CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005336
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
 MEF1 
Gene Synonyms/Alias
 YLR069C; L2195 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
203PRVTFINKMDRMGSDacetylation[1]
386AFKLEEGKYGQLTYVacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
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). 
Sequence Annotation
 NP_BIND 77 84 GTP (By similarity).
 NP_BIND 148 152 GTP (By similarity).
 NP_BIND 202 205 GTP (By similarity).
 MOD_RES 34 34 Phosphoserine.
 MOD_RES 38 38 Phosphoserine.  
Keyword
 Complete proteome; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 761 AA 
Protein Sequence
MSVQKMMWVP RKMVGGRIPF FTCSKVFSGF SRRSFHESPL ARSTYEEEKV LVDEIKQKLT 60
PDDIGRCNKL RNIGISAHID SGKTTFTERV LYYTKRIKAI HEVRGRDNVG AKMDSMDLER 120
EKGITIQSAA TYCSWDKEGK NYHFNLIDTP GHIDFTIEVE RALRVLDGAV LVVCAVSGVQ 180
SQTVTVDRQM RRYNVPRVTF INKMDRMGSD PFRAIEQLNS KLKIPAAAVQ IPIGSESSLS 240
GVVDLINRVA IYNKGDNGEI IEKGPVPENL KPLMEEKRQL LIETLADVDD EMAEMFLEEK 300
EPTTQQIKDA IRRSTIARSF TPVLMGSALA NTGIQPVLDA IVDYLPNPSE VLNTALDVSN 360
NEAKVNLVPA VQQPFVGLAF KLEEGKYGQL TYVRVYQGRL RKGNYITNVK TGKKVKVARL 420
VRMHSSEMED VDEVGSGEIC ATFGIDCASG DTFTDGSVQY SMSSMYVPDA VVSLSITPNS 480
KDASNFSKAL NRFQKEDPTF RVKFDPESKE TIISGMGELH LEIYVERMRR EYNVDCVTGK 540
PQVSYRESIT IPADFDYTHK KQSGGAGQYG RVIGTLSPVD DITKGNIFET AIVGGRIPDK 600
YLAACGKGFE EVCEKGPLIG HRVLDVKMLI NDGAIHAVDS NELSFKTATM SAFRDAFLRA 660
QPVIMEPIMN VSVTSPNEFQ GNVIGLLNKL QAVIQDTENG HDEFTLKAEC ALSTMFGFAT 720
SLRASTQGKG EFSLEFSHYA PTAPHVQKEL ISEFQKKQAK K 761 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; ISA:SGD.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0070125; P:mitochondrial translational elongation; ISA:SGD. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR027417; P-loop_NTPase.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005225; Small_GTP-bd_dom.
 IPR004540; Transl_elong_EFG/EF2.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C
 SM00889; EFG_IV 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.