P47264
Gene name |
MG018 |
Protein name |
Uncharacterized ATP-dependent helicase MG018 |
Names |
|
Species |
Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasmoides genitalium) |
KEGG Pathway |
mge:MG_018 |
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 P47264
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P47264-F1 | Predicted | AlphaFoldDB |
No variants for P47264
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P47264 | |||||
No associated diseases with P47264
No regional properties for P47264
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P47264 | |||
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent activity, acting on DNA | Catalytic activity that acts to modify DNA, driven by ATP hydrolysis. |
| ATP-dependent chromatin remodeler activity | An activity, driven by ATP hydrolysis, that modulates the contacts between histones and DNA, resulting in a change in chromosome architecture within the nucleosomal array, leading to chromatin remodeling. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| helicase activity | Catalysis of the reaction: ATP + H2O = ADP + phosphate, to drive the unwinding of a DNA or RNA helix. |
| hydrolase activity | Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. |
| zinc ion binding | Binding to a zinc ion (Zn). |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTVAEIKKLA | LNNQVFNEAK | ALLEKGNVIF | PKKFLKRKKI | IIEVLDGKVF | KVQINLKTAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHLDCSCSND | KQNCVHIIAA | LLKYNDLKNQ | DNKEFDLNKA | DKLECKEVEI | LIENVSLAIV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NGSWKLKIGF | VINIDKVQTN | TTALRFYCCD | NKDVYFLHTE | DEQLFRIALD | KFNSVERQTL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LIFDQLNKTK | QMQYENNSLL | FNLDQFLSLV | KEVKKPSLFL | LNEDKTDNIL | FLRSQHKING |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSHVCGFLNN | KVFDFVSYNE | KTKQIVLRLA | YLNKFTDFKF | PYNINIYKLA | FGETLFFHFL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IHLKMNGFKN | IFFQSDVVIV | KESEYLPKMF | LTIEFNTQKN | KFITDAFFKY | KNKNSNTLTT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VYPHRYYLAQ | KTNTSNFNRL | LFYEQALQRF | YEELFQIDYL | RRFENIPIKD | KNQIALFKTV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FDDYKTIDLA | ELKLTSNLLN | YKQLHFSISD | IKALKIEDRQ | LKIEFKAGGI | DLKLIKSVLS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NYYKGNAICI | GEDGWYDLND | ENAKALISFW | SQIDLRNATC | DANNNLLLAK | YHLFEVVDTI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SKYTDVTNLL | DEKTALQLKI | ASENQFHLSL | DNNQINNLRK | YQKEGVKWIR | ALEDNQFGGI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LADEMGLGKT | AQVIFAMLDS | YQSTKSLLPS | LIIVPASLLL | NWKSEFQKFA | PHVKIVTANG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NFKERSQVYE | SLKNQILLMS | FNVLRSDIKW | ISQKKFHYVV | IDEAQGIKNE | NSTVTKAAKK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IKGNFCLALT | GTPIENRLLD | LWSCFDFVLP | NFLGNKKQFS | DQFEKEKNDE | SFQKLMKKTS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PFILRRTKNK | VLKELPKKII | TDIYVELSEE | HQKLYDKQKT | DGLKEIKESD | AKNALNILSL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ILKLRHICSL | VKDNDVNDFE | DNSKANAALN | IIYEALENKR | KVILFTQFLD | VIDCFKQTLK |
| 910 | 920 | 930 | 940 | 950 | 960 |
| NQKIDHLVFD | GRKTVKNRNT | IIQKFNSAKE | PCVMLASLKA | GGVGINLTAA | EVVIHFDVWW |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| NSAVENQATD | RAHRIGQSKT | VQVYRIIAKN | TIEERVCQVQ | NQKQELVKKT | LVEDVNFFKS |
| 1030 | |||||
| LSHEELLKLF | E |