EF1GB_XENLA
ID EF1GB_XENLA Reviewed; 437 AA.
AC Q91375;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Elongation factor 1-gamma-B;
DE Short=EF-1-gamma-B;
DE AltName: Full=eEF-1B gamma-B;
DE AltName: Full=p47;
GN Name=eef1g-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=8111972; DOI=10.1002/dvg.1020140605;
RA Morales J., Bassez T., Cormier P., Mulner-Lorillon O., Belle R.,
RA Osborne H.B.;
RT "Expression of elongation factor 1 alpha (EF-1 alpha) and 1 beta gamma (EF-
RT 1 beta gamma) are uncoupled in early Xenopus embryos.";
RL Dev. Genet. 14:440-448(1993).
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; S69726; AAB29958.1; -; mRNA.
DR PIR; I51238; I51238.
DR RefSeq; NP_001081481.1; NM_001088012.1.
DR AlphaFoldDB; Q91375; -.
DR SMR; Q91375; -.
DR IntAct; Q91375; 1.
DR PRIDE; Q91375; -.
DR GeneID; 397861; -.
DR KEGG; xla:397861; -.
DR CTD; 397861; -.
DR Xenbase; XB-GENE-6252331; eef1g.S.
DR OrthoDB; 1341490at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 397861; Expressed in pancreas and 19 other tissues.
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 Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..437
FT /note="Elongation factor 1-gamma-B"
FT /id="PRO_0000208821"
FT DOMAIN 2..87
FT /note="GST N-terminal"
FT DOMAIN 89..222
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 225..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 50249 MW; 9DB03AD4FC87E557 CRC64;
MAGGTLYTYP DNWRAYKPLI AAQYSRFPIK VASSPPEFQF GLTNKTPEFL KKFPLGKVPA
FEGNNGFCLF ESSAIAHYVA NDELRGSNNR LHQAQVIQWV GFSDSHVVPP ASAWVFPTLG
IMQFNKQATE QAKEEIKTVL GVLDCHLQTR TFLVGERITL ADITLTCSLL WLYKQVLEPS
FRQPYGNVTR WFVTCVNQPE FRAVLGEVKL CDKMAQFDAK KFAEVQPKKE TPKKEKPAKE
PKKKKKKKKK ATPAPAPAPE DDLDESEKAL AAEPKSKDPY AHLPKSSFIM DEFKRKYSNE
DTLTVALPYF WEHFEKEGWS IWYAEYKFPE ELTQTFMSCN LITGMFQRLD KLRKTAFASV
ILFGTNNNST ISGVWVFRGH DLAFTLSEDW QIDYESYTWR KLESDSEECR TMVKEYFAWE
GEFKHVGKAF NQGKIFK
