ID D3DZH8_METRM Unreviewed; 735 AA.
AC D3DZH8;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=mru_1806 {ECO:0000313|EMBL:ADC47656.1};
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47656.1, ECO:0000313|Proteomes:UP000008680};
RN [1] {ECO:0000313|EMBL:ADC47656.1, ECO:0000313|Proteomes:UP000008680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC {ECO:0000313|Proteomes:UP000008680};
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
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; CP001719; ADC47656.1; -; Genomic_DNA.
DR AlphaFoldDB; D3DZH8; -.
DR STRING; 634498.mru_1806; -.
DR KEGG; mru:mru_1806; -.
DR PATRIC; fig|634498.28.peg.1807; -.
DR eggNOG; arCOG01559; Archaea.
DR HOGENOM; CLU_002794_11_1_2; -.
DR Proteomes; UP000008680; 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:ADC47656.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000008680}.
FT DOMAIN 23..264
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 32..39
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 98..102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 152..155
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 735 AA; 81148 MW; 0C6E406150D89885 CRC64;
MVMILSRRDK MIAKIKELMY QPKNIRNIGI CAHIDHGKTT LSDNLLAGAG MISEELAGDQ
RFLDFDEQEQ ARGITIDAAN VSMVHEYHGD EYLINLIDTP GHVDFGGDVT RAMRAVDGAV
VVVCAVEGIM PQTETVLRQA LREKVKPVLF INKVDRLINE VKLGPEELAN KFIGIINEAN
KLITKMAPKD KKDEWLVKVD DGSVAFGSAY HNWAINIPMM QETGINFKDI IDYCNDENQK
ELAKKVPLAD VLLGMVVEHL PSPEVSQQYR CPNIWDGDIE SEAGQTMINT SPDGPLAVMV
TNVSVDKHAG EVATGRVYGG TVEQGSEVYL VGGQARSRVQ QVGVFFGPER VPTEKVPAGN
IVYITGAKGA TAGETICSPE NKIVEFEGIE HISEPVVTVA VEAKNTKDLP KLIEVLRQTA
KEDPTIHVNI NEETGEHLVS GMGELHLEVI GVRINNKGVD ILTSEPIVVY RETVAGKTPN
PVEGKSPNKH NRLYLEVSPL DDSIFEALQN GDIKEGKIKA KEEAQQFIDH GLDKEEARRV
WDVYNKSLFI NMTRGIQYLD EIKELVIEGF ESALEEGPVA NEIAMGMKFT LVDAKLHEDA
VHRGPAQILP AIRNAIKGGM MMADPTLLEP VQKVFINTPT DYMGSVTKEI LNRRGQIIDM
PTEGDMVNVE AKVPVAEMFG FAGEIRSATQ GRCLWSTENS GFERLPRELQ GQIVREIRQR
KGLAPEPFGP DHYLG
//
