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 P63392
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P63392-F1 | Predicted | AlphaFoldDB |
No variants for P63392
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P63392 | |||||
No associated diseases with P63392
7 regional properties for P63392
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ABC transporter-like, ATP-binding domain | 610 - 843 | IPR003439 |
| domain | AAA+ ATPase domain | 635 - 820 | IPR003593 |
| domain | Siderophore-interacting protein, C-terminal domain | 131 - 241 | IPR007037 |
| domain | ABC transporter type 1, transmembrane domain | 294 - 575 | IPR011527 |
| domain | FAD-binding 9, siderophore-interacting | 61 - 113 | IPR013113 |
| conserved_site | ABC transporter-like, conserved site | 746 - 760 | IPR017871 |
| domain | FAD-binding domain, ferredoxin reductase-type | 15 - 122 | IPR017927 |
2 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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
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. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
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 |
| MARGLQGVML | RSFGARDHTA | TVIETISIAP | HFVRVRMVSP | TLFQDAEAEP | AAWLRFWFPD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PNGSNTEFQR | AYTISEADPA | AGRFAVDVVL | HDPAGPASSW | ARTVKPGATI | AVMSLMGSSR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FDVPEEQPAG | YLLIGDSASI | PGMNGIIETV | PNDVPIEMYL | EQHDDNDTLI | PLAKHPRLRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RWVMRRDEKS | LAEAIENRDW | SDWYAWATPE | AAALKCVRVR | LRDEFGFPKS | EIHAQAYWNA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GRAMGTHRAT | EPAATEPEVG | AAPQPESAVP | APARGSWRAQ | AASRLLAPLK | LPLVLSGVLA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALVTLAQLAP | FVLLVELSRL | LVSGAGAHRL | FTVGFAAVGL | LGTGALLAAA | LTLWLHVIDA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RFARALRLRL | LSKLSRLPLG | WFTSRGSGSI | KKLVTDDTLA | LHYLVTHAVP | DAVAAVVAPV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GVLVYLFVVD | WRVALVLFGP | VLVYLTITSS | LTIQSGPRIV | QAQRWAEKMN | GEAGSYLEGQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PVIRVFGAAS | SSFRRRLDEY | IGFLVAWQRP | LAGKKTLMDL | ATRPATFLWL | IAATGTLLVA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| THRMDPVNLL | PFMFLGTTFG | ARLLGIAYGL | GGLRTGLLAA | RHLQVTLDET | ELAVREHPRE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PLDGEAPATV | VFDHVTFGYR | PGVPVIQDVS | LTLRPGTVTA | LVGPSGSGKS | TLATLLARFH |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DVERGAIRVG | GQDIRSLAAD | ELYTRVGFVL | QEAQLVHGTA | AENIALAVPD | APAEQVQVAA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| REAQIHDRVL | RLPDGYDTVL | GANSGLSGGE | RQRLTIARAI | LGDTPVLILD | EATAFADPES |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EYLVQQALNR | LTRDRTVLVI | AHRLHTITRA | DQIVVLDHGR | IVERGTHEEL | LAAGGRYCRL |
| 850 | |||||
| WDTGQGSRVA | VAAAQDGTR |