Q8RI94
Gene name |
ligA |
Protein name |
DNA ligase |
Names |
Polydeoxyribonucleotide synthase [NAD(+)] |
Species |
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) |
KEGG Pathway |
fnu:FN1717 |
EC number |
6.5.1.2: 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 Q8RI94
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8RI94-F1 | Predicted | AlphaFoldDB |
No variants for Q8RI94
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8RI94 | |||||
No associated diseases with Q8RI94
10 regional properties for Q8RI94
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BRCT domain | 615 - 695 | IPR001357 |
| domain | Helix-hairpin-helix DNA-binding motif, class 1 | 465 - 484 | IPR003583-1 |
| domain | Helix-hairpin-helix DNA-binding motif, class 1 | 501 - 520 | IPR003583-2 |
| domain | Helix-hairpin-helix DNA-binding motif, class 1 | 565 - 584 | IPR003583-3 |
| domain | Zinc-finger, NAD-dependent DNA ligase C4-type | 428 - 453 | IPR004149 |
| domain | NAD-dependent DNA ligase, OB-fold | 342 - 418 | IPR004150 |
| domain | NAD-dependent DNA ligase, adenylation | 29 - 337 | IPR013839 |
| domain | NAD-dependent DNA ligase, N-terminal | 26 - 467 | IPR013840 |
| active_site | NAD-dependent DNA ligase, active site | 139 - 168 | IPR018239 |
| domain | DisA/LigA, helix-hairpin-helix motif | 532 - 594 | IPR041663 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.5.1.2 | Forming phosphoric ester bonds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA ligase (NAD+) activity | Catalysis of the reaction: NAD+ + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + nicotinamide nucleotide + deoxyribonucleotide(n+m). |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| base-excision repair, DNA ligation | The ligation by DNA ligase of DNA strands. Ligation occurs after polymerase action to fill the gap left by the action of endonucleases during base-excision repair. |
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEIKKRIEEL | KNNQTGLTFY | SSQELNDLEK | IVKLREDLNK | YRDSYYNDNK | SLISDYEFDI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLKELESLEE | KYPQYKEISS | PTTSVGASLK | ENKFKKVEHL | HPMLSLANSY | NIGEIVEFIE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RIKKKIPKEQ | ELKYCLEVKL | DGLSISLTYR | QGKLVRAVTR | GDGFIGEDVT | ENILEIASIV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KTLPQAIDME | IRGEVVLPLA | SFEKLNNERL | EKGEELFANP | RNAASGTLRQ | LDSKIVKDRG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LDAYFYFLVE | ADKLGLKSHS | ESIKFLESMG | IKTTGIFELL | ETSKDIEKRI | NYWEKERESL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PYETDGLVIK | VDEINLWDEI | GYTSKTPRWA | IAYKFPAHQV | STVLNDVTWQ | VGRTGKLTPV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AELQEVELSG | SKVKRASLHN | ISEIQRKDIR | IGDRVFIEKA | AEIIPQVVKA | IKEERTGNEK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VIEEPTCCPI | CNHKLEREEG | LVDIKCINEE | CPAKVQGEIE | YFVSRDALNI | MGLGSKIVEK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FIDLGYIKTV | VDIFDLKNHR | EALENIDKMG | KKSIENLLNS | IEESKNRDYD | KILYALGIAE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IGKVTSKILA | KASKNIDKLM | AMTFEDLTSI | EGIGEIAANE | IIAFFTKEKN | QKIIQGLKEK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GLKFEIKESE | ASVQNVNPNF | VGKNFLFTGT | LKHFTREQIK | EEIEKLGGKN | LSSVSKNLDY |
| 670 | 680 | 690 | |||
| LIVGEKAGSK | LKKAQEIPTI | KILTEEEFIE | LKDKFD |