Q5LRS1
Gene name |
ctaA |
Protein name |
Heme A synthase |
Names |
HAS, Cytochrome aa3-controlling protein |
Species |
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) |
KEGG Pathway |
sil:SPO2054 |
EC number |
1.17.99.9: With other acceptors |
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 Q5LRS1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5LRS1-F1 | Predicted | AlphaFoldDB |
No variants for Q5LRS1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5LRS1 | |||||
No associated diseases with Q5LRS1
5 regional properties for Q5LRS1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ATP-dependent RNA helicase DEAD-box, conserved site | 148 - 156 | IPR000629 |
| domain | Helicase, C-terminal | 214 - 375 | IPR001650 |
| domain | DEAD/DEAH box helicase domain | 26 - 191 | IPR011545 |
| domain | Helicase superfamily 1/2, ATP-binding domain | 21 - 218 | IPR014001 |
| domain | RNA helicase, DEAD-box type, Q motif | 2 - 30 | IPR014014 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.17.99.9 | With other acceptors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a heme protein. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| heme A biosynthetic process | The chemical reactions and pathways resulting in the formation of heme A, a derivative of heme found in cytochrome aa3. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSKRSIFEE | VSDGARAAAA | QPGMIDRGRG | GARGAIRAWL | AVLFALVVAM | IVVGGLTRLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DSGLSITEWR | PVTGAIPPLS | EADWQAEFDK | YKQIDQWRLQ | NQWMELADFK | SIYWWEWGHR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QLGRVIGLVW | ALGFFGFLLA | RKIPAGWTGR | LILPGVLGGV | QGAVGAWMVA | SGITQGEGMT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SVASYRLATH | LGLAFVILGL | LAWSILQLGR | SERDLMQARR | TKEARLFGLA | TGWLHLAFLQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ILIGALVAGL | DAGRNYVDWP | LMAGQVIPPD | PLELSPLWRN | FFENPGLVQF | IHRIVGYLLL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AYGVMVWLRG | RRSAHAQTRF | AFNAGFAALS | LQVVLGIVTV | LYAAPWQIAI | LHQLLAVGVF |
| 370 | |||||
| VLILRARFLC | AYPIATSIRG |