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Database: UniProt
Entry: A0A195C5T8_9HYME
LinkDB: A0A195C5T8_9HYME
Original site: A0A195C5T8_9HYME 
ID   A0A195C5T8_9HYME        Unreviewed;       473 AA.
AC   A0A195C5T8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-FEB-2023, entry version 26.
DE   SubName: Full=Elongation factor 1-gamma {ECO:0000313|EMBL:KYM95995.1};
GN   ORFNames=ALC62_13443 {ECO:0000313|EMBL:KYM95995.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM95995.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYM95995.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYM95995.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM95995.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ978251; KYM95995.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195C5T8; -.
DR   STRING; 456900.A0A195C5T8; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; 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; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR   PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW   ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..122
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          123..256
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          314..473
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50040"
FT   REGION          262..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  54694 MW;  1FCD3F00013A6DF2 CRC64;
     MCTYCMNIFV FGTSFLKSTI RRFILIILIS MYCNVMQCYA KCILYTYPEN FRAYKALVAA
     QFSGTQIKIA DDFVFGETNK SEAFLKKFPL GKVPAFETRD GKYITESNAI AYYVANDQLR
     GKTEIERALV IQWLGFADSE ILPASCAWVF PLLGIMPYHK QTVEHAKEDI FKVLTALNSH
     LLTRTYLVGE RLTLADICVA MTLLHLYQYI LEPELRKPYQ NVNRWFQTVI YQPESIAVIG
     AFKLADKTIE YDPKKFAETL GKSSKKEKKE KESKKETKET KESKKESKVV TDKITAVEDE
     ADATEEALAA EPKKKNPFAS MPKSSFDLED FKRFYSNEDE SKSIPYFWQK FDPENYSIWL
     SEYKYNNELT KVFMSCNLIS GMYQRLDSLR KGAFASCCIF GEDNDNTISG IWVWRGQDLV
     FALSPDWQVD FESYSWTKLD ASKEETKTLV EQYFSWVGTD KEGRKFNQGK VFK
//
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