ID C9RDK2_METVM Unreviewed; 726 AA.
AC C9RDK2;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891, ECO:0000256|HAMAP-Rule:MF_00054};
DE Short=EF-2 {ECO:0000256|HAMAP-Rule:MF_00054};
GN Name=fusA {ECO:0000256|HAMAP-Rule:MF_00054};
GN OrderedLocusNames=Metvu_1528 {ECO:0000313|EMBL:ACX73381.1};
OS Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
OS (Methanococcus vulcanius).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=579137 {ECO:0000313|EMBL:ACX73381.1, ECO:0000313|Proteomes:UP000002063};
RN [1] {ECO:0000313|EMBL:ACX73381.1, ECO:0000313|Proteomes:UP000002063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700851 / DSM 12094 / M7
RC {ECO:0000313|Proteomes:UP000002063};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lcollab F.I., Brettin T., Detter J.C.,
RA Han C., Tapia R., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinikova G., Sieprawska-Lupa M., Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus vulcanius M7.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome. {ECO:0000256|ARBA:ARBA00024731,
CC ECO:0000256|HAMAP-Rule:MF_00054}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00054}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00054}.
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DR EMBL; CP001787; ACX73381.1; -; Genomic_DNA.
DR RefSeq; WP_015733600.1; NC_013407.1.
DR AlphaFoldDB; C9RDK2; -.
DR STRING; 579137.Metvu_1528; -.
DR GeneID; 8513875; -.
DR KEGG; mvu:Metvu_1528; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR OrthoDB; 6290at2157; -.
DR Proteomes; UP000002063; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd01514; Elongation_Factor_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00054_A; EF_G_EF_2_A; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004543; Transl_elong_EFG/EF2_arc.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00490; aEF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00054};
KW Elongation factor {ECO:0000256|HAMAP-Rule:MF_00054,
KW ECO:0000313|EMBL:ACX73381.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00054};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00054}.
FT DOMAIN 19..260
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT MOD_RES 602
FT /note="Diphthamide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 726 AA; 80926 MW; 562DFDC52EDCB922 CRC64;
MGKRAKMISK IKELMEKYDK IRNIGICAHI DHGKTTLSDN LLAGAGMISK ELAGEQLALD
FDEEEAQRGI TIFAANVSMV HNYEGEEYLI NLIDTPGHVD FGGDVTRAMR AIDGAIVVVC
AVEGVMPQTE TVLRQALKER VKPVLFINKV DRLINELKLT PEELMNRFVK IINDINNLIR
KMAPEEFKDE WLVKVEDGSV AFGSAYNNWA ISVPFMKKSG ITFKDIIQYC EEDRQDELAD
RAPLHEVVLD MVIKHLPSPP EAQKYRIPHL WKGDLESEAG KAMLNCDPNG PLAGVITKII
VDKHAGAVSV CRLFSGRIKQ GDEVYMVTNQ QKAKIQQVSV FMGPERIPVE SISAGNICAL
VGLKEASAGE TICSPDKIIE PFEAITHISE PVITVAIEAK NTKDLPKLIE ILRQVAREDP
TVKVEINEET GEHLLSGMGE LHIEIITKLK IERDAGIPVE VGQPIVVYRE TVTGQSPVVE
SKSPNKHNKL YFVVEPLEEG VLKAYKEGKI PDVDTKRKLD DKIVQELIKA GMDPEEAKRV
MCIYEGNVLV NMTRGIVHLD EVKELIIQGF KEAMKNGPLA AEKCQGVKVK LMDAVLHEDA
IHRGPAQMIP AARFGVRDAM MQAKPVLLEP MQFVYINTPQ DFMGAAMREI SNRRGQILDM
EQEGDMAIIK AKCPVSEMFG FAGAIRGATQ GRCLWSIEFA GYEKVPRDMQ EQLIKQIRER
KGLKLE
//
