EF1G2_ORYSJ
ID EF1G2_ORYSJ Reviewed; 418 AA.
AC Q6YW46; Q84PA8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Elongation factor 1-gamma 2;
DE Short=EF-1-gamma 2;
DE AltName: Full=eEF-1B gamma 2;
GN OrderedLocusNames=Os02g0220500, LOC_Os02g12800; ORFNames=B1131G07.11;
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 [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 [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-418 (ISOFORM 1).
RC STRAIN=cv. Nipponbare;
RX PubMed=12684538; DOI=10.1073/pnas.0737574100;
RA Cooper B., Clarke J.D., Budworth P., Kreps J., Hutchison D., Park S.,
RA Guimil S., Dunn M., Luginbuehl P., Ellero C., Goff S.A., Glazebrook J.;
RT "A network of rice genes associated with stress response and seed
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4945-4950(2003).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6YW46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6YW46-2; Sequence=VSP_017654;
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DR EMBL; AP005797; BAD17614.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS77698.1; -; Genomic_DNA.
DR EMBL; AK103901; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY224455; AAO72574.1; -; mRNA.
DR RefSeq; XP_015625858.1; XM_015770372.1. [Q6YW46-2]
DR AlphaFoldDB; Q6YW46; -.
DR SMR; Q6YW46; -.
DR IntAct; Q6YW46; 3.
DR STRING; 4530.OS02T0220500-01; -.
DR PRIDE; Q6YW46; -.
DR EnsemblPlants; Os02t0220500-01; Os02t0220500-01; Os02g0220500. [Q6YW46-2]
DR GeneID; 4328752; -.
DR Gramene; Os02t0220500-01; Os02t0220500-01; Os02g0220500. [Q6YW46-2]
DR KEGG; osa:4328752; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR InParanoid; Q6YW46; -.
DR OMA; QEIPKFI; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6YW46; 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 Alternative splicing; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..418
FT /note="Elongation factor 1-gamma 2"
FT /id="PRO_0000228123"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT DOMAIN 87..215
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 210..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"
FT VAR_SEQ 237..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_017654"
SQ SEQUENCE 418 AA; 47356 MW; 73C7123AB0605E56 CRC64;
MALVLHAGSG NKNAFKALIA AEYSGVKVEL VKNFQMGVSN KTPEFLKMNP IGKIPVLETP
DGPVFESNAI ARYVTRSKAD NPLYGSSLIE YAHIEQWNDF SATEVDANIG KWLYPRLGIA
PYVAVSEEAA IAALKRSLGA LNTHLASNTY LVGHSVTLAD IVMTCNLYMG FARIMTKSFT
SEFPHVERYF WTMVNQPNFK KVLGDVKQAE SVPPVQKKAP PPKEQKPKEA KKEAPKEAPK
PKAVEKPEEE EEAPKPKPKN PLDLLPPSKM ILDEWKRLYS NTKTNFREVA IKGFWDMYDP
EGYSLWFCDY KYNDENTVSF VTMNKVGGFL QRMDLCRKYA FGKMLVIGSE PPFKVKGLWL
FRGPEIPKFV MDEVYDMELY EWTKVDISDE AQKERVSAMI EDLEPFEGES LLDAKCFK