ID V4LXB5_9CREN Unreviewed; 737 AA.
AC V4LXB5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ORFNames=MGAcid_03610 {ECO:0000313|EMBL:ESQ23591.1};
OS uncultured Acidilobus sp. MG.
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus; environmental samples.
OX NCBI_TaxID=1410573 {ECO:0000313|EMBL:ESQ23591.1, ECO:0000313|Proteomes:UP000017902};
RN [1] {ECO:0000313|EMBL:ESQ23591.1, ECO:0000313|Proteomes:UP000017902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT "Predominant Acidilobus-like populations from geothermal environments of
RT Yellowstone National Park exhibit similar metabolic potential in different
RT hypoxic microbial communities.";
RL Submitted (OCT-2013) 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:ESQ23591.1}.
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DR EMBL; AYMA01000001; ESQ23591.1; -; Genomic_DNA.
DR AlphaFoldDB; V4LXB5; -.
DR STRING; 1410573.MGAcid_03610; -.
DR PATRIC; fig|1410573.3.peg.339; -.
DR Proteomes; UP000017902; 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:ESQ23591.1};
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 19..263
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 603
FT /note="Diphthamide"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00054"
SQ SEQUENCE 737 AA; 82112 MW; 5869033866296772 CRC64;
MGARVKMVSE IEKIMGNIEQ VRNIGVIAHV DHGKTTTSDA LLAGAGIISE RVAGEALVLD
YLKVEKERQI TVKAANASLY HEYNGKGYII NLIDTPGHID FTGMVTRSLR VLDGAIVVVD
AAEGVMTQTE TVLRQALEER VRPVLFINKI DRLVKELRLT PAQIQDRLVE IIKDVNNLID
MYAEPEFKDK WRLNPAAGNV AFGSAKDLWG ITVPLASKKG VNFQHIIEAY SSDDKEKVEA
LRRKVPLHET LLDMVVKFIP NPKEAQKYRI PKIWKGNLDS DLGKAMMEAD PNGPLVFYAN
AIRVEKAGLV ATGRVFSGTL EPGREVYILS QNLTSRILQV SLYMGPFREL TNRVTAGNIA
AIMGIENLRA GETLVDVAYK SQAAPFEQLH YIAEPVVTVA IEPTKVQDLP KLVDALRKLT
IEDPNLVTKI NEETGEYLLS GMGQLHLEIA LWMLKEFYGL EVKASPPIIV YRESAREQSK
TFEGKSPNKH NRFYISVEPL NEETIELIHK GVVREDQDPR DRAKILRDQA GWDYDEARRI
WAIDENINVF VDMTSGVQYL KDVKDTIIGG FRVAVKEGPL AAEPVRGLKV VLHDAIVHED
PVHRGPGQLY PAIRNAIWAG ILTSRPTLLE PVQKLDIRVP MEFLSAVTTI IVKKRGKIIN
VESTGMGTRV MAEIPIAESF DLATELRGST AGKAIWGTEF SRWAPVPDSM LEDLIKKIRE
RKGLPPRPPS VDDLLGP
//
