ID J4GUS3_9APHY Unreviewed; 743 AA.
AC J4GUS3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Elongation factor Tu {ECO:0000256|RuleBase:RU004061};
GN ORFNames=FIBRA_07354 {ECO:0000313|EMBL:CCM05145.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM05145.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM05145.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM05145.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the GcvH family.
CC {ECO:0000256|ARBA:ARBA00009249}.
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; HE797181; CCM05145.1; -; Genomic_DNA.
DR RefSeq; XP_012184428.1; XM_012329038.1.
DR AlphaFoldDB; J4GUS3; -.
DR STRING; 599839.J4GUS3; -.
DR GeneID; 24100056; -.
DR HOGENOM; CLU_373858_0_0_1; -.
DR InParanoid; J4GUS3; -.
DR OrthoDB; 167272at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; 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 GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR CDD; cd03707; EFTU_III; 1.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 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_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR005225; Small_GTP-bd_dom.
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; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR NCBIfam; TIGR00485; EF-Tu; 1.
DR NCBIfam; TIGR00527; gcvH; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF01597; GCV_H; 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; SSF51230; Single hybrid motif; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|PIRSR:PIRSR617453-50};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 70..268
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT DOMAIN 639..721
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT MOD_RES 680
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR617453-50"
SQ SEQUENCE 743 AA; 80990 MW; 8B8D80B7A6C40B78 CRC64;
MFRTPLAASR TISRRLCVSR AAQSYHTGAR NVVRNPARSV HSTFIKSNGA SWVIRRGYAD
AAGSKFSRAK PHLNIGTIGH VDHGKTTLTA AITKVLAERG GAKFTDYADI DKAPEEKARG
ITINSSHVEY ESETRHYGHI DCPGHADYIK NMITGAAQMD GAIIVVSATD GQMPQTREHL
LLARQVGVKK LVVFINKVDQ IQDQEMLELV DMEMRDLLST YNFDGEETPI IMGSALAALE
GRNPDIGADK IVELVRACDL EKPFLLPVED VFSISGRGTV ATGRVERGVC HKGDEVEVVG
LGDSFKTTLT GIEMFHKELD RGEAGDNMGV LLRGVKREQI RRGQVIIAPG SIKAVRKFQA
QIYVLTKDEG GRYTPFMDNY RPQLFLRTAD VTCGLHWPEG TSDAAEKMVM PGDNVEMICD
LMHDVAAEIG TRFTLREGGK TGLFLRYVDS RRLTSSFLEE YISHISATSV SMHDPHSTPK
VESGLTRLST CRTVPYIASL STLALTERNG FTDASELLRI LSVLERMAEK YVRIYGIGCT
VSGQPSGSRL TASPQGPERA GFSGHDLCAF LDRPGWLQPP ATMFSAIRLA SRSSSSAAAV
RTARRPAAGA FRTPFMRTLV TKRYTEDHEA VVFDDSTMTG TVYITNYAQS SLGDVVFVEL
PVEGSTVAQG DQIGAVESVK AASDIYAPIS GTVAEVNSGL ADQPGLLNKS PEDQGWLCKI
KVNDAAEIEK LLTEDAYKAH CDS
//
