AVSYAARKYG ISRMDTIQEA LKKCSNLIPI HTAVFKKGED
110 120 130 140 150
FWQYHDGCGS WVQDPAKQIS VEDHKVSLEP YRRESRKALK IFKSACDLVE
160 170 180 190 200
RASIDEVFLD LGRICFNMLM FDNEYELTGD LKLKDALSNI REAFIGGNYD
210 220 230 240 250
INSHLPLIPE KIKSLKFEGD VFNPEGRDLI TDWDDVILAL GSQVCKGIRD
260 270 280 290 300
SIKDILGYTT SCGLSSTKNV CKLASNYKKP DAQTIVKNDC LLDFLDCGKF
310 320 330 340 350
EITSFWTLGG VLGKELIDVL DLPHENSIKH IRETWPDNAG QLKEFLDAKV
360 370 380 390 400
KQSDYDRSTS NIDPLKTADL AEKLFKLSRG RYGLPLSSRP VVKSMMSNKN
410 420 430 440 450
LRGKSCNSIV DCISWLEVFC AELTSRIQDL EQEYNKIVIP RTVSISLKTK
460 470 480 490 500
SYEVYRKSGP VAYKGINFQS HELLKVGIKF VTDLDIKGKN KSYYPLTKLS
510 520 530 540 550
MTITNFDIID LQKTVVDMFG NQVHTFKSSA GKEDEEKTTS SKADEKTPKL
560 570 580 590 600
ECCKYQVTFT DQKALQEHAD YHLALKLSEG LNGAEESSKN LSFGEKRLLF
610 620 630
SRKRPNSQHT ATPQKKQVTS SKNILSFFTR KK
Length:632
Mass (Da):71,515
Last modified:November 1, 1996 - v1
Checksum:iCFB1A9FBC8AFE39B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64856.1.
BK006938 Genomic DNA. Translation: DAA12259.1.
PIRiS69702.
RefSeqiNP_010707.3. NM_001180727.3.

Genome annotation databases

EnsemblFungiiYDR419W; YDR419W; YDR419W.
GeneIDi852028.
KEGGisce:YDR419W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64856.1.
BK006938 Genomic DNA. Translation: DAA12259.1.
PIRiS69702.
RefSeqiNP_010707.3. NM_001180727.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JIHX-ray2.25A/B1-513[»]
2R8JX-ray3.10A/B1-531[»]
2R8KX-ray3.30A/B1-531[»]
2WTFX-ray2.50A/B1-513[»]
2XGPX-ray2.70A/B1-513[»]
2XGQX-ray2.70A/B1-513[»]
3MFHX-ray2.00A1-513[»]
3MFIX-ray1.76A1-513[»]
3OHAX-ray2.00A1-513[»]
3OHBX-ray2.00A1-513[»]
ProteinModelPortaliQ04049.
SMRiQ04049. Positions 1-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32477. 90 interactions.
DIPiDIP-6500N.
IntActiQ04049. 8 interactions.
MINTiMINT-708283.

Proteomic databases

MaxQBiQ04049.
PRIDEiQ04049.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR419W; YDR419W; YDR419W.
GeneIDi852028.
KEGGisce:YDR419W.

Organism-specific databases

EuPathDBiFungiDB:YDR419W.
SGDiS000002827. RAD30.

Phylogenomic databases

HOGENOMiHOG000065930.
InParanoidiQ04049.
KOiK03509.
OMAiGYTTSCG.
OrthoDBiEOG092C18P5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29960-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ04049.
PROiQ04049.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. UmuC.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLH_YEAST
AccessioniPrimary (citable) accession number: Q04049
Secondary accession number(s): D6VT49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1860 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.