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EF1G_RABIT
ID   EF1G_RABIT              Reviewed;         437 AA.
AC   P29694;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
GN   Name=EEF1G;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Spleen;
RX   PubMed=1454551; DOI=10.1093/nar/20.21.5849;
RA   Sheu G.-T., Traugh J.A.;
RT   "Nucleotide sequence of a rabbit cDNA encoding elongation factor 1 gamma.";
RL   Nucleic Acids Res. 20:5849-5849(1992).
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components.
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC       gamma.
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DR   EMBL; X68142; CAA48242.1; -; mRNA.
DR   PIR; S26649; S26649.
DR   RefSeq; NP_001095173.1; NM_001101703.1.
DR   RefSeq; XP_008272599.1; XM_008274377.2.
DR   AlphaFoldDB; P29694; -.
DR   SMR; P29694; -.
DR   STRING; 9986.ENSOCUP00000021097; -.
DR   GeneID; 100009282; -.
DR   GeneID; 103344933; -.
DR   KEGG; ocu:100009282; -.
DR   KEGG; ocu:103344933; -.
DR   CTD; 1937; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   InParanoid; P29694; -.
DR   OrthoDB; 1341490at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.70.1010; -; 1.
DR   InterPro; IPR001662; EF1B_G_C.
DR   InterPro; IPR036433; EF1B_G_C_sf.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00647; EF1G; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SMART; SM01183; EF1G; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF89942; SSF89942; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Elongation factor; Isopeptide bond; Protein biosynthesis;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CHAIN           2..437
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208816"
FT   DOMAIN          2..87
FT                   /note="GST N-terminal"
FT   DOMAIN          88..216
FT                   /note="GST C-terminal"
FT   DOMAIN          276..437
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          221..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         147
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         401
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         434
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         434
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        253
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
SQ   SEQUENCE   437 AA;  50049 MW;  DDC2864547C1FBFE CRC64;
     MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
     FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
     MHHNKQATEN AKEEVKRILG LLDAHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
     RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
     KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
     DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
     ILFGTNNSSS ISGIWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPSSEETQ TLVREYFAWE
     GAFQHVGKAF NQGKVFK
 
 
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