ID A0A0E0JXF1_ORYPU Unreviewed; 864 AA.
AC A0A0E0JXF1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Elongation factor 1-gamma {ECO:0008006|Google:ProtNLM};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC02G08050.4};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC02G08050.4}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC02G08050.4}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000256|ARBA:ARBA00003468}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000256|ARBA:ARBA00011237}.
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DR AlphaFoldDB; A0A0E0JXF1; -.
DR EnsemblPlants; OPUNC02G08050.4; OPUNC02G08050.4; OPUNC02G08050.
DR Gramene; OPUNC02G08050.4; OPUNC02G08050.4; OPUNC02G08050.
DR Proteomes; UP000026962; Chromosome 2.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 2.
DR CDD; cd03044; GST_N_EF1Bgamma; 2.
DR Gene3D; 1.20.1050.10; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 2.
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; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR PANTHER; PTHR44372:SF1; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR Pfam; PF00647; EF1G; 2.
DR Pfam; PF00043; GST_C; 2.
DR Pfam; PF02798; GST_N; 2.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 2.
DR SFLD; SFLDG00358; Main_(cytGST); 2.
DR SMART; SM01183; EF1G; 2.
DR SUPFAM; SSF89942; eEF1-gamma domain; 2.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS50040; EF1G_C; 2.
DR PROSITE; PS50405; GST_CTER; 2.
DR PROSITE; PS50404; GST_NTER; 2.
PE 4: Predicted;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|PROSITE-
KW ProRule:PRU00519};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 24..105
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 110..238
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 281..441
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT DOMAIN 447..528
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 533..661
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 704..864
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 233..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 98010 MW; 501458683A242D98 CRC64;
MSNLICTVRS AAGSLIGRRQ PGEMALVLHT FDGNKNAFKA LIAAEYSGVK VELAKNFQMG
VSNKTPEYLK MNPIGKVPVL ETPDGPVFES NAIARYVTRS KADNPLYGSS LIEYAHIEQW
IDFSATEVDA NIGKWLYPRL GFAPYVAVSE EAAIAALKRS LGALNTHLAS NTYLVGHSVT
LADIVMTCNL YMGFACIMTR IFTSEFPHVE RYFWTMVNQP NFKKVMNDVK QADSVPPVQK
KAAPPKEQKP KEAKKEAPKE APKPKAVEKP EEEEEAPKPK PKNPLDLLPP SKMILDEWKR
LYSNTKTNFR EVAIKGFWDM YDPEGYSLWF CDYKYNDENT VSFVTMNKVG GFLQRMDLCR
KYAFGKMLVI GSEPPFKVKG LWLFRGPEIP KFVMDEVYDM ELYEWTKVDI SDEAQKERVS
AMIEDLEPFE GEALLDAKCF KRQPGEMALV LHTFDGNKNA FKALIAAEYS GVKVELAKNF
QMGVSNKTPE YLKMNPIGKV PVLETPDGPV FESNAIARYV TRSKADNPLY GSSLIEYAHI
EQWIDFSATE VDANIGKWLY PRLGFAPYVA VSEEAAIAAL KRSLGALNTH LASNTYLVGH
SVTLADIVMT CNLYMGFACI MTRIFTSEFP HVERYFWTMV NQPNFKKVMN DVKQADSVPP
VQKKAAPPKE QKPKEAKKEA PKEAPKPKAV EKPEEEEEAP KPKPKNPLDL LPPSKMILDE
WKRLYSNTKT NFREVAIKGF WDMYDPEGYS LWFCDYKYND ENTVSFVTMN KVGGFLQRMD
LCRKYAFGKM LVIGSEPPFK VKGLWLFRGP EIPKFVMDEV YDMELYEWTK VDISDEAQKE
RVSAMIEDLE PFEGEALLDA KCFK
//
