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Database: UniProt
Entry: A0A0N4SZU3_BRUPA
LinkDB: A0A0N4SZU3_BRUPA
Original site: A0A0N4SZU3_BRUPA 
ID   A0A0N4SZU3_BRUPA        Unreviewed;       529 AA.
AC   A0A0N4SZU3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Tr-type G domain-containing protein {ECO:0000313|WBParaSite:BPAG_0000132901-mRNA-1};
GN   ORFNames=BPAG_LOCUS1330 {ECO:0000313|EMBL:VDN82516.1};
OS   Brugia pahangi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000132901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BPAG_0000132901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN82516.1, ECO:0000313|Proteomes:UP000278627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00003982}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249}.
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DR   EMBL; UZAD01000098; VDN82516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N4SZU3; -.
DR   STRING; 6280.A0A0N4SZU3; -.
DR   WBParaSite; BPAG_0000132901-mRNA-1; BPAG_0000132901-mRNA-1; BPAG_0000132901.
DR   Proteomes; UP000038020; Unplaced.
DR   Proteomes; UP000278627; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   CDD; cd01883; EF1_alpha; 1.
DR   CDD; cd03693; EF1_alpha_II; 1.
DR   CDD; cd03705; EF1_alpha_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_A; EF_Tu_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00483; EF-1_alpha; 1.
DR   PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1.
DR   PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278627}.
FT   DOMAIN          67..304
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          509..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  57780 MW;  436FAE8F44C1B27A CRC64;
     MSTAHSACRV VCARRSRSVV LCGVEHFRPS ESLRCKKISV SSRLFVYWLS TRNVSSEVLA
     HIMGKEKTHI NIVVIGHVDS GKSTTTGHLI YKCGGIDKRT IEKFEKEAQE MGKGSFKYAW
     VLDKLKAERE RGITIDIALW KFETSKYYVT IIDAPGHRDF IKNMITGTSQ ADCAVLVVAC
     GTGEFEAGIS KNGQTREHAL LAQTLGVKQL IVACNKMDST EPAFSEARFN EVTNEVSNYI
     KKIGYNPKAV AFVPISGFNG DNMLEPSPNM PWFKGWNVER KEGNASGKTL LEALDAVIPP
     SRPTDKPLRL PLQDVYKIGG IGTVPVGRVE TGILKPGMVV TFAPQNITTE VKSVEMHHEA
     LQEALPGDNV GFNVKNVSIK EIRRGSVASD SKNDPAKETK QFTAQVIIMN HPGQIAAGYT
     PVLDCHTAHI ACKFAELKEK VDRRSGKKVE DNPKFLKSGD AGIIDLIPTK PLCVETFTEY
     PPLGRFAVRD MRQTVAVGVI KGVEKTEGGA GKVTKAAQKA GTAPAAKKK
//
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