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Database: UniProt
Entry: A0A1U8AWK2_NELNU
LinkDB: A0A1U8AWK2_NELNU
Original site: A0A1U8AWK2_NELNU 
ID   A0A1U8AWK2_NELNU        Unreviewed;       487 AA.
AC   A0A1U8AWK2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Elongation factor 1-gamma-like isoform X1 {ECO:0000313|RefSeq:XP_010272550.1};
GN   Name=LOC104608303 {ECO:0000313|RefSeq:XP_010272550.1};
GN   ORFNames=HUJ06_025789 {ECO:0000313|EMBL:DAD24325.1};
OS   Nelumbo nucifera (Sacred lotus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX   NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010272550.1};
RN   [1] {ECO:0000313|EMBL:DAD24325.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:DAD24325.1};
RX   PubMed=32343808;
RA   Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA   Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT   "Distinct Expression and Methylation Patterns for Genes with Different
RT   Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL   Mol. Biol. Evol. 37:2394-2413(2020).
RN   [2] {ECO:0000313|RefSeq:XP_010272550.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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   EMBL; DUZY01000001; DAD24325.1; -; Genomic_DNA.
DR   RefSeq; XP_010272550.1; XM_010274248.2.
DR   STRING; 4432.A0A1U8AWK2; -.
DR   GeneID; 104608303; -.
DR   KEGG; nnu:104608303; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   OrthoDB; 159792at2759; -.
DR   Proteomes; UP000189703; Unplaced.
DR   Proteomes; UP000607653; 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; ELONGATION FACTOR 1-GAMMA 1-RELATED; 1.
DR   PANTHER; PTHR44372:SF1; 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:UP000189703}.
FT   DOMAIN          65..146
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          151..279
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          327..487
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50040"
FT   REGION          276..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  54954 MW;  4C917BA2959D579E CRC64;
     MTGRQPSFPL LKQTLIFPGA PETLEGLTLQ LLSNKKPLSH QSANLGPGLP QCSADIEEIV
     LLQAMTLVLH AGNTNKNAFK ALIAAEYNGV TVKLVPNFEM GVSNKTPQFL KMNPIGKVPV
     LETPDGPIFE SNAIARYVAR LKGDTPLYGS SLIEFARIEQ WIDFASLEID ANILKWFIPR
     AGFAVYLPPA EEAAISALKR ALDALNKHLA SNTFLVGHSV TLADIVMTCN LSLGFSRVMT
     KSFTSEFPHV ERYFWTMVNQ PNFKKILGEV KQVESVPPVQ SAKKPSQSKE PAKHKAKDEP
     KKETKKEPAK PKVEEPAEEE EAPKPKLKNP LDLLPPSKMI LDEWKRLYSN TKSNFREVAI
     KGFWDMFDPD GYSLWFCDYK YNDENTVSFV TLNKVSGFLQ RMDLARKYAF GKILVIGSEP
     PYKVKGLWLF RGQEIPQFVL DECYDMELYD WRKVDINDEA QKERVNQMIE DAEPFEGEAL
     LDAKCFK
//
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