O94429
Gene name |
mef2 (SPBC660.10) |
Protein name |
Ribosome-releasing factor 2, mitochondrial |
Names |
RRF2mt, Elongation factor G 2, mitochondrial, EF-G2mt, mEF-G 2 |
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPBC660.10 |
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 O94429
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O94429-F1 | Predicted | AlphaFoldDB |
No variants for O94429
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O94429 | |||||
No associated diseases with O94429
7 regional properties for O94429
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 669 - 798 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 26 - 314 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 354 - 418 | IPR004161 |
| domain | Small GTP-binding protein domain | 28 - 162 | IPR005225 |
| domain | Elongation factor G, domain III | 441 - 516 | IPR009022 |
| conserved_site | Tr-type G domain, conserved site | 69 - 84 | IPR031157 |
| domain | Elongation Factor G, domain II | 440 - 514 | IPR041095 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial translation | The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. 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; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code. |
| mitochondrial translational elongation | The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis in a mitochondrion. |
| ribosome disassembly | The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRIVWKPLK | IRLPVWRRYQ | SNISINSIRN | VGIIAHIDAG | KTTLTEKMLY | YGGFTSHFGN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VDTGDTVMDY | LPAERQRGIT | INSAAISFTW | RNQRINLIDT | PGHADFTFEV | ERSVAVLDGA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VAIIDGSAGV | EAQTKVVWKQ | ATKRGIPKVI | FVNKMDRVGS | SLGSTIRSIY | TNLDCPYPLV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LQLPVYSDGL | QERKFLGILD | ILQQKMILWD | TSDNKLGTDG | THVQELPIPE | SHMERFIEAR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NALVMSLCDV | DETLCDEYLE | NEDSLAFTND | RLFKIIKQKT | ISGNVVPVLC | GSSLKNIAVQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PIMDAIIDYL | PSPVEFYEKN | ASKETSSDKI | ISLDKRPLLA | KIFKVIHHAS | RGILTYVRVN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGTLSRGMMM | FNPRTKKSER | AIRLYNVFAD | QTQEVDCISA | GNIGVISGIK | QFHTGDIIIN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KENSKNFHEY | LSGNQSVISI | PEPVCIASIE | PYSLKDEPAL | LEALANMNRE | DPSFRYTQDL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ENGQLLIQGM | GIMHLQVSYE | RLVSEFGARA | SLGKVQVGYR | ETLIDVSFNS | VTLSTENKEN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LIINVYLIPI | SDEGDETLKK | YFSEGEIQKV | RSKGQEDGVL | FYGWKPENSC | TLPDHLSFQR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IQENIYFGIV | AGLSHGPLHG | FPLTNLQSFC | TISSFLSNDF | PLSLLTQASM | KATKNAVFSL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YKRSPKSFRI | LEPYMDVTIT | TPEEYVGIVS | KDLVGKRGAT | IKEITEIGKN | AASKDSQIAI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GILGERYLPA | DEPSSVKANN | ASSLLQSSSV | IKCIRAQVPL | EQILDYNSVI | SSLTKGNAKF |
| 790 | 800 | 810 | |||
| LMSHPMESQT | PKLVNYGSSF | HPMSMQRQKR | IFP |