O67037
Gene name |
rgy1 |
Protein name |
Reverse gyrase 1 |
Names |
|
Species |
Aquifex aeolicus (strain VF5) |
KEGG Pathway |
aae:aq_886 |
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 O67037
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O67037-F1 | Predicted | AlphaFoldDB |
No variants for O67037
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O67037 | |||||
No associated diseases with O67037
1 regional properties for O67037
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Class II aldolase/adducin N-terminal | 11 - 239 | IPR001303 |
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. |
| 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). |
| DNA helicase activity | Unwinding of a DNA helix, driven by ATP hydrolysis. |
| DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA topological change | The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number. |
| DNA unwinding involved in DNA replication | The process in which interchain hydrogen bonds between two strands of DNA are broken or 'melted', generating unpaired template strands for DNA replication. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIKAIFDTLC | PNCGGEISAE | RLLKGLPCEK | CLPEEVNREE | VCQKLENGSF | KEFCELLSEL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KDWEDFFKEI | LGTSPWSLQK | SWARKVFLGR | SFAMLAPTGV | GKTTFGLSMA | SYLAKQGKKS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YIILPTQLLV | EQVSERIKTF | GVDEDRLIVW | GKLSEKKKKE | LKERIQKGDF | DILITTSMFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YKNYEILPKD | FSFIFVDDVD | SFLKTAKNVD | KVLYLLGFSE | EDIHKAFELI | RLKEKPNKSE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EDWEEIKKRS | EELREIAKKK | KGVLAVSSAT | GNPRSNRIKL | FRELLGFEVG | KPSVLLRNIV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ETYEETQNLK | ETLLKRVKEF | GKGGLVFVSS | DYGREAVEEV | KKFLESHGVK | AVTYEEDLKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FEKGEAQVAI | GISSFKNPLA | RGIDLPHVVR | YAIFYGVPKI | RVPLKVETSV | SHLLWALLSL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RPIILKDEKL | KSEVKKVDTW | IQRLRRYSFL | SDDFVEERPD | LKDRIENLRK | EVQEFLLRED |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IVEKIKNSEE | LTLRLGEEGF | ELVVADVTGY | LQASGRTSRM | YAGGLTKGLS | HVLVDDRRAF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KNLEKKVRWF | NQDINFKKIE | EVDLKEVLRE | IDEDRKKVRE | ILEGKVKAEQ | KEHVKPVLVV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VESPNKARTI | ANFFGKPMGR | KIGGIDVLEV | MVGDLYIMIT | ASLGHVFDLV | KDKEFHGVIA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KNGEYVPIYE | VIEGKENIVK | GLRELAQEVD | TVLIGTDPDT | EGEKIGWDLG | ALLSPYIPNV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ERIEFHEVTR | KAIKHAVENP | RDFNENLVKA | QLVRRIADRW | VGFEVSRIVQ | QAFDKHWLSG |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GRVQIPVLGW | IIEREKLYRK | KKHVVQITFK | ENGRWLRLGF | EFQDKKEAKE | FYENLKEIDV |
| 850 | 860 | 870 | 880 | 890 | 900 |
| EVLEEREELK | NPPPPFTTDT | MLKEASDRYR | ISVPKLMQLA | QELFEYGLIT | YHRTDSTRVS |
| 910 | 920 | 930 | 940 | 950 | 960 |
| DVGIGVAKEW | ISEELGKELF | YPRVWGEGGA | HECIRPTKPL | DVEDLRSMML | AGQLQNLTRE |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| HLLLYELIFK | RFMASQMKPV | KVKTKKVKVK | ALGREQELIL | TTEILEEGFN | KVYPLELQPD |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LKGSVYVEDK | KELKSVPMAY | LYTQGSLVEE | MKRRGIGRPS | TYATIVSKLL | ERGYVIERHG |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| FLIPTKLGKQ | VYEFLKSREK | IMPFVSEEFT | RKLEELMDKV | EEGKEDYLQV | LDELYKKVNE |
| FEKANV |