EF2_BOMMO
ID EF2_BOMMO Reviewed; 844 AA.
AC Q1HPK6; P82216; Q19P05;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translation elongation factor 2;
DE Short=EF-2;
GN Name=tef2 {ECO:0000312|EMBL:ABF71565.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1] {ECO:0000312|EMBL:ABF51485.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=306 {ECO:0000312|EMBL:ABF71565.1};
RC TISSUE=Midgut {ECO:0000312|EMBL:ABF71565.1};
RA Gao L., Chen K.P., Yao Q., Chen H.Q.;
RT "Cloning of Bombyx mori translation elongation factor 2 gene.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:ABF51485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA Lin T.B., Chen J.E.;
RT "Blast silkworm EST database for functional genes.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 558-571.
RC STRAIN=Xinhang X Keming {ECO:0000269|PubMed:11280994};
RC TISSUE=Body wall {ECO:0000269|PubMed:11280994}, and
RC Fat body {ECO:0000269|PubMed:11280994};
RX PubMed=11280994;
RA Zhong B.-X.;
RT "Protein database for several tissues derived from five instar of
RT silkworm.";
RL Yi Chuan Xue Bao 28:217-224(2001).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC {ECO:0000250|UniProtKB:P13639}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF71565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ515926; ABF71565.1; ALT_INIT; mRNA.
DR EMBL; DQ443396; ABF51485.1; -; mRNA.
DR RefSeq; NP_001037593.1; NM_001044128.2.
DR RefSeq; NP_001163865.1; NM_001170394.1.
DR AlphaFoldDB; Q1HPK6; -.
DR SMR; Q1HPK6; -.
DR IntAct; Q1HPK6; 1.
DR MINT; Q1HPK6; -.
DR STRING; 7091.BGIBMGA004165-TA; -.
DR PRIDE; Q1HPK6; -.
DR GeneID; 733027; -.
DR KEGG; bmor:733027; -.
DR CTD; 733027; -.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q1HPK6; -.
DR OrthoDB; 140796at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_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; IPR005517; Transl_elong_EFG/EF2_IV.
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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CHAIN 2..844
FT /note="Translation elongation factor 2"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT /id="PRO_0000274546"
FT DOMAIN 17..348
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT BINDING 108..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT BINDING 162..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 701
FT /note="Diphthamide"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CONFLICT 216
FT /note="G -> V (in Ref. 1; ABF71565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 844 AA; 94784 MW; 8BA138DE257A33BC CRC64;
MVNFTVDEIR GMMDKKRNIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGAR AGETRFTDTR
KDEQDRCITI KSTAISMFFE LEEKDLVFIT NPDQREKSEK GFLINLIDSP GHVDFSSEVT
AALRVTDGAL VVVDCVSGVC VQTETVLRQA IAERIKPILF MNKMDRALLE LQLEAEELYQ
TFQRIVENVN VIIATYNDDG GPMGEVRVDP SKGSVGFGSG LHGWAFTLKQ FSEMYADKFK
IDLVKLMNRL WGENFFNPQT KKWSKQKDDD NKRSFCMYVL DPIYKVFDAI MKFKKEEIDD
LLKKIGVTIK HEDSDKDGKA LLKVVMRSWL PAGEALLQMI AIHLPSPVVA QKYRMEMLYE
GPHDDEAAIG IKSCDPEAPL MMYVSKMVPT SDKGRFYAFG RVFSGKVVTG QKARIMGPNF
TPGKKEDLYE KTIQRTILMM GRYVEAIEDV PSGNICGLVG VDQFLVKTGT ITTFKNAHNM
KVMKFSVSPV VRVAVEPKNP ADLPKLVEGL KRLAKSDPMV QCINEESGEH IVAGAGELHL
EICLKDLEED HACIPIKKSD PVVSYRETVA EESDQLCLSK SPNKHNRLFM KAQPMPDGLP
EDIDEGRVNP RDDFKTRARY LTEKYEYDVT EARKIWCFGP EGTGPNILVD CSKGVQYLNE
IKDSVVAGFQ WAAKEGVMAE ENLRGVRFNI YDVTLHTDAI HRGGGQIIPT TRRCLYACLL
TAQPRLMEPV YLCEIQCPEV AVGGIYGVLN RRRGHVFEES QVAGTPMFIV KAYLPVNESF
GFTADLRSNT GGQAFPQCVF DHWQVLPGDP CEPQSKPYNV VQETRKRKGL KEGLPDLTQY
LDKL
