ID A0A101X529_9CREN Unreviewed; 740 AA.
AC A0A101X529;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 34.
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:KUO84924.1};
GN ORFNames=AT709_02145 {ECO:0000313|EMBL:KUO84924.1};
OS Caldivirga sp. MG_3.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=1714256 {ECO:0000313|EMBL:KUO84924.1, ECO:0000313|Proteomes:UP000054806};
RN [1] {ECO:0000313|EMBL:KUO84924.1, ECO:0000313|Proteomes:UP000054806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (DEC-2015) 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}.
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:KUO84924.1}.
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DR EMBL; LOCB01000062; KUO84924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101X529; -.
DR Proteomes; UP000054806; 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:KUO84924.1};
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}.
FT DOMAIN 21..262
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 96..100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
FT MOD_RES 603
FT /note="Diphthamide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 740 AA; 82685 MW; CE89884FC4FAC5D2 CRC64;
MSVRIVEKKI EDILDIMRNP SQIRNVGTLA HVDHGKTTTT DSLLMGAGLL SPKVAGKALA
MDYVEIEQLR QLTIKAANIS LYFEYGGKPY LINFVDTPGH VDFTGHVTRS LRVMDGALVV
VDAVEGVMTQ TETVVRQAME ELVRPVLFIN KIDRLIKELR LSPQEIGNRI LYITKEFNSL
IDTYAPPEFK EKWKVSVNKG QVAFGSALGK WGLTIPMMQE KGIKFSYIMD AYERNAVDEL
AQEFPLYKTL LTMIIEHIPP PNVTQKYRVP KLWKGDLNSP IGKALLDADP NGPLVIAVSK
VNKDPHAGLI ATGRVFSGTI REGDEVYIIG QKLTKRVLQT YLYMGPSRII VPEVMAGNIV
ALMGVDEARA GDTLVAPSIK DIPPFEKMRY VSEPVVTVAI EPKNPNDLAK LVEGLRDLVI
EDPTLSLKID EETGQVLLSG VGTLHLEIAT WLLKDRTGLD FVVSQPLVRF RETVRARSQV
FEGKSPNKHN RLYISVEPLD EESISLIQYS EITEDMDPRE RARILREKAN WDTDEARGIW
AIDNQYINVL IDKTSGIQHL REIRDYIIQG FRWSVSAGPL AQEPVRGVKV ILHDAVVHED
PAHRGPAQIM PATKNAIFAS ILSANPTLLE PLLLIDAKTT VDNMGPVTSV ITRHRGRVID
VTQTETMEVV IKGEIPVIEA FNISDELRSA TTGKVFWSLQ FSRWAPVPES LRESLILSIR
EKKGLPKELP KVEDFISPFA
//
