Q8W585
PR
Gene name |
FTSH8 (At1g06430, F12K11.22, F12K11_24) |
Protein name |
ATP-dependent zinc metalloprotease FTSH 8, chloroplastic |
Names |
AtFTSH8 |
Species |
Arabidopsis thaliana (Mouse-ear cress) |
KEGG Pathway |
ath:AT1G06430 |
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 Q8W585
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8W585-F1 | Predicted | AlphaFoldDB |
21 variants for Q8W585
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| tmp_1_1962454_C_A | 24 | K>N | No | 1000Genomes | |
| ENSVATH01018603 | 30 | T>I | No | 1000Genomes | |
| ENSVATH10696866 | 38 | A>V | No | 1000Genomes | |
| tmp_1_1962406_C_G | 40 | L>F | No | 1000Genomes | |
| ENSVATH10696865 | 44 | K>N | No | 1000Genomes | |
| ENSVATH10696794 | 64 | G>D | No | 1000Genomes | |
| tmp_1_1962231_C_T | 99 | V>I | No | 1000Genomes | |
| ENSVATH00008717 | 135 | S>N | No | 1000Genomes | |
| tmp_1_1962096_C_T | 144 | A>T | No | 1000Genomes | |
| ENSVATH01018601 | 148 | D>N | No | 1000Genomes | |
| ENSVATH04530023 | 171 | F>I | No | 1000Genomes | |
| tmp_1_1961626_C_A | 300 | R>S | No | 1000Genomes | |
| tmp_1_1961574_C_T | 318 | V>M | No | 1000Genomes | |
| ENSVATH04530018 | 404 | G>V | No | 1000Genomes | |
| tmp_1_1961117_G_A | 440 | A>V | No | 1000Genomes | |
| tmp_1_1961108_C_T | 443 | R>H | No | 1000Genomes | |
| tmp_1_1960708_C_A | 552 | V>L | No | 1000Genomes | |
| tmp_1_1960434_G_A | 613 | T>I | No | 1000Genomes | |
| tmp_1_1960339_G_A | 645 | L>F | No | 1000Genomes | |
| ENSVATH10696785 | 672 | A>G | No | 1000Genomes | |
| ENSVATH10696724 | 681 | T>I | No | 1000Genomes |
No associated diseases with Q8W585
1 regional properties for Q8W585
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GPCR, rhodopsin-like, 7TM | 53 - 400 | IPR017452 |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast | A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
| chloroplast envelope | The double lipid bilayer enclosing the chloroplast and separating its contents from the rest of the cytoplasm; includes the intermembrane space. |
| chloroplast thylakoid | Sac-like membranous structures (cisternae) in a chloroplast combined into stacks (grana) and present singly in the stroma (stroma thylakoids or frets) as interconnections between grana. An example of this component is found in Arabidopsis thaliana. |
| chloroplast thylakoid membrane | The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| 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. |
| thylakoid | A membranous cellular structure that bears the photosynthetic pigments in plants, algae, and cyanobacteria. In cyanobacteria thylakoids are of various shapes and are attached to, or continuous with, the plasma membrane. In eukaryotes they are flattened, membrane-bounded disk-like structures located in the chloroplasts; in the chloroplasts of higher plants the thylakoids form dense stacks called grana. Isolated thylakoid preparations can carry out photosynthetic electron transport and the associated phosphorylation. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| ATP-dependent peptidase activity | Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| PSII associated light-harvesting complex II catabolic process | The chemical reactions and pathways resulting in the breakdown of one or more components of the light-harvesting complex of photosystem II. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q2KJI7 | AFG3L2 | AFG3-like protein 2 | Bos taurus (Bovine) | PR |
| Q9UQ90 | SPG7 | Paraplegin | Homo sapiens (Human) | PR |
| Q9Y4W6 | AFG3L2 | AFG3-like protein 2 | Homo sapiens (Human) | PR |
| Q3ULF4 | Spg7 | Paraplegin | Mus musculus (Mouse) | PR |
| O88967 | Yme1l1 | ATP-dependent zinc metalloprotease YME1L1 | Mus musculus (Mouse) | PR |
| Q7TT47 | Spg7 | Paraplegin | Rattus norvegicus (Rat) | PR |
| O80983 | FTSH4 | ATP-dependent zinc metalloprotease FTSH 4, mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9FGM0 | FTSH11 | ATP-dependent zinc metalloprotease FTSH 11, chloroplastic/mitochondrial | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAASSACLLG | NGLSVYTTKQ | RFQKLGLDRT | SKVTVVKASL | DEKKHEGRRG | FFKLLLGNAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGVGLLASGN | ANADEQGQGV | SSSRMSYSRF | LEYLDKGRVE | KVDLYENGTI | AIVEAVSPEL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GNRIQRVRVQ | LPGLSQELLQ | KLRAKNIDFA | AHNAQEDQGS | PILNLIGNLA | FPVILIGGLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLSRRSSGGM | GGPGGPGFPL | QIGQSKAKFQ | MEPNTGVTFD | DVAGVDEAKQ | DFMEVVEFLK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KPERFTAVGA | RIPKGVLLVG | PPGTGKTLLA | KAIAGEAGVP | FFSISGSEFV | EMFVGVGASR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VRDLFKKAKE | NAPCIVFVDE | IDAVGRQRGT | GIGGGNDERE | QTLNQLLTEM | DGFEGNTGVI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VVAATNRADI | LDSALLRPGR | FDRQVSVDVP | DVKGRTDILK | VHSGNKKFES | GVSLEVIAMR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TPGFSGADLA | NLLNEAAILA | GRRGKTAISS | KEIDDSIDRI | VAGMEGTVMT | DGKSKSLVAY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HEVGHAICGT | LTPGHDAVQK | VTLIPRGQAR | GLTWFIPSDD | PTLISKQQLF | ARIVGGLGGR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AAEEVIFGES | EVTTGAVSDL | QQITGLAKQM | VTTFGMSEIG | PWSLMDSSEQ | SDVIMRMMAR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NSMSEKLAND | IDTAVKTLSD | KAYEIALSQI | RNNREAMDKI | VEILLEKETM | SGDEFRAILS |
| 670 | 680 | ||||
| EFTEIPPENR | VASSTSTSTP | TPASV |