CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015651
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G 
Protein Synonyms/Alias
 EF-G 
Gene Name
 fusA 
Gene Synonyms/Alias
 DVU_1300 
Created Date
 July 27, 2013 
Organism
 Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIM 
NCBI Taxa ID
 882 
Lysine Modification
Position
Peptide
Type
References
430ALSAALAKLAKEDPSmethylation[1]
Reference
 [1] Post-translational modifications of Desulfovibrio vulgaris Hildenborough sulfate reduction pathway proteins.
 Gaucher SP, Redding AM, Mukhopadhyay A, Keasling JD, Singh AK.
 J Proteome Res. 2008 Jun;7(6):2320-31. [PMID: 18416566] 
Functional Description
 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 17 24 GTP (By similarity).
 NP_BIND 81 85 GTP (By similarity).
 NP_BIND 135 138 GTP (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 691 AA 
Protein Sequence
MARVVPIDMQ RNIGIMAHID AGKTTTTERI LFYTGVSHKI GEVHDGAATM DWMEQEQERG 60
ITITSAATTC FWREHRVNII DTPGHVDFTI EVERSLRVLD GAVCVFDAVA GVEPQSETVW 120
RQADRYGVPR ICFVNKMDRI GASFERCVGM IRDRLRAKPI PVQLPIGAED RFEGVIDLIT 180
GKAVTFDKAS KGQTFNVGDV PAEYRDQYDA MRFEMIEAVA EEDEALMEKY LGGEELTVEE 240
IISCVRKATI ARNIVPVLCG SAFRNMGVQP LLDAVVDFLP SPVDIEQMKG VNPDKEEETI 300
VCPCDDKEPL AALVFKLFSD PYIGHLSFCR IYSGFIESGM TVLNANTGKR ERVGRLLKMH 360
ANKREEIKWA GAGDIVALVG LKLASTGDTI CDEKRPVVLE SLDIPEPVIE VAIEPKTKAD 420
RDALSAALAK LAKEDPSFRV KGDDETNQTL IAGMGELHLE IIVDRLTREF SVNANVGKPQ 480
VAYRETITKP GKADTKHVKQ SGGRGQYGHA VIEIEPNPGK GYEFVNSITG GVIPKEYIAP 540
IDKGIQDALK SGILSGFPTV DIKVNLVFGS YHDVDSSEQA FYVTGSMAIK EAIAKSGPVL 600
LEPIMDVEVV TPDEYLGDVM GDLNGRRGKV QSMEARVGAQ SIRAQVPLSE MFGYATDLRS 660
KTQGRATFSM QFHHYERVPA ALAEELVKKK G 691 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
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.