| Tag | Content |
|---|
| CPLM ID | CPLM-011522 |
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 |
Gene Name | Gfm1 |
Gene Synonyms/Alias | Efg; Efg1; Gfm |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 540 | VPFDFTHKKQSGGAG | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis (By similarity). |
Sequence Annotation | NP_BIND 54 61 GTP (By similarity).
NP_BIND 121 125 GTP (By similarity).
NP_BIND 175 178 GTP (By similarity).
MOD_RES 176 176 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Complete proteome; Direct protein sequencing; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 751 AA |
Protein Sequence | MRLLRITAGL GRGPLPRVPA ILGWQGKQAN WKTYRWCSSG SIPNEKIRNI GISAHIDSGK 60
TTLTERVLYY TGRIATMHEV KGKDGVGAVM DSMELERQRG ITIQSAATYT MWRDVNINII 120
DTPGHVDFTI EVERALRVLD GAVLVLCAVG GVQCQTMTVS RQMKRYNVPF LTFINKLDRM 180
GSNPARALQQ MRSKLNHNAA FVQIPIGLEG DFKGIIDLIE ERAIYFDGDF GQIVRYDEIP 240
ADLRAAAADH RQELIECVAN SDEQLGELFL EEKIPSVSDL KLAIRRATLS RSFTPVFLGS 300
ALKNKGVQPL LDAVLEFLPN PSEVQNYALL NQNDSKEKNK ILMNPKRDDS HPFVGLAFKL 360
EAGRFGQLTY VRNYQGELKK GSTIYNTRTG KKVRVQRLVR MHADMMEDVE EVYAGDICAL 420
FGIDCASGDT FTNKDNSDLS MESIHVPDPV ISVAMKPSNK NDLEKFSKGI ARFTREDPTF 480
KVHFDTESKE TIVSGMGELH LEIYAQRMER EYGCPCITGK PKVAFRETVT APVPFDFTHK 540
KQSGGAGQYG KVIGVLEPLA PEDYTKLEFS DETFGANVPK QFVPAVEKGF LDACEKGPLS 600
GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAS ATLCIIEPIM SVEVIAPNEF 660
QGAVFAGINR RHGVITGQDG IEDYFTLYAD VPLNNMFGYS TELRSCTEGK GEYTMEYNRY 720
QPCSPSTQEE LVNKYLEATG QLPVKKGKAK N 751 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. 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. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |