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
//