ID A0A0V0Y7C1_TRIPS Unreviewed; 859 AA.
AC A0A0V0Y7C1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Elongation factor 2 {ECO:0000313|EMBL:KRX96042.1};
GN Name=eef-2 {ECO:0000313|EMBL:KRX96042.1};
GN ORFNames=T4E_9883 {ECO:0000313|EMBL:KRX96042.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX96042.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX96042.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX96042.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KRX96042.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDU01000048; KRX96042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y7C1; -.
DR STRING; 6337.A0A0V0Y7C1; -.
DR Proteomes; UP000054815; 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 CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR CDD; cd03700; EF2_snRNP_like_II; 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 Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 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; IPR005517; Transl_elong_EFG/EF2_IV.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 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 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:KRX96042.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815}.
FT DOMAIN 17..267
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 859 AA; 96198 MW; 01B08CD5A4EBBFB3 CRC64;
MVHFTVDEIR ALMDRKKNVR NMSVIAHVDH GKSTLTDSLV SKAGIIAAQK AGEMRFTDTR
KDEQERCITI KSTAVSMYFE LSQRDLLYVR GENQIDYDEK GGSKVPFPGF LINLIDSPGH
VDFSSEVTAA LRVTDGALVV VDCVSGVCVQ TETVLRQAIG ERIKPVLFMN KMDRALLELQ
LDQEELYQTF QRIVENTNVI IATYGEETGP MGNIMVDPAV GSVGFGSGLH GWAFTLKQFA
EMYAEKFGIQ AEKLMKNLWG DRYFNPKTKK WTSTSSEGSK RGFNQFVLDP IFKVFDAVMN
MKKEETATLL EKLNVKLPAD ERDLEGKPLL KAIMRRWLPA GETMLQMICI HLPSPVTAQK
YRIELLYEGP QDDEAAVAMK NCDVNGPLMM YISKMVPTSD KGRFYAFGRV FSGKVMTGMK
ARIQGPNYVP GKKEDLYEKA IQRTVLMMGR YVEPIEDVPS GNICGLVGVD QYLVKSGTIT
NFKDAHNMRV MKFSVSPVVR VAVEPQNPAD LPKLVEGLKR LAKSDPMVQC VFEESGEHIV
AGAGELHLEI CLKDLEEDHA CIPLKKSDPV VSYRYFEIFF RETVVDTSNQ MCLSKSPNKH
NRIYMKAQPM PDGLPEDIDK GEVNPRDDVK TRGRLLAERY GYDVNEARKI WCFGPDGSGP
NILVDCTKGV QYLNEIKDSV VAGFQWATKE GVLCEENMRG VRFDIHDVTL HADAIHRGGG
QIIPTARRVL YASALTASPR LLEPVYLVEI QCPETAVGGI YGVLNRRRGH VFEENQVAGT
PMFIVKAYLP VNESFGFTAD LRSNTGGQAF PQCVFDHWQV LPGDPFDTNS RPYHVVAETR
KRKGLKEGIP DLSNYLDKL
//