ID A0A0V1H6U5_9BILA Unreviewed; 455 AA.
AC A0A0V1H6U5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 18.
DE SubName: Full=Elongation factor 1-gamma {ECO:0000313|EMBL:KRZ06279.1};
GN ORFNames=T11_3279 {ECO:0000313|EMBL:KRZ06279.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ06279.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ06279.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ06279.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ06279.1}.
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DR EMBL; JYDP01000122; KRZ06279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1H6U5; -.
DR STRING; 268475.A0A0V1H6U5; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR Gene3D; 1.20.1050.10; -; 2.
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; IPR004046; GST_C.
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 SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 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:UP000055024}.
FT DOMAIN 80..247
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 296..455
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50040"
SQ SEQUENCE 455 AA; 52493 MW; E99041B5F27B4981 CRC64;
MAIAGTLYGD RDGFRAKKII TAAEFGNKKI KIEPLSKIKH NSPCPPSEIL FVTNEGNYLF
DCNAVACYLA NPFHGSAGGD KFHDSDVLQW IHMADTKILA PLLSWVIPCL SAYPYKSTVN
KLTFFTENIF SFSRNTVAVK LLYDHIRLRY VAEAKEETLQ AMQWLNTQLL LKTFLVGERL
SLADIIMACD VLPAYQHVFD ERIRKRFANV TRWFLTIINQ PFFKKAIGDV PLCEKAAVFD
EQLFKEFLAG SLTVERIVKY DAKHAAIVQS EVKAKPAEAP KKEVVVEEEK VAESDKKDPF
AAFPKGKFDM DAFKRVYSNE DTETKAIPYF WSHFDPDNYS IWFCEYKYPK ELEKVFMSCN
LITGMFQRLD KMRKNAFASV CLFGEDNNST ISGIWIWRGQ ELAFKLSEDW QIDYESYDWS
KLDPKDEKTK SLVNEYLKWE GKFDGKKFNQ GKIFK
//
