Q46577
Gene name |
uvrA |
Protein name |
UvrABC system protein A |
Names |
UvrA protein, Excinuclease ABC subunit A |
Species |
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
KEGG Pathway |
dra:DR_1771 |
EC number |
|
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 Q46577
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q46577-F1 | Predicted | AlphaFoldDB |
No variants for Q46577
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q46577 | |||||
No associated diseases with Q46577
6 regional properties for Q46577
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 644 - 975 | IPR003439 |
| domain | AAA+ ATPase domain | 671 - 960 | IPR003593 |
| conserved_site | ABC transporter-like, conserved site | 527 - 541 | IPR017871-1 |
| conserved_site | ABC transporter-like, conserved site | 868 - 882 | IPR017871-2 |
| domain | UvrA, interaction domain | 131 - 239 | IPR041102 |
| domain | UvrA DNA-binding domain | 297 - 407 | IPR041552 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| excinuclease repair complex | Any of the protein complexes formed by the UvrABC excinuclease system, which carries out nucleotide excision repair. Three different complexes are formed by the 3 proteins as they proceed through the excision repair process. First a complex consisting of two A subunits and two B subunits bind DNA and unwind it around the damaged site. Then, the A subunits disassociate leaving behind a stable complex between B subunits and DNA. Now, subunit C binds to this B+DNA complex and causes subunit B to nick the DNA on one side of the complex while subunit C nicks the DNA on the other side of the complex. DNA polymerase I and DNA ligase can then repair the resulting gap. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| excinuclease ABC activity | Catalysis of the hydrolysis of ester linkages within deoxyribonucleic acid at sites flanking regions of damaged DNA to which the Uvr ABC excinuclease complexes bind. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| nucleotide-excision repair | A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts). |
| SOS response | An error-prone process for repairing damaged microbial DNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQDKLIVRGA | REHNLKDITV | ELPRDRFVVI | TGVSGSGKST | LAFDTIYAEG | QRRYVESLSA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YARQFLGLME | KPDVDSITGL | SPAISIDQKT | TSHNPRSTVG | TVTEIHDYLR | LLYARVGTPY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CPICGRKIEK | QSPSEVTDRL | LAGFPDKRAI | LLAPAVRGRK | GEYKKLFADL | RREGYARVRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DGTLYELEEA | EKLKLEKFEK | HDVDIVIDRL | TLRESDRSRI | AESVELGIRR | GEGLLRVLLP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DAGEDGGAHE | ELYSEKFACP | EHGSVLEELE | PRSFSFNSPY | GACGDCAGIG | AKQEFSPERI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IDEKLSIAGG | AIIPWTKKGA | DAGIYYWDKL | KALAEHLDFD | LKTPWKDLPA | KAQKAVLHGP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GEAFEVVYRR | GGKETMRFMT | EFEGVITNLE | RRYADTESEF | MRERLEELME | LRPCPTCGGT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RYKPEILAVR | VGGLNISQTS | GMSVLDADAF | FQQLQEGELD | HAAIEPFLKR | HTGGTAKAHG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PLHYEYDLGT | FGAAVAAPIL | RAIRTRLKFL | VDVGLDYLSL | DRTANTLSGG | EAQRIRLATQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VGSGLTGVLY | VLDEPSIGLH | PKDNGRLIGT | LKNLRDLGNS | LLVVEHDEDT | MLEADYLIDM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GPGAGVHGGE | VIASGTPEQV | KQDKNSLTGK | YLRGEMKIEV | PAERRPGNGK | FLKVFGARQN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NLQDVDVSIP | LGTMTVVTGP | SGSGKSTLIH | DILHATLARE | LNGAKTTPGL | YDRIEGMEQL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DKVIEIDQSP | IGRTPRSNPA | TYTGVFTEIR | DLFTRTPEAR | RRGYQAGRFS | FNVKGGRCEH |
| 790 | 800 | 810 | 820 | 830 | 840 |
| CKGDGVMKIE | MNFLPDIYVP | CEVCHGARYN | RETLEVKYNH | KTIADVLDLT | VEDAHEFFEA |
| 850 | 860 | 870 | 880 | 890 | 900 |
| IPTIERKMQL | LLDVGLGYMK | IGQPSTTLSG | GEAQRIKLAT | ELSKRATGRT | IYILDEPTTG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LHFEDVRKLM | DVLQRLAEGG | NTLVIIEHNL | DVMKSADYLI | DLGPEGGVRG | GTVVAVGTPE |
| 970 | 980 | 990 | 1000 | 1010 | |
| EVAAHPTSYT | GEYLRKVPGI | VAAEPRARGE | KAEKPAKAKA | PAKKRTKKQT | ELVEAD |