Q47155

PR
Gene name
dinB (dinP, b0231, JW0221)
Protein name
DNA polymerase IV
Names
Pol IV, Translesion synthesis polymerase IV, TSL polymerase IV
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b0231
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

202-284 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

32 structures for Q47155

Entry ID Method Resolution Chain Position Source
1OK7 X-ray 165 A C 336-351 PDB
1UNN X-ray 190 A C/D 243-351 PDB
4IR1 X-ray 238 A A/F 2-351 PDB
4IR9 X-ray 233 A A/F 2-351 PDB
4IRC X-ray 267 A A/F 2-341 PDB
4IRD X-ray 248 A A/F 2-341 PDB
4IRK X-ray 232 A A/B 2-341 PDB
4Q43 X-ray 245 A A/F 2-351 PDB
4Q44 X-ray 271 A A/F 2-341 PDB
4Q45 X-ray 218 A A/F 2-341 PDB
4R8U X-ray 230 A PDB
5C5J X-ray 210 A A/F 2-351 PDB
5YUR X-ray 204 A A/F 2-351 PDB
5YUS X-ray 194 A A/F 2-351 PDB
5YUT X-ray 215 A A/F 2-351 PDB
5YUU X-ray 189 A A/F 2-351 PDB
5YUV X-ray 206 A A/F 2-351 PDB
5YUW X-ray 212 A A/F 2-351 PDB
5YUX X-ray 204 A A/F 2-351 PDB
5YUY X-ray 174 A A/F 2-351 PDB
5YUZ X-ray 183 A A/F 2-351 PDB
5YV0 X-ray 209 A A/F 2-351 PDB
5YV1 X-ray 209 A A/F 2-351 PDB
5YV2 X-ray 190 A A/F 2-351 PDB
5YV3 X-ray 203 A A/F 2-351 PDB
5YYD X-ray 205 A A/F 2-351 PDB
5YYE X-ray 233 A A/F 2-351 PDB
5ZLV X-ray 235 A A/F 2-351 PDB
6IG1 X-ray 197 A A/F 2-351 PDB
6JUP X-ray 244 A A/F 2-341 PDB
6JUQ X-ray 274 A A/F 2-341 PDB
AF-Q47155-F1 Predicted AlphaFoldDB

13 variants for Q47155

Variant ID(s) Position Change Description Diseaes Association Provenance
36 E>ARG strain: ECOR 45B1 [UniProt] No
124 Q>K strain: ECOR 35D [UniProt] No
132 N>S strain: ECOR 34B1 and ECOR 37UG [UniProt] No
135 Q>H strain: ECOR 70B1 [UniProt] No
170 P>S strain: ECOR 37UG [UniProt] No
171 A>T strain: ECOR 45B1, ECOR 46D, ECOR 49D and ECOR 50D [UniProt] No
176 L>F strain: ECOR 37UG [UniProt] No
201 G>S strain: ECOR 59B2 [UniProt] No
210 M>I strain: ECOR 37UG, ECOR 45B1, ECOR 51B2, ECOR 52B2, ECOR 58B1 and ECOR 70B1 [UniProt] No
210 M>T strain: ECOR 35D, ECOR 46D, ECOR 49D, ECOR 50D, ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2 [UniProt] No
225 R>C strain: ECOR 59B2 and ECOR 60B2 [UniProt] No
310 A>S strain: ECOR 57B2, ECOR 59B2, ECOR 60B2 and ECOR 62B2 [UniProt] No
321 D>N strain: ECOR 35D [UniProt] No

No associated diseases with Q47155

3 regional properties for Q47155

Type Name Position InterPro Accession
domain UmuC domain 4 - 185 IPR001126
domain DNA polymerase, Y-family, little finger domain 240 - 347 IPR017961
conserved_site DNA polymerase type-Y, HhH motif 166 - 197 IPR024728

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
damaged DNA binding Binding to damaged DNA.
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
magnesium ion binding Binding to a magnesium (Mg) ion.

6 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
DNA synthesis involved in DNA repair Synthesis of DNA that proceeds from the broken 3' single-strand DNA end and uses the homologous intact duplex as the template.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
error-free translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions but does not causes an increase in the endogenous mutation level. For S. cerevisiae, RAD30 encodes DNA polymerase eta, which incorporates two adenines. When incorporated across a thymine-thymine dimer, it does not increase the endogenous mutation level.
error-prone translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
SOS response An error-prone process for repairing damaged microbial DNA.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9UBT6 POLK DNA polymerase kappa Homo sapiens (Human) PR
10 20 30 40 50 60
MRKIIHVDMD CFFAAVEMRD NPALRDIPIA IGGSRERRGV ISTANYPARK FGVRSAMPTG
70 80 90 100 110 120
MALKLCPHLT LLPGRFDAYK EASNHIREIF SRYTSRIEPL SLDEAYLDVT DSVHCHGSAT
130 140 150 160 170 180
LIAQEIRQTI FNELQLTASA GVAPVKFLAK IASDMNKPNG QFVITPAEVP AFLQTLPLAK
190 200 210 220 230 240
IPGVGKVSAA KLEAMGLRTC GDVQKCDLVM LLKRFGKFGR ILWERSQGID ERDVNSERLR
250 260 270 280 290 300
KSVGVERTMA EDIHHWSECE AIIERLYPEL ERRLAKVKPD LLIARQGVKL KFDDFQQTTQ
310 320 330 340 350
EHVWPRLNKA DLIATARKTW DERRGGRGVR LVGLHVTLLD PQMERQLVLG L