Q8TIW3

PR
Gene name
dbh
Protein name
DNA polymerase IV
Names
Pol IV
Species
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
KEGG Pathway
mac:MA_4027
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)

212-297 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8TIW3

Entry ID Method Resolution Chain Position Source
AF-Q8TIW3-F1 Predicted AlphaFoldDB

No variants for Q8TIW3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8TIW3

No associated diseases with Q8TIW3

3 regional properties for Q8TIW3

Type Name Position InterPro Accession
domain UmuC domain 6 - 197 IPR001126
domain DNA polymerase, Y-family, little finger domain 254 - 362 IPR017961
conserved_site DNA polymerase type-Y, HhH motif 178 - 209 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.

2 GO annotations of biological process

Name Definition
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-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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MMQRVIIHVD MDYFYAAIEE REKPELLGKA VVVCMLSGRS ELSGSVSTCN YIAREFGIRS
70 80 90 100 110 120
GMPCSRAKKL NPEAVFLPVR KEFYTSVSDR IMEILRSYAD PGENGDSFEQ ISVDEAFLEI
130 140 150 160 170 180
TYRAGGDFNL AFELGMQIKK EIKEKENLTC SIGIGPNKLI AKMASSAKKP DGITVVSPEN
190 200 210 220 230 240
QEAFLWPLKV SKLWGIGDVT AKKLQEMDIV TVKDLAEHDV IELISTFGKS RGTWLKQAAS
250 260 270 280 290 300
GIDDSPLKER EGSEQIGRIA TLPEDTLDQE LILSLLEKLA GDVIEKLDSR ELSFRVVTVT
310 320 330 340 350 360
VINSNFRTYT KSRTLNHPVS SKETLLEAAR EILSEFLSES KTEFRRVGVR VGGLQKKKGQ
TSLFDY