ID A0A078H104_BRANA Unreviewed; 412 AA.
AC A0A078H104;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=BnaA08g26240D protein {ECO:0000313|EMBL:CDY31074.1};
GN Name=BnaA08g26240D {ECO:0000313|EMBL:CDY31074.1};
GN ORFNames=GSBRNA2T00047149001 {ECO:0000313|EMBL:CDY31074.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY31074.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY31074.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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 EMBL; LK032267; CDY31074.1; -; Genomic_DNA.
DR RefSeq; XP_013657702.1; XM_013802248.1.
DR AlphaFoldDB; A0A078H104; -.
DR STRING; 3708.A0A078H104; -.
DR PaxDb; 3708-A0A078H104; -.
DR EnsemblPlants; CDY31074; CDY31074; GSBRNA2T00047149001.
DR GeneID; 106362367; -.
DR Gramene; CDY31074; CDY31074; GSBRNA2T00047149001.
DR KEGG; bna:106362367; -.
DR OMA; NNQEYAN; -.
DR OrthoDB; 159792at2759; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
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; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 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:SF8; BNAC08G13770D PROTEIN; 1.
DR PANTHER; PTHR44372; ELONGATION FACTOR 1-GAMMA 1-RELATED; 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 SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
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:UP000028999}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 87..215
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 252..412
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 214..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 46531 MW; 915F4A4EECC37154 CRC64;
MALVMHSYKG NKNSDKAFIA AEFAGVKIDM PSGFEMGVTN KTTEFLKMNP LGKIPVLETP
EGPIFESNAI ARYVSRLNGE NSLNGSSLIE YAHIEQWIDF SSLEIYGNIF NWFVPRMGFM
PYSVPGEEAA ISALKRGLEA LNTHLASNTY LVGHSVTLAD IITVCNLNLG FSTVMTKSFT
SAFPHVERYF WTLINQPNFK KVVGDVKQTE SVPAIKKAGQ PAKPKEQPKK KEAPAAEATK
VVEEEEAPKP KAKNPLDLLP PSPMVLDEWK RLYSNTKSNF REVAIKGFWD MYDPEGYSLW
FCDYKYNDEN MVSFVTLNKV GGFLQRMDLA RKYAFGKMLI CGSEGPFKVK GLWLFRGPEI
PKFVMDEVYD MELYEWTKVD ISDEAQKERV SQMIEDAEPF EGEALLDAKC FK
//
