Q10179
Gene name |
grs1 (SPAC3F10.03) |
Protein name |
Putative glycine--tRNA ligase |
Names |
Diadenosine tetraphosphate synthetase, Ap4A synthetase, Glycyl-tRNA synthetase, GlyRS |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC3F10.03 |
EC number |
6.1.1.14: Ligases forming aminoacyl-tRNA and related compounds |
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 Q10179
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q10179-F1 | Predicted | AlphaFoldDB |
6 variants for Q10179
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_2821784_G_C | 100 | G>A | No | Jeffares_SNPs | |
| I_2821969_G_C | 162 | E>Q | No | Jeffares_SNPs | |
| I_2822069_A_G | 195 | E>G | No | Jeffares_SNPs | |
| I_2822816_C_T | 444 | S>L | No | Jeffares_SNPs | |
| I_2822821_C_T | 446 | P>S | No | Jeffares_SNPs | |
| I_2823173_A_G | 563 | N>S | No | Jeffares_SNPs |
No associated diseases with Q10179
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.14 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glycine-tRNA ligase activity | Catalysis of the reaction: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). |
| protein dimerization activity | The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits. |
| transferase activity | Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cytoplasmic translation | The chemical reactions and pathways resulting in the formation of a protein in the cytoplasm. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein. |
| diadenosine tetraphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of diadenosine tetraphosphate, a derivative of the nucleoside adenosine with four phosphate groups attached. |
| glycyl-tRNA aminoacylation | The process of coupling glycine to glycyl-tRNA, catalyzed by glycyl-tRNA synthetase. The glycyll-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a glycine-accepting tRNA. |
| mitochondrial glycyl-tRNA aminoacylation | The process of coupling glycine to glycyl-tRNA in a mitochondrion, catalyzed by glycyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTEVSKAAAF | DRTQFEELMK | KRFFFSPSFQ | IYGGISGLYD | YGPPGSALQS | NLVDIWRKHF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIEESMLEVD | CSMLTPHEVL | KTSGHVDKFA | DWMCKDPATG | EIFRADHLVE | EVLEARLKGD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KEARGQNSND | QPEESDDKKK | RKKKVKEIRA | TRLDDKTVEE | YEFILAQIDN | YDGDQLGELM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KKYDIRNPAT | NGELETPRQF | NLMFETQIGP | SGGLKGYLRP | ETAQGQFLNF | SRLLEFNNGK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VPFASAMVGK | AFRNEISPRS | GLLRVREFLM | AEVEHFVDPK | NKEHDRFDEV | SHMPLRLLPR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GVQLEGKTDI | LEMPIGDAVK | KGIVDNTTLG | YFMARISLFL | EKIGIDMNRV | RFRQHMSNEM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AHYACDCWDA | EIQCSYGWIE | CVGCADRSAY | DLSVHSKATK | TPLVVQEALP | EPVVVEQFEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EVNRKKFGPR | FKRDAKAVEE | AMISWPESEK | VEKSAQLVAE | GKIIVNVNGV | EHTVESDLVT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IEKRKHTEHI | RTYTPNVIEP | SFGLGRILYV | LMEHAYWTRP | EDVNRGVLSF | PASIAPIKAL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IVPLSRNAEF | APFVKKLSAK | LRNLGISNKI | DDSNANIGRR | YARNDELGTP | FGLTVDFETL |
| 610 | 620 | 630 | 640 | 650 | |
| QNETITLRER | DSTKQVRGSQ | DEVIAALVSM | VEGKSSFEDA | LAKFGEFKST | QE |