Q54BU4
Gene name |
abcB1 (mrpA, DDB_G0293416) |
Protein name |
ABC transporter B family member 1 |
Names |
ABC transporter ABCB.1 |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0293416 |
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 Q54BU4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54BU4-F1 | Predicted | AlphaFoldDB |
No variants for Q54BU4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54BU4 | |||||
No associated diseases with Q54BU4
4 regional properties for Q54BU4
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ABC-type transporter activity | Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATPase-coupled transmembrane transporter activity | Primary active transporter of a solute across a membrane, via the reaction: ATP + H2O = ADP + phosphate, to directly drive the transport of a substance across a membrane. The transport protein may be transiently phosphorylated (P-type transporters), or not (ABC-type transporters and other families of transporters). Primary active transport occurs up the solute's concentration gradient and is driven by a primary energy source. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| chemotaxis | The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis). |
| culmination involved in sorocarp development | The process whose specific outcome is the progression of the culminant over time, from its formation to the mature structure. Culmination begins with a morphogenetic change of the finger-like or migratory slug giving rise to an organized structure containing a stalk and a sorus. This process is the final stage of sorocarp development. |
| hyperosmotic response | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. |
| transmembrane transport | The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTKKNFNDEE | NESLLETYNK | QQQKQSISTT | NRSDQKFGIN | NANKQFSLNN | KKSINGEEID |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EEELIEDTIF | FKFKLDSKQR | NSIKLFIQIV | SLVILAGYLI | SINALYFSTN | ARSIIFYPSI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NSNTTDSGSV | SPTSTPSPTP | TPTPSPTSLL | LQTLTSTTTS | YDSSEIEALN | GGTFNMKYFF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YFSTFDILLI | SYFISLFWLL | LIFSDSFIYH | TISYIITIIA | LIYNVIKSYF | TITQILSINN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NIITTSSSSN | EIYNGSDSYL | PNESPLFDSL | KVREIIIVIV | LVGIPLMVLF | LVLHIITLQL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SFKKYKRLSD | KEKQFYNQSN | EEKRLNKKVE | VKHSNLKRLI | QLSRPELPII | LAAMVALVFS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SLTSLAMPYF | FGSIVQVVAT | THSFNNLNSS | TLALVVIFVI | GSISTLVRSW | LFYLAGQKFV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ARIRRNLFSS | IVNQEIGYFD | QCRTGELLSR | LSSDSQVIQN | SVTVNISMLF | RYTIQIIGSV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ILLFITNWRL | TLLMLGIVPV | LAISTVVYGK | KIKQLGKQFQ | DELAKSSTTG | EEVISNIRTV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RSFSKEQKFI | DLYSKDINGS | YLIGKSLAVA | TGVFSGIVFL | VAQLAIVLIV | YVGARQVLDG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| TLSTGDLTSF | LLYTLSLAMS | LAFISSLMTD | FLKAIGSSDR | IFEIFDRVPA | INVSGGKQIQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NPLGEIELKD | VEFSYPTRPN | NSVLKGLNLK | LSKGTITALV | GPSGGGKSTV | IAMIERFYDP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NSGSITFDGI | DIKELDPVWY | RGIIGYVSQE | PVLFAGSIKD | NITFGNDSAT | MDQIISAAEK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ANAHSFIEEF | ENGYDTIVGE | RGVRLSGGQK | QRVAIARAMI | QNPMILLLDE | ATSALDAESE |
| 850 | 860 | 870 | 880 | 890 | 900 |
| YLVKQAIDEI | MKDRTVIVIA | HRLSTVINAN | TVVVINQGKI | EEMGTHKELL | NNTDGIYHNL |
| VKRQLSSDD |