ID A0A0R0LW63_9MICR Unreviewed; 464 AA.
AC A0A0R0LW63;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptide elongation factor 1 alpha {ECO:0000313|EMBL:KRH93612.1};
GN ORFNames=M153_7190003529 {ECO:0000313|EMBL:KRH93612.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH93612.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH93612.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH93612.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRH93612.1}.
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DR EMBL; LGUB01000278; KRH93612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0LW63; -.
DR VEuPathDB; MicrosporidiaDB:M153_7190003529; -.
DR Proteomes; UP000051530; 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:UniProtKB-KW.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd01513; Translation_factor_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 InterPro; IPR004161; EFTu-like_2.
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; IPR004160; Transl_elong_EFTu/EF1A_C.
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; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:KRH93612.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000313|EMBL:KRH93612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051530}.
FT DOMAIN 5..239
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 464 AA; 50454 MW; 4648A3311713E7F2 CRC64;
MSAEKPILNV CFIGHVDSGK STTVGNLAYQ LGAIDARSME KLKKEAEERG RGTFSFAYVM
DLSKAERDRG ITITTSLMKL ETSKHLLNVI DCPGHQDFIK NMVTGAAQAD VGVVLVPCAT
GEFESCISGG TLKDHIMISG VLGCRKLIVC VNKVDTIEES KKLSRFDEVA KEMRAIISKS
HPDKDPIIIP ISGYLGINII EKGEKFDWFK GWLPEKNAEG AEKIFTLEGA LNSQIPPPRP
IDQPLRMPID SVHKISGIGM VYTGRVSVGT IKPGMTISCQ PAGVVAECKT LEIHKETRDK
VVAGENCGLA LKNPTKGSAN LIKPGHVFSD AKNSPCQLYK GSRAKIVIVE HPKGIKVGYC
PVMDIATNHV PCQITKLYSK RIPGIKEEIT APDLVQKGEN VTCMIHPQKD VVMETLKECA
SLARFALRDG GHIVGIGAIE QCFTPEDYDK EVPPVKAKPT RARG
//
