GenomeNet

Database: UniProt
Entry: B0X828_CULQU
LinkDB: B0X828_CULQU
Original site: B0X828_CULQU 
ID   B0X828_CULQU            Unreviewed;       430 AA.
AC   B0X828;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   SubName: Full=Elongation factor 1-gamma {ECO:0000313|EMBL:EDS42297.1, ECO:0000313|EnsemblMetazoa:CPIJ014663-PA};
GN   Name=6048964 {ECO:0000313|EnsemblMetazoa:CPIJ014663-PA};
GN   ORFNames=CpipJ_CPIJ014663 {ECO:0000313|EMBL:EDS42297.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS42297.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS42297.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ014663-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ014663-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) 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   EMBL; DS232472; EDS42297.1; -; Genomic_DNA.
DR   RefSeq; XP_001865800.1; XM_001865765.1.
DR   AlphaFoldDB; B0X828; -.
DR   STRING; 7176.B0X828; -.
DR   EnsemblMetazoa; CPIJ014663-RA; CPIJ014663-PA; CPIJ014663.
DR   GeneID; 6048964; -.
DR   KEGG; cqu:CpipJ_CPIJ014663; -.
DR   VEuPathDB; VectorBase:CPIJ014663; -.
DR   VEuPathDB; VectorBase:CQUJHB013053; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   HOGENOM; CLU_011226_3_1_1; -.
DR   InParanoid; B0X828; -.
DR   OMA; TQYFSWT; -.
DR   OrthoDB; 159792at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
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:UP000002320}.
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          84..216
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   DOMAIN          271..430
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50040"
FT   REGION          221..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  48933 MW;  D23B808746676456 CRC64;
     MAGTLYTYPE NFRAYKALIA AQFSGAKVTV ASDFVFGQTN KSEAFLKKFP LGKVPAFETA
     DGKFLTESNA IAYYVSNEQL RGKTDLEKAE VLSFLSLADN ELLPAVHGWV FAFMGIIQFQ
     KNNVERAKQD LKATLTALNS RLVNQTFLVG ERLTLADIVV FATLLSAYEK VLDPSFRAPF
     GSLTRWFNTV LNQPQVKAVV KGFTMCAKVA EIDPKKFAEF QAKTGGAQQQ QQKEPKEKKE
     KKPAPAKKEK EAEPAEELDA AELALAEEPK SKDPFDAMPK GTFNFDDFKR CYSNEDEAKS
     IPYFFEKFDP EHYSIWYGEY KYPEELTKVF MSCNLITGMF QRLDKMRKQA FSSVCLFGED
     NNSTISGVWV WRGQDLAFEL SPDWQVDYEV YDWKKLDPKS EETKKLVTQY FSWSGTDSKG
     RKFNQGKIFK
//
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