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Q97W02

- DPO4_SULSO

UniProt

Q97W02 - DPO4_SULSO

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Protein

DNA polymerase IV

Gene

dbh

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. It is involved in translesional synthesis.

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Temperature dependencei

Highly active from 35 to 95 degrees Celsius. Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi7 – 71Magnesium
Sitei12 – 121Substrate discrimination
Metal bindingi105 – 1051Magnesium
Active sitei106 – 1061

GO - Molecular functioni

  1. damaged DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. DNA repair Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

DNA damage, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-2274-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase IV (EC:2.7.7.7)
Short name:
Pol IV
Gene namesi
Name:dbh
Synonyms:dpo4
Ordered Locus Names:SSO2448
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1062DE → AA: Loss of function. 1 Publication
Mutagenesisi342 – 35211Missing: Almost complete loss of interaction with PCNA. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352DNA polymerase IVPRO_0000173976Add
BLAST

Interactioni

Subunit structurei

Monomer. Interacts with the PCNA heterotrimer via PCNA1.1 Publication

Protein-protein interaction databases

DIPiDIP-48855N.
STRINGi273057.SSO2448.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi11 – 199Combined sources
Helixi21 – 233Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Turni38 – 403Combined sources
Beta strandi41 – 466Combined sources
Helixi48 – 514Combined sources
Turni52 – 543Combined sources
Beta strandi57 – 593Combined sources
Helixi61 – 677Combined sources
Beta strandi71 – 755Combined sources
Helixi78 – 9215Combined sources
Turni93 – 953Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi106 – 1105Combined sources
Turni112 – 1143Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 13619Combined sources
Beta strandi140 – 1478Combined sources
Helixi148 – 15811Combined sources
Turni159 – 1613Combined sources
Beta strandi163 – 1653Combined sources
Helixi168 – 17710Combined sources
Helixi180 – 1823Combined sources
Helixi188 – 1958Combined sources
Turni196 – 1983Combined sources
Helixi202 – 2065Combined sources
Helixi210 – 2178Combined sources
Helixi219 – 22911Combined sources
Beta strandi244 – 25512Combined sources
Helixi258 – 27619Combined sources
Beta strandi281 – 29010Combined sources
Turni291 – 2933Combined sources
Beta strandi295 – 3017Combined sources
Helixi308 – 32518Combined sources
Beta strandi330 – 34011Combined sources
Beta strandi343 – 3464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JX4X-ray1.70A1-352[»]
1JXLX-ray2.10A1-352[»]
1N48X-ray2.20A1-352[»]
1N56X-ray2.40A/B1-352[»]
1RYRX-ray2.28A1-352[»]
1RYSX-ray2.03A/B1-352[»]
1S0MX-ray2.70A/B1-352[»]
1S0NX-ray2.80A1-352[»]
1S0OX-ray2.10A/B1-352[»]
1S10X-ray2.10A1-352[»]
1S97X-ray2.40A/B/C/D1-352[»]
1S9FX-ray2.00A/B/C/D1-352[»]
2AGOX-ray2.85A1-341[»]
2AGPX-ray2.90A/B1-341[»]
2AGQX-ray2.10A1-341[»]
2ASDX-ray1.95A/B2-352[»]
2ASJX-ray2.35A/B2-352[»]
2ASLX-ray2.65A/B2-352[»]
2ATLX-ray2.80A/B2-352[»]
2AU0X-ray2.70A/B2-352[»]
2BQ3X-ray2.00A1-352[»]
2BQRX-ray2.37A1-352[»]
2BQUX-ray2.50A1-352[»]
2BR0X-ray2.17A1-352[»]
2C22X-ray2.56A1-352[»]
2C28X-ray2.27A1-352[»]
2C2DX-ray2.57A1-352[»]
2C2EX-ray2.61A1-352[»]
2C2RX-ray2.55A1-352[»]
2IA6X-ray2.50A/B1-352[»]
2IBKX-ray2.25A1-352[»]
2IMWX-ray2.05P1-348[»]
2J6SX-ray2.50A1-352[»]
2J6TX-ray2.60A1-352[»]
2J6UX-ray2.50A1-352[»]
2JEFX-ray2.17A1-352[»]
2JEGX-ray2.38A1-352[»]
2JEIX-ray2.39A1-352[»]
2JEJX-ray1.86A1-352[»]
2R8GX-ray2.70A1-352[»]
2R8HX-ray2.48A1-352[»]
2R8IX-ray2.38A1-352[»]
2RDIX-ray1.92A1-341[»]
2RDJX-ray2.20A/B1-352[»]
2UVRX-ray2.90A1-352[»]
2UVUX-ray2.70A1-352[»]
2UVVX-ray2.20A1-352[»]
2UVWX-ray2.09A1-352[»]
2V4QX-ray2.60A1-352[»]
2V4RX-ray2.50A1-352[»]
2V9WX-ray3.00A/B1-352[»]
2VA2X-ray2.80A/B1-352[»]
2VA3X-ray2.98A1-352[»]
2W8KX-ray3.10A1-352[»]
2W8LX-ray3.00A1-352[»]
2W9AX-ray2.60A1-352[»]
2W9BX-ray2.28A/B1-352[»]
2W9CX-ray2.87A/B1-352[»]
2XC9X-ray2.20A1-352[»]
2XCAX-ray2.50A1-352[»]
2XCPX-ray2.60A/B1-352[»]
3FDSX-ray2.05A1-352[»]
3GIIX-ray2.60A2-341[»]
3GIJX-ray2.40A/B2-341[»]
3GIKX-ray2.90A2-341[»]
3GILX-ray2.71A/B2-341[»]
3GIMX-ray2.70A2-341[»]
3KHGX-ray2.96A/B2-341[»]
3KHHX-ray2.70A/B2-341[»]
3KHLX-ray2.10A/B2-341[»]
3KHRX-ray2.01A/B2-341[»]
3M9MX-ray2.90B1-352[»]
3M9NX-ray1.93B1-352[»]
3M9OX-ray2.00B1-352[»]
3PR4X-ray2.65A1-341[»]
3PR5X-ray2.40B1-341[»]
3PVXX-ray3.03A1-341[»]
3PW0X-ray2.91A1-341[»]
3PW2X-ray2.74A1-341[»]
3PW4X-ray2.90A1-341[»]
3PW5X-ray3.00A1-341[»]
3PW7X-ray2.90A/E1-341[»]
3QZ7X-ray2.00A1-352[»]
3QZ8X-ray2.00A1-352[»]
3RAQX-ray2.25A/B2-341[»]
3RAXX-ray1.89A/B2-341[»]
3RB0X-ray3.22A/B2-341[»]
3RB3X-ray2.80A2-341[»]
3RB4X-ray2.80A/B2-341[»]
3RB6X-ray2.70A/B2-341[»]
3RBDX-ray2.50A/B2-341[»]
3RBEX-ray2.80A/B2-341[»]
3T5HX-ray2.35A1-341[»]
3T5JX-ray2.40A1-341[»]
3T5KX-ray2.90A1-341[»]
3T5LX-ray2.90A1-341[»]
3V6HX-ray2.30A/B1-342[»]
3V6JX-ray2.30A/J1-342[»]
3V6KX-ray3.60A/J1-342[»]
4F4WX-ray1.90A/B231-352[»]
4F4XX-ray2.05A231-352[»]
4F4YX-ray2.34A/B5-211[»]
A/B127-335[»]
4F4ZX-ray2.30A/B1-246[»]
4F50X-ray2.22A246-352[»]
4FBTX-ray2.00A1-341[»]
4FBUX-ray2.60A/B1-341[»]
4G3IX-ray2.50A/B1-341[»]
4GC6X-ray2.90A1-352[»]
4GC7X-ray2.89A/B1-352[»]
4JUZX-ray2.65A1-341[»]
4JV0X-ray2.95A1-341[»]
4JV1X-ray2.30A1-341[»]
4JV2X-ray2.74A1-341[»]
4QW8X-ray2.29A1-341[»]
4QW9X-ray2.40A1-341[»]
4QWAX-ray2.20A1-341[»]
4QWBX-ray1.80A1-343[»]
4QWCX-ray2.40A/D1-342[»]
4QWDX-ray2.05A1-341[»]
4QWEX-ray2.20A1-341[»]
ProteinModelPortaliQ97W02.
SMRiQ97W02. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97W02.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 187185UmuCAdd
BLAST

Domaini

The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0389.
HOGENOMiHOG000082707.
InParanoidiQ97W02.
KOiK04479.
OMAiDQPISAT.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
HAMAPiMF_01113. DNApol_IV.
InterProiIPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
[Graphical view]
PfamiPF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view]
SUPFAMiSSF100879. SSF100879. 1 hit.
PROSITEiPS50173. UMUC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q97W02-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIVLFVDFDY FYAQVEEVLN PSLKGKPVVV CVFSGRFEDS GAVATANYEA
60 70 80 90 100
RKFGVKAGIP IVEAKKILPN AVYLPMRKEV YQQVSSRIMN LLREYSEKIE
110 120 130 140 150
IASIDEAYLD ISDKVRDYRE AYNLGLEIKN KILEKEKITV TVGISKNKVF
160 170 180 190 200
AKIAADMAKP NGIKVIDDEE VKRLIRELDI ADVPGIGNIT AEKLKKLGIN
210 220 230 240 250
KLVDTLSIEF DKLKGMIGEA KAKYLISLAR DEYNEPIRTR VRKSIGRIVT
260 270 280 290 300
MKRNSRNLEE IKPYLFRAIE ESYYKLDKRI PKAIHVVAVT EDLDIVSRGR
310 320 330 340 350
TFPHGISKET AYSESVKLLQ KILEEDERKI RRIGVRFSKF IEAIGLDKFF

DT
Length:352
Mass (Da):40,193
Last modified:October 1, 2001 - v1
Checksum:iC0B0AD4B3A3E87D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK42588.1.
PIRiE90416.
RefSeqiNP_343798.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42588; AAK42588; SSO2448.
GeneIDi1453915.
KEGGisso:SSO2448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK42588.1 .
PIRi E90416.
RefSeqi NP_343798.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JX4 X-ray 1.70 A 1-352 [» ]
1JXL X-ray 2.10 A 1-352 [» ]
1N48 X-ray 2.20 A 1-352 [» ]
1N56 X-ray 2.40 A/B 1-352 [» ]
1RYR X-ray 2.28 A 1-352 [» ]
1RYS X-ray 2.03 A/B 1-352 [» ]
1S0M X-ray 2.70 A/B 1-352 [» ]
1S0N X-ray 2.80 A 1-352 [» ]
1S0O X-ray 2.10 A/B 1-352 [» ]
1S10 X-ray 2.10 A 1-352 [» ]
1S97 X-ray 2.40 A/B/C/D 1-352 [» ]
1S9F X-ray 2.00 A/B/C/D 1-352 [» ]
2AGO X-ray 2.85 A 1-341 [» ]
2AGP X-ray 2.90 A/B 1-341 [» ]
2AGQ X-ray 2.10 A 1-341 [» ]
2ASD X-ray 1.95 A/B 2-352 [» ]
2ASJ X-ray 2.35 A/B 2-352 [» ]
2ASL X-ray 2.65 A/B 2-352 [» ]
2ATL X-ray 2.80 A/B 2-352 [» ]
2AU0 X-ray 2.70 A/B 2-352 [» ]
2BQ3 X-ray 2.00 A 1-352 [» ]
2BQR X-ray 2.37 A 1-352 [» ]
2BQU X-ray 2.50 A 1-352 [» ]
2BR0 X-ray 2.17 A 1-352 [» ]
2C22 X-ray 2.56 A 1-352 [» ]
2C28 X-ray 2.27 A 1-352 [» ]
2C2D X-ray 2.57 A 1-352 [» ]
2C2E X-ray 2.61 A 1-352 [» ]
2C2R X-ray 2.55 A 1-352 [» ]
2IA6 X-ray 2.50 A/B 1-352 [» ]
2IBK X-ray 2.25 A 1-352 [» ]
2IMW X-ray 2.05 P 1-348 [» ]
2J6S X-ray 2.50 A 1-352 [» ]
2J6T X-ray 2.60 A 1-352 [» ]
2J6U X-ray 2.50 A 1-352 [» ]
2JEF X-ray 2.17 A 1-352 [» ]
2JEG X-ray 2.38 A 1-352 [» ]
2JEI X-ray 2.39 A 1-352 [» ]
2JEJ X-ray 1.86 A 1-352 [» ]
2R8G X-ray 2.70 A 1-352 [» ]
2R8H X-ray 2.48 A 1-352 [» ]
2R8I X-ray 2.38 A 1-352 [» ]
2RDI X-ray 1.92 A 1-341 [» ]
2RDJ X-ray 2.20 A/B 1-352 [» ]
2UVR X-ray 2.90 A 1-352 [» ]
2UVU X-ray 2.70 A 1-352 [» ]
2UVV X-ray 2.20 A 1-352 [» ]
2UVW X-ray 2.09 A 1-352 [» ]
2V4Q X-ray 2.60 A 1-352 [» ]
2V4R X-ray 2.50 A 1-352 [» ]
2V9W X-ray 3.00 A/B 1-352 [» ]
2VA2 X-ray 2.80 A/B 1-352 [» ]
2VA3 X-ray 2.98 A 1-352 [» ]
2W8K X-ray 3.10 A 1-352 [» ]
2W8L X-ray 3.00 A 1-352 [» ]
2W9A X-ray 2.60 A 1-352 [» ]
2W9B X-ray 2.28 A/B 1-352 [» ]
2W9C X-ray 2.87 A/B 1-352 [» ]
2XC9 X-ray 2.20 A 1-352 [» ]
2XCA X-ray 2.50 A 1-352 [» ]
2XCP X-ray 2.60 A/B 1-352 [» ]
3FDS X-ray 2.05 A 1-352 [» ]
3GII X-ray 2.60 A 2-341 [» ]
3GIJ X-ray 2.40 A/B 2-341 [» ]
3GIK X-ray 2.90 A 2-341 [» ]
3GIL X-ray 2.71 A/B 2-341 [» ]
3GIM X-ray 2.70 A 2-341 [» ]
3KHG X-ray 2.96 A/B 2-341 [» ]
3KHH X-ray 2.70 A/B 2-341 [» ]
3KHL X-ray 2.10 A/B 2-341 [» ]
3KHR X-ray 2.01 A/B 2-341 [» ]
3M9M X-ray 2.90 B 1-352 [» ]
3M9N X-ray 1.93 B 1-352 [» ]
3M9O X-ray 2.00 B 1-352 [» ]
3PR4 X-ray 2.65 A 1-341 [» ]
3PR5 X-ray 2.40 B 1-341 [» ]
3PVX X-ray 3.03 A 1-341 [» ]
3PW0 X-ray 2.91 A 1-341 [» ]
3PW2 X-ray 2.74 A 1-341 [» ]
3PW4 X-ray 2.90 A 1-341 [» ]
3PW5 X-ray 3.00 A 1-341 [» ]
3PW7 X-ray 2.90 A/E 1-341 [» ]
3QZ7 X-ray 2.00 A 1-352 [» ]
3QZ8 X-ray 2.00 A 1-352 [» ]
3RAQ X-ray 2.25 A/B 2-341 [» ]
3RAX X-ray 1.89 A/B 2-341 [» ]
3RB0 X-ray 3.22 A/B 2-341 [» ]
3RB3 X-ray 2.80 A 2-341 [» ]
3RB4 X-ray 2.80 A/B 2-341 [» ]
3RB6 X-ray 2.70 A/B 2-341 [» ]
3RBD X-ray 2.50 A/B 2-341 [» ]
3RBE X-ray 2.80 A/B 2-341 [» ]
3T5H X-ray 2.35 A 1-341 [» ]
3T5J X-ray 2.40 A 1-341 [» ]
3T5K X-ray 2.90 A 1-341 [» ]
3T5L X-ray 2.90 A 1-341 [» ]
3V6H X-ray 2.30 A/B 1-342 [» ]
3V6J X-ray 2.30 A/J 1-342 [» ]
3V6K X-ray 3.60 A/J 1-342 [» ]
4F4W X-ray 1.90 A/B 231-352 [» ]
4F4X X-ray 2.05 A 231-352 [» ]
4F4Y X-ray 2.34 A/B 5-211 [» ]
A/B 127-335 [» ]
4F4Z X-ray 2.30 A/B 1-246 [» ]
4F50 X-ray 2.22 A 246-352 [» ]
4FBT X-ray 2.00 A 1-341 [» ]
4FBU X-ray 2.60 A/B 1-341 [» ]
4G3I X-ray 2.50 A/B 1-341 [» ]
4GC6 X-ray 2.90 A 1-352 [» ]
4GC7 X-ray 2.89 A/B 1-352 [» ]
4JUZ X-ray 2.65 A 1-341 [» ]
4JV0 X-ray 2.95 A 1-341 [» ]
4JV1 X-ray 2.30 A 1-341 [» ]
4JV2 X-ray 2.74 A 1-341 [» ]
4QW8 X-ray 2.29 A 1-341 [» ]
4QW9 X-ray 2.40 A 1-341 [» ]
4QWA X-ray 2.20 A 1-341 [» ]
4QWB X-ray 1.80 A 1-343 [» ]
4QWC X-ray 2.40 A/D 1-342 [» ]
4QWD X-ray 2.05 A 1-341 [» ]
4QWE X-ray 2.20 A 1-341 [» ]
ProteinModelPortali Q97W02.
SMRi Q97W02. Positions 1-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48855N.
STRINGi 273057.SSO2448.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK42588 ; AAK42588 ; SSO2448 .
GeneIDi 1453915.
KEGGi sso:SSO2448.

Phylogenomic databases

eggNOGi COG0389.
HOGENOMi HOG000082707.
InParanoidi Q97W02.
KOi K04479.
OMAi DQPISAT.

Enzyme and pathway databases

BioCyci SSOL273057:GCH2-2274-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q97W02.

Family and domain databases

Gene3Di 3.30.1490.100. 1 hit.
HAMAPi MF_01113. DNApol_IV.
InterProi IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. DNA_repair_prot_UmuC-like.
IPR017963. DNA_repair_prot_UmuC-like_N.
IPR022880. DNApol_IV.
IPR024728. PolY_HhH_motif.
[Graphical view ]
Pfami PF00817. IMS. 1 hit.
PF11799. IMS_C. 1 hit.
PF11798. IMS_HHH. 1 hit.
[Graphical view ]
SUPFAMi SSF100879. SSF100879. 1 hit.
PROSITEi PS50173. UMUC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol eta."
    Boudsocq F., Iwai S., Hanaoka F., Woodgate R.
    Nucleic Acids Res. 29:4607-4616(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Low fidelity DNA synthesis by a Y family DNA polymerase due to misalignment in the active site."
    Kokoska R.J., Bebenek K., Boudsocq F., Woodgate R., Kunkel T.A.
    J. Biol. Chem. 277:19633-19638(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  4. "Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication."
    Ling H., Boudsocq F., Woodgate R., Yang W.
    Cell 107:91-102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TERNARY COMPLEX WITH DNA AND AN INCOMING NUCLEOTIDE, MUTAGENESIS OF 105-ASP-GLU-106.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  5. "Structural insight into recruitment of translesion DNA polymerase Dpo4 to sliding clamp PCNA."
    Xing G., Kirouac K., Shin Y.J., Bell S.D., Ling H.
    Mol. Microbiol. 71:678-691(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-244 IN COMPLEX WITH PCNA, INTERACTION WITH PCNA1, SUBUNIT, DNA-BINDING, MUTAGENESIS OF 342-GLU--THR-352.

Entry informationi

Entry nameiDPO4_SULSO
AccessioniPrimary (citable) accession number: Q97W02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 1, 2001
Last modified: November 26, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3