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Database: UniProt
Entry: A0A1S3BU72_CUCME
LinkDB: A0A1S3BU72_CUCME
Original site: A0A1S3BU72_CUCME 
ID   A0A1S3BU72_CUCME        Unreviewed;       409 AA.
AC   A0A1S3BU72;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Elongation factor 1-gamma-like {ECO:0000313|RefSeq:XP_008452240.1};
GN   Name=LOC103493313 {ECO:0000313|RefSeq:XP_008452240.1};
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008452240.1};
RN   [1] {ECO:0000313|Proteomes:UP000089565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX   PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA   Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA   Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA   Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA   Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA   Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA   Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA   Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT   "The genome of melon (Cucumis melo L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN   [2] {ECO:0000313|RefSeq:XP_008452240.1}
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   RefSeq; XP_008452240.1; XM_008454018.2.
DR   AlphaFoldDB; A0A1S3BU72; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   InParanoid; A0A1S3BU72; -.
DR   OrthoDB; 159792at2759; -.
DR   Proteomes; UP000089565; Unplaced.
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:UP000089565}.
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          86..214
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          249..409
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50040"
FT   REGION          214..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  46159 MW;  35D5A8CE413E5F98 CRC64;
     MALVLHSWTP SKNVYKVLIA AEYNGVKVDL APDFTMGVSN KSPEFLKMNP IGKVPLLQTP
     DGAIFESNAI TRYVARLKDS GLYGSSPIDY GHIEQWIDFS SLEIDSHIST ILAPRYGYGV
     YYAPAEEAAN AALKRSLGAL NSYLASNTFL VGHSVTLADI VLTCNLYYGF TYILPKSFTS
     AFPHVERYFW TLVNQPNFKK IIGEVKQTDA VPPVKTPEEA AAAAKAKAEP KKQEEKPAAP
     AEEAPKPKAK NPLDLLPPSS MILDDWKRLY SNTKTNFREV AIKGFWDMYD PEGYSLWFCD
     YKYNDENTVS FVTLNKVGGF LQRMDIARKY AFGKMLVIGS EAPYKVKGLW LFRGKEIPQF
     VLDECYDMEL YEWKKVDVSD EAQKERVNQM IEDQEPFEGE ALLDAKCFK
//
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