ID A0A200PRE7_9MAGN Unreviewed; 843 AA.
AC A0A200PRE7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Translation elongation factor EFG {ECO:0000313|EMBL:OVA00775.1};
GN ORFNames=BVC80_9083g73 {ECO:0000313|EMBL:OVA00775.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA00775.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA00775.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA00775.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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:OVA00775.1}.
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DR EMBL; MVGT01004287; OVA00775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200PRE7; -.
DR STRING; 56857.A0A200PRE7; -.
DR InParanoid; A0A200PRE7; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000195402; 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; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 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 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:OVA00775.1};
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:UP000195402}.
FT DOMAIN 17..344
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 843 AA; 93879 MW; CD2E420173F1023A CRC64;
MVKFTAEELR RIMDLKHNIR NMSVIAHVDH GKSTLTDSLV AAAGIIAQEV AGDVRMTDTR
ADEAERGITI KSTGISLYYE MTDDALKNYK GERQGNEYLI NLIDSPGHVD FSSEVTAALR
ITDGALVVVD CVEGVCVQTE TVLRQALGER IRPVLTVNKM DRCFLELQVD GEEAYQTFSR
VIENANVIMA TYEDPLLGDV QVYPEKGTVA FSAGLHGWAF TLTNFANMYA SKFGVDESKM
MERLWGENYF DPATKKWTSK NTGSPTCKRG FVQFCYEPIK QIINTCMNDQ KDKLWPMLQK
LGVTMKSEEK DLIGKALMKR VMQTWLPASS ALLEMMIFHL PSPATAQKYR VENLYEGPLD
DMYANAIRNC DPEGPLMLYV SKMIPASDKG RFFAFGRVFA GKVSTGLKVR IMGPNYVPGQ
KKDLYVKSVQ RTVIWMGKKQ ESVEDVPCGN TVALVGLDQF ITKNATLTNE KEVDAHPIRA
MKFSVSPVVR VAVQCKVASD LPKLVEGLKR LAKSDPMVVC TIEESGEHII AGAGELHLEI
CLKDLQDDFM GGAEIIKSDP VVSFRETVLE KSCRTVMSKS PNKHNRLYME ARPLEEGLAE
AIDEGRIGPR DDPKVRSKVL SEEFGWDKDL AKKIWCFGPE TTGPNMVVDM CKGVQYLNEI
KDSVVAGFQW ASKEGALAEE NMRGICFEVC DVVLHADAIH RGGGQVIPTA RRVIYASQIT
AKPRLLEPVY LVEIQAPEQA LGGIYGVLNQ KRGHVFEEMQ RPGTPLYNIK AYLPVIESFG
FSGQLRAATS GQAFPQCVFD HWDMMSADPL EAGSQAAQLV MDIRKRKGLK EQMTPLSEFE
DKL
//
