ID A0A2K6RST1_RHIRO Unreviewed; 420 AA.
AC A0A2K6RST1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Elongation factor 1-gamma {ECO:0000256|ARBA:ARBA00022218};
DE AltName: Full=eEF-1B gamma {ECO:0000256|ARBA:ARBA00030426};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000044075.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000044075.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6RST1; -.
DR STRING; 61622.ENSRROP00000044075; -.
DR Ensembl; ENSRROT00000068589.1; ENSRROP00000044075.1; ENSRROG00000045033.1.
DR GeneTree; ENSGT00390000007552; -.
DR OMA; GYESYTW; -.
DR Proteomes; UP000233200; Unplaced.
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};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00519}; Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT DOMAIN 2..84
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 84..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 263..420
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
FT REGION 217..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 48139 MW; 7F1F49FCA5CD9354 CRC64;
VAAGTLYTYP ENWRAFKALI AAQYSGAQVW VLSTPPHFHF GQTNCTPEFL RKFPASKVPD
EDGFCVFESN AIAYYVSNEL WGSTPEAAAK VVQWVSFADS DIVPPASTWV FPTLSIMHHN
KQATENAKEE VRQILGLLDA HLKTRTFLVG KRVTLADITV VCTLLCLYKQ VLEPSFCQAF
PNTNRWFLTC INQPQFRAVL GEVKLCEKMA QFDAKKFAET QEGSQEEKQK PQAEGKEEKK
AAAPAPEEEV DECEQALAAE PKAKNPFTHL PKSTFVLDEF KRKYSDEDTL SVALPYFWEH
FDKDSWSLWY SEYRFPEELT QTFMSCNLIT GMFQRLDKLR KNAFTSVILF GTNNSGSISG
VWVFQGQELA FRLSPDWQVD YESYTRRKLD PTQMLVQEYF SWERAFQHVG KVFNQGEIFK
//
