O34398
Gene name |
ligd (ykoU, BSU13400) |
Protein name |
Bifunctional non-homologous end joining protein LigD |
Names |
NHEJ DNA polymerase |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU13400 |
EC number |
6.5.1.1: Forming phosphoric ester bonds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O34398
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O34398-F1 | Predicted | AlphaFoldDB |
No variants for O34398
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O34398 | |||||
No associated diseases with O34398
5 regional properties for O34398
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DNA ligase, ATP-dependent, central | 16 - 208 | IPR012310 |
| domain | DNA ligase D | 13 - 592 | IPR014143 |
| domain | DNA ligase D, polymerase domain | 325 - 564 | IPR014145 |
| domain | DNA ligase D, ligase domain | 5 - 310 | IPR014146 |
| domain | LigD polymerase domain, type 3 | 341 - 563 | IPR033652 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.5.1.1 | Forming phosphoric ester bonds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA ligase (ATP) activity | Catalysis of the reaction: ATP + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + diphosphate + deoxyribonucleotide(n+m). |
| 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. |
| exonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by removing nucleotide residues from the 3' or 5' end. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA recombination | Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. |
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| sporulation resulting in formation of a cellular spore | The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAFTMQPVLT | SSPPIGAEWR | YEVKYDGYRC | ILRIHSSGVT | LTSRNGVELS | STFPEITQFA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KTAFQHLEKE | LPLTLDGEIV | CLVNPCRADF | EHLQVRGRLK | RPDKIQESAN | ARPCCFLAFD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLERSGEDVT | LLSYLDRKKS | LRELISAAKL | PASPDPYAKE | TIQSIPCYDH | FDQLWEMVIK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YDGEGIVAKK | TNSKWLEKKR | SSDWLKYKNF | KQAYVCITGF | NPNNGFLTVS | VLKNGIMTPI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ASVSHGMRDE | EKSAIREIME | QHGHQTPSGE | FTLEPSICAA | VQYLTILQGT | LREVSFIGFE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FQMDWTECTY | AQVIRHSKPV | HPKLQFTSLD | KIIFEKNKKT | KEDFIQYMIE | VSDYLLPFLK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NRAVTVIRYP | HGSRSESFFQ | KNKPDYAPDF | VQSFYDGSHE | HIVCEDMSTL | LWLCNQLALE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FHVPFQTIKS | RRPAEIVIDL | DPPSRDDFLM | AVQAANELKR | LLDSFGITSY | PKLSGNKGIQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LYIPLSPEAF | TYEETRQFTQ | LIAEYCTNAF | PELFTTERLI | KNRHCKLYLD | YLQHAEGKTI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ICPYSTRGNE | LGTVAAPLYW | HEVQSSLTPA | LFTIDTVIDR | IKKQGCPFFD | FYRNPQDEPL |
| 610 | |||||
| SAILHQLKKK | S |