Q2GEH0
Gene name |
secA |
Protein name |
Protein translocase subunit SecA |
Names |
|
Species |
Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia sennetsu) |
KEGG Pathway |
nse:NSE_0232 |
EC number |
7.4.2.8: Linked to the hydrolysis of a nucleoside triphosphate |
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 Q2GEH0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2GEH0-F1 | Predicted | AlphaFoldDB |
No variants for Q2GEH0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2GEH0 | |||||
No associated diseases with Q2GEH0
8 regional properties for Q2GEH0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Helicase, C-terminal | 410 - 614 | IPR001650 |
| domain | SecA DEAD-like, N-terminal | 5 - 390 | IPR011115 |
| domain | SecA Wing/Scaffold | 596 - 793 | IPR011116 |
| domain | SecA, preprotein cross-linking domain | 228 - 346 | IPR011130 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 89 - 247 | IPR014001 |
| domain | SecA motor DEAD | 2 - 599 | IPR014018 |
| conserved_site | SecA conserved site | 488 - 503 | IPR020937 |
| domain | SecA, C-terminal helicase domain | 408 - 569 | IPR044722 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.4.2.8 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| protein-exporting ATPase activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + protein+(in) -> ADP + phosphate + protein+(out); drives the concomitant secretion of proteins. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| intracellular protein transmembrane transport | The directed movement of proteins in a cell, from one side of a membrane to another by means of some agent such as a transporter or pore. |
| protein import | The targeting and directed movement of proteins into a cell or organelle. Not all import involves an initial targeting event. |
| protein targeting | The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLDLVHKIFD | SRNRKIKRKL | KDGLEQVNSL | ETRIRDLSSD | ELRNKTSEFK | ERLFKQSASL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DEILPEAYAC | VREASLRTLG | MRHFDVQIMG | GIVLHWGMIS | EMHTGEGKTL | VATLAAYLNA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LSEKGVHVVT | VNDYLARRDT | EWMKQIYRHL | GLQVSCITSD | MRDPERAHAY | KADITYATNN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ELGFDYLRDN | MKFSKGEMVQ | RDLHYAIVDE | VDSILIDEAR | TPLIISGVTD | NASYLYASMN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KLAEKLDSTL | YIVDEKTRTV | SLTEEGQEAI | EKLLMAEKFI | ESGSSLYEPQ | NLQLVHCLNQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLKAINLFQK | NKDYIVQDGQ | IVLIDEFTGR | MMHGRRYSEG | LHQALEAKEN | LKIQNENQTL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASITFQNYFR | MYGKLSGMTG | TAATEREEFS | TIYGLEVVQI | PSHLPVRRVD | HDDEIYASKK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EKYEAILALA | KECHEKLQPI | LIGTTSIENS | EELSRELKKA | KLKHSVLNAK | QHAFEAEIIA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QAGKPGAITI | ATNMAGRGTD | IQLGGNINFN | ISANDEAEKE | HAKNEEIVRK | AGGLYVIGTE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RHESRRIDNQ | LRGRSGRQGD | PGESKFFLSL | DDDLLRVFGT | SGIRNMLKKQ | LSNNGAIKHS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| YITRSLEKAQ | KKVESRNYEI | RKNLIKFDDV | INEQRKVIFS | QRNNIMESGD | IDLLPIVTEV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NAKTLENARS | KNFYDISTLI | HSMQSIYNED | FKELHKTEDI | DGFIDSKTKS | IIAEKERAHV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EFLLEIKKRI | MIAILDQLWK | EHLQFLENLR | LSINLKAVAQ | KNPLIEFKHE | AFQAFQRLSE |
| 790 | 800 | ||||
| RWHENIIASF | VRVKLVERMH | MKVM |