B1ZWH2
Gene name |
ligA1 |
Protein name |
DNA ligase 1 |
Names |
Polydeoxyribonucleotide synthase [NAD(+)] 1 |
Species |
Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1) |
KEGG Pathway |
ote:Oter_0004 |
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 B1ZWH2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1ZWH2-F1 | Predicted | AlphaFoldDB |
No variants for B1ZWH2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1ZWH2 | |||||
No associated diseases with B1ZWH2
8 regional properties for B1ZWH2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BRCT domain | 596 - 675 | IPR001357 |
| domain | Zinc-finger, NAD-dependent DNA ligase C4-type | 412 - 437 | IPR004149 |
| domain | NAD-dependent DNA ligase, OB-fold | 326 - 401 | IPR004150 |
| domain | NAD-dependent DNA ligase, adenylation | 5 - 322 | IPR013839 |
| domain | NAD-dependent DNA ligase, N-terminal | 5 - 452 | IPR013840 |
| active_site | NAD-dependent DNA ligase, active site | 116 - 145 | IPR018239 |
| conserved_site | NAD-dependent DNA ligase, conserved site | 336 - 351 | IPR033136 |
| domain | DisA/LigA, helix-hairpin-helix motif | 514 - 582 | 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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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 |
|---|---|
| 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. |
| 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 |
| MTPVEAQSRI | AELRAQVARH | DELYHRRAQP | QIGDFEYDAL | KRELAELEAA | WPQFARGASP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TEQVGDDRTE | GFQVYRHRER | MMSLDNTYSE | TELREFHDRL | VRELERDGLK | FVIEPKIDGL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVSITYEKGK | LVRAVTRGNG | IEGDDITTNA | LTIKSLPREL | KRADGVPLPA | VIEIRGEVFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TTEEFLRINR | QREEAGEPLY | ANPRNLAAGT | IKQLDPREVA | QRKLEVVLYG | RGYVEPASAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PETQAQFHGW | VKAWGLPTVE | RFWTATGADE | IWAAVQELDA | LRDTFAYATD | GAVVKLDAVP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LQRRAGSTSK | SPRWAMAYKF | APDRAETQLR | AITVQVGRTG | VLTPVAELDP | VQLAGTTVSR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ATLHNRDEIA | RKDIRVGDFV | YVEKAGEIIP | AVIGVNPARR | APECVPYVFP | EKCPECGTAV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VQLEGEVAVR | CPNFSCPVQV | RRRVQHFASK | ACVDIEGMGE | AMVDVLVEKG | WVHSVPDIYQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LKRENLLTLG | KSVEKSTDKL | LEAIEASKRA | ELWRFIHGLG | IPHAGAAAAK | DLARTFGGLE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RLASARYEDF | IREKASVIGG | IGETMALAIL | AYFAEPRNRA | VVDELVRVGV | QPVVPNSGSA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LAGKTFVLTG | TLPTLTRDEA | TAQIEAAGGK | VSSGVSKKTS | YVLAGEEAGS | KLEKARALAV |
| 670 | |||||
| PVIDEAEFLR | LLSGG |