ID   EF1G1_ORYSJ             Reviewed;         418 AA.
AC   Q9ZRI7; Q0E2Q6; Q6YW45;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Elongation factor 1-gamma 1;
DE            Short=EF-1-gamma 1;
DE   AltName: Full=eEF-1B gamma 1;
GN   OrderedLocusNames=Os02g0220600, LOC_Os02g12800; ORFNames=B1131G07.12;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9742959; DOI=10.1016/s0014-5793(98)01014-x;
RA   Kidou S., Tsukamoto S., Kobayashi S., Ejiri S.;
RT   "Isolation and characterization of a rice cDNA encoding the gamma-subunit
RT   of translation elongation factor 1B (eEF1Bgamma).";
RL   FEBS Lett. 434:382-386(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
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; D89802; BAA34206.1; -; mRNA.
DR   EMBL; AP005797; BAD17615.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08232.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77699.1; -; Genomic_DNA.
DR   RefSeq; XP_015625389.1; XM_015769903.1.
DR   AlphaFoldDB; Q9ZRI7; -.
DR   SMR; Q9ZRI7; -.
DR   IntAct; Q9ZRI7; 3.
DR   STRING; 4530.OS02T0220600-02; -.
DR   PaxDb; Q9ZRI7; -.
DR   PRIDE; Q9ZRI7; -.
DR   EnsemblPlants; Os02t0220600-02; Os02t0220600-02; Os02g0220600.
DR   GeneID; 4328753; -.
DR   Gramene; Os02t0220600-02; Os02t0220600-02; Os02g0220600.
DR   KEGG; osa:4328753; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   HOGENOM; CLU_011226_3_0_1; -.
DR   OMA; VQWATEN; -.
DR   OrthoDB; 1341490at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q9ZRI7; baseline and differential.
DR   Genevisible; Q9ZRI7; OS.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   Gene3D; 3.30.70.1010; -; 1.
DR   InterPro; IPR044628; EF-1-gamma_plant.
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   PANTHER; PTHR44372; PTHR44372; 1.
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..418
FT                   /note="Elongation factor 1-gamma 1"
FT                   /id="PRO_0000208828"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          87..213
FT                   /note="GST C-terminal"
FT   DOMAIN          258..418
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          211..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  47479 MW;  1354FDB215BA64EA CRC64;
     MALVLHTFDG NKNAFKALIA AEYSGVKVEL AKNFQMGVSN KTPEYLKMNP IGKVPILETP
     DGPVFESNAI ARYVTRSKSD NPLYGSSLIE YAHIEQWIDF SATEVDANTG KWLFPRLGFA
     PYVAVSEEAA IAALKRSLGA LNTHLASNTY LVGHSVTLAD IVMTCNLYMG FARIMTKNFT
     SEFPHVERYF WTMVNQPNFK KVMGDVKQAD SVPQVQKKAA APKEQKPKEA KKEAPKEAPK
     PKAAEKPEEE EEAPKPKPKN PLDLLPPSKM ILDEWKRLYS NTKTNFREVA IKGFWDMYDP
     EGYSLWFCDY KYNDENTVSF VTMNKVGGFL QRMDLCRKYA FGKMLVIGSE PPFKVKGLWL
     FRGPEIPKFV MDEVYDMELY EWTKVDISDE AQKERVSAMI EDLEPFEGEA LLDAKCFK