| Tag | Content |
|---|
| CPLM ID | CPLM-023403 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Elongation factor G, mitochondrial |
Protein Synonyms/Alias | EF-Gmt; Elongation factor G 1, mitochondrial; mEF-G 1; Elongation factor G1; dEF-G1; Protein iconoclast |
Gene Name | ico |
Gene Synonyms/Alias | CG4567 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 171 | PCLAFINKLDRLGSN | acetylation | [1] | | 582 | QFVPGVEKGYREMAE | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). Essential during development as it acts as a retrograde signal from mitochondria to the nucleus to slow down cell proliferation if mitochondrial energy output is low. |
Sequence Annotation | NP_BIND 49 56 GTP (By similarity).
NP_BIND 116 120 GTP (By similarity).
NP_BIND 170 173 GTP (By similarity). |
Keyword | Complete proteome; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 745 AA |
Protein Sequence | MSLITRLLTG NNTLRLRALK SLGKAGYSSH AKFSEHKPIE RIRNIGISAH IDSGKTTLTE 60
RILFYTGRIA EMHEVRGKDN VGATMDSMEL ERQRGITIQS AATYTLWKDT NINIIDTPGH 120
VDFTVEVERA LRVLDGAVLV LCAVGGVQSQ TLTVNRQMKR YNVPCLAFIN KLDRLGSNPY 180
RVLSQMRSKM NHNAAFIQLP IGVESNCKGI VDLVREKAIY FEGEHGMDIR LDEIPQDMRV 240
ESLERRQELI EHLSNADETL GELFLEEKPF TEDDIKAALR RTCINRTFTP VLVGTALKNK 300
GVQPLLDAVL DYLPNPGEVE NLGFIEKEGQ DPEKVVLNPA RDGKDPFVGL AFKLEAGRFG 360
QLTYLRCYQG VLRKGDNIFN ARTNKKVRIA RLVRLHSNQM EDVNEVYAGD IFALFGVDCA 420
SGDTFTTNPK NNLSMESIFV PEPVVSMAIK PNNTKDRDNF SKAIARFTKE DPTFHFFFDN 480
DVKETLVSGM GELHLEIYAQ RMEREYGCPV TLGKPKVAFR ETLVGPCEFD YLHKKQSGGS 540
GQYARIIGVM EPLPPNQNTL LEFVDETVGT NVPKQFVPGV EKGYREMAEK GMLSGHKLSG 600
IRFRLQDGGH HIVDSSELAF MLAAHGAIKE VFQNGSWQIL EPIMLVEVTA PEEFQGAVMG 660
HLSKRHGIIT GTEGTEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFTME YSRYSPCLPD 720
VQDQIVRQYQ ESQGLAQPDK KKKKN 745 |
Gene Ontology | GO:0005739; C:mitochondrion; NAS:UniProtKB. GO:0005634; C:nucleus; IDA:FlyBase. GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0003924; F:GTPase activity; ISS:UniProtKB. GO:0003746; F:translation elongation factor activity; ISS:UniProtKB. GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
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PRINTS | |