ID A0A267E8Y9_9PLAT Unreviewed; 1121 AA.
AC A0A267E8Y9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Elongation factor 2 {ECO:0000256|ARBA:ARBA00017891};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig030490g1 {ECO:0000313|EMBL:PAA57162.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA57162.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA57162.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA57162.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA57162.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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.
CC {ECO:0000256|ARBA:ARBA00024731}.
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:PAA57162.1}.
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DR EMBL; NIVC01002523; PAA57162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267E8Y9; -.
DR STRING; 282301.A0A267E8Y9; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 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; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
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:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 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 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000215902}.
FT DOMAIN 29..291
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 206..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA57162.1"
SQ SEQUENCE 1121 AA; 121841 MW; 5032BEB9C1AF630B CRC64;
NSALILTVKS IRASQRQMEP PTATKSKAER TRNVCILAHV DHGKTTLADC LIATNGIIPS
RSVARLRYMD SLEQEQERGI TMKSSIISLL YNRKECSEQY VVNLIDSPGH IDFSSEVSAA
VRLSDGAIVV VDAVEGVSPQ TVAVLRQAWR ESVTPVLLIN KVDRLILELR LSPTDAYHHL
WKLIESVNAL MAELYRMEFF ERQEQQEQQQ QQQQQQEKPK ESQPVEKTTD SVAEVTLSSD
WLSGLESAED EHVYFAPARG NVVFASALDG WGFRLDDFAG LLAKRLGCSE RILSRALWGD
YFYAAKEKKV YRGASVKGRK PLFVQLVLEN LWTVYDTFVT NRDADKISKM CASLDIRLGP
RDLKSGADPH SALAAFSAQW LPVARAVLEA VVARCPSPRQ LSTDKVNRLL TIGGVEGSPE
SAGLSCLRQH FLACSPDGPL VAFASKMMAV PAGCIVEPAP AGLTSAPPPE ASATSAAELE
QRRLEARRQW EAMRATKAAA VDANGESAAE ASASNTDNDS SPSVYVAFCR IYSGIVRPGD
RLFLLSPRHR PDRLPPGLAE LTPDALDAEK RLSDSGLRHA SVCTIGRVLL MRGRDFESVP
GAGAGAIVGV EGLADRVIKT ATLSATLDCP AFSDMASEAA PIIRVAVECV NPADQSRLLA
GLRLLERHDP GAEVLLEDTG ENVVCSSGEV HLAKCLSDLR QCYAKVEFTT SPIVVPFRET
LATDEALAEA AAAAADDPDA DTDDADEAPP EELLSQLDIG ESGGKDDPEV LDACRGLVCC
RMQARDADRH LALTVRAVPL SAGAIRLLEN HADALRRRPT AAGAADTALL ALRDGLRSEL
LALDSAATSD AAAASVELGR LADCSVLAAG PRRDPCNLLL LGPSARLPDG TLAAPLLPTN
TTNSTPASAV SSHLWQAIIN GFQWTCQQGP LCREPLRGVA FVLLDVCEVS TAGDERYPEL
TVSAGQLMSH ASKTFGKAFL CHANRRLMLA AFTVDVQCRS EVLGKVHAVL AKHQGRIVSE
DLREGTNMFV LRGHMPVIES FGLADELRKR TSGFAGAQLR FSHWALCDWD PLMLPREDDD
LRDERMRIVN YLMEVRRRKG MPVRQQIVQH ADKQRTRSRK K
//
