EFGM_ASPFU
ID EFGM_ASPFU Reviewed; 802 AA.
AC Q4WP57;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN Name=mef1; ORFNames=AFUA_4G08110;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAHF01000005; EAL89977.2; -; Genomic_DNA.
DR RefSeq; XP_752015.2; XM_746922.2.
DR AlphaFoldDB; Q4WP57; -.
DR SMR; Q4WP57; -.
DR STRING; 746128.CADAFUBP00006346; -.
DR EnsemblFungi; EAL89977; EAL89977; AFUA_4G08110.
DR GeneID; 3508949; -.
DR KEGG; afm:AFUA_4G08110; -.
DR VEuPathDB; FungiDB:Afu4g08110; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q4WP57; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 25..802
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385559"
FT DOMAIN 100..387
FT /note="tr-type G"
FT BINDING 109..116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 185..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 239..242
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 802 AA; 89220 MW; 399DEC9670379895 CRC64;
MRCPSLARLP NRALSGLTRS PVRLQSQNFL YQRCASTAAL RSPIAGPAYQ SVFHRHNLQR
RNASAATTAA VLEAAASNPD GLSQEAIIDN LDPAEAIRLS RLRNIGIAAH IDSGKTTCTE
RVLFYTGRIK AIHEVRGRDN VGAKMDSMDL EREKGITIQS AATFCDWIKK GDDGKEEKYH
INLIDTPGHI DFTIEVERAL RVLDGAVMIL CAVSGVQSQT ITVDRQMRRY NVPRISFVNK
MDRMGANPFK AVEQINTKLK IPAAAVQVPI GAEDEFEGVV DLIRMKSIYN DGPNGETVVV
KDEIPEKVKS VVEERRRMLI ETLADVDDEI AELFLEETEP TEQQLKAAIR RATIGLKFTP
VFMGSALANK SVQPMLDGVI DYLPNPSEVE NLALDRKRDE ASVKLVPYNS QPFVGLAFKL
EESNFGQLTY IRVYQGTLRK GANVFNARNN KKVKVPRIVR MHSNEMEEVS EIGAGEICAV
FGVDCASGDT FTDGQLGYTM TSMFVPEPVI SLSIKPKNSK DSANFSKAMA RFQREDPTFR
VSYNAESEET LISGMGELHL DIYIERMRRE YRVDCVTGPP QVAYRETIGN RVEFDHLLKK
QSGGPGEYAR VVGWMEPTGK LEDNKFEEQI VGGSISEKFL FACEKGFNLA CEKGPLIGHK
VLGTKMVIND GATHMTDSSE MSFKNATQQA FRKAFMESNP SVLEPMMKIA VTAPGEFQGD
VISLLNKRNA TINDTETGVD EFTVYADCSL NGMFGFSTHL RAATQGKGEF TMEFSHYEKA
QPQLQKELIQ KYLKAQADRH KK
