ID A0A366M8C1_9EURY Unreviewed; 725 AA.
AC A0A366M8C1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ECO:0000313|EMBL:RBQ22491.1};
GN ORFNames=ALNOE001_19230 {ECO:0000313|EMBL:RBQ22491.1};
OS Methanobrevibacter sp. NOE.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=2006182 {ECO:0000313|EMBL:RBQ22491.1, ECO:0000313|Proteomes:UP000253099};
RN [1] {ECO:0000313|EMBL:RBQ22491.1, ECO:0000313|Proteomes:UP000253099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOE {ECO:0000313|EMBL:RBQ22491.1};
RA Lind A.E., Lewis W.H., Spang A., Guy L., Embley M.T., Ettema T.J.G.;
RT "Genomic insight into two independent archaeal endosymbiosis events.";
RL Submitted (JUN-2018) 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|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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBQ22491.1}.
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DR EMBL; NIZT01000064; RBQ22491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366M8C1; -.
DR Proteomes; UP000253099; Unassembled WGS sequence.
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; 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; 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:RBQ22491.1};
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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00054};
KW Reference proteome {ECO:0000313|Proteomes:UP000253099}.
FT DOMAIN 13..254
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 88..92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT MOD_RES 592
FT /note="Diphthamide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 725 AA; 80244 MW; 2C0AA0432B1AE614 CRC64;
MIEKIKDLMY QPKFIRNIGI VAHIDHGKTT LSDNLLAGAG MISEDLAGDA RSLDFDEQES
ARGITIDAAS VSMVHKFSDD DYLINLIDTP GHVDFGGDVT RAMRAVDGAV VVVCAVEGIM
PQTETVFRQA LKENVRPVLF INKVDRLINE LKLEPEELQN RFLKIIAEAN KLIRGMAPED
KKDQWKVDVA DGSVAFGSAY HNWAINIPIM QKSGINFKDI IDHCNDEKQK ELAQKVPITE
VLLGIVVEHL PSPLVSQQYR VPTIWDGDIE SEEGQAMIHT DAEGPLAVMV TNVSIDKHAG
EIATGRVYGG TIEKGSEVFL VGSHAKARAQ QVGVFFGAER VNTDKVPAGN IVAITGAKGA
IAGETICDSD KKIKEFEGIE HISEPVVTVA VEAKNTKNLP KLIEILRQVS KEDPTVRVDI
NEETGQHLIS GMGELHLEII TYRIKEKGVE ITTSEPIVVY RETVAGKIEN PVEGKSPNKH
NRFYITVEPL DQPIYDAIED GNIKEGKVKG KEMASTFIEK GMDKEEARKV WDVYNKSVFL
NMTRGIQYLD EVKELLLEGF ESALDSGPIA NEIVMGMKFK LVDAKLHEDA VHRGPAQVLP
SIRKAIFAAI MMAQPTLLEP LQKVFINTPQ HYMGNATREI QNRRGQIADM GQEGDMASVE
SKVPVAEMFG FAGDIRSATE GRCLWSTENV GFERLPTELQ KQIIREIRER KGLSPEPYGP
EHYIG
//
