EFGM_SCHPO
ID EFGM_SCHPO Reviewed; 770 AA.
AC Q9USZ1; Q9UUA3;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=SPBC1306.01c, SPBC409.22c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 ECO:0000269|PubMed:16823372}.
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}.
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DR EMBL; CU329671; CAB52624.1; -; Genomic_DNA.
DR PIR; T50308; T50308.
DR RefSeq; NP_595472.2; NM_001021382.3.
DR AlphaFoldDB; Q9USZ1; -.
DR SMR; Q9USZ1; -.
DR BioGRID; 276327; 11.
DR STRING; 4896.SPBC1306.01c.1; -.
DR MaxQB; Q9USZ1; -.
DR PaxDb; Q9USZ1; -.
DR EnsemblFungi; SPBC1306.01c.1; SPBC1306.01c.1:pep; SPBC1306.01c.
DR GeneID; 2539776; -.
DR KEGG; spo:SPBC1306.01c; -.
DR PomBase; SPBC1306.01c; mef1.
DR VEuPathDB; FungiDB:SPBC1306.01c; -.
DR eggNOG; KOG0462; Eukaryota.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q9USZ1; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; Q9USZ1; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q9USZ1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:PomBase.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISS:PomBase.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 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; IPR035649; EFG_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..770
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007448"
FT DOMAIN 57..353
FT /note="tr-type G"
FT BINDING 66..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 151..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 205..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 770 AA; 86325 MW; E237A371A4C11D28 CRC64;
MLKLSFRSLT SRLPRLSTLV VRGYASVANT GIEASNTSEN NLNIQEQLND NDKKRLKQIR
NIGISAHIDS GKTTFTERVL YYTGRIKDIH EVRGKDNVGA KMDFMELERE KGITIQSAAT
HCTWERTVDQ IEANEKQKTD FEKSYNINII DTPGHIDFTI EVERALRVLD GAVLVLCAVS
GVQSQTITVD RQMRRYNVPR ISFVNKMDRM GADPWKVIQQ INTKLKIPAA AVQIPIGQED
KLEGVVDLIQ MRAIYNRGSK GEKIEISQQV PENLIELAKE KRSALIEKLA DLDEEIADIY
VMEEDPTPEQ LMGAIRRTTL ARKFTPVLMG SALSNVGVQS VLDAVCDYLP NPSEVENIAL
NAADSEKPVS LVPSSEKPLV ALAFKLEEGR FGQLTYLRIY QGTLKRGNYI YNVNSTKKIK
VSRLVRMHSN DMEEIEKVEA GGICALFGIE CASGDTFTDG SVSYTMTSMF VPEPVISLSL
KPKSKDTTSF SKALNRFQRE DPTFRVQLDN ESKETIISGM GELHLEVYVE RMRREYKVDC
ETGKPRVAFR ETLSKKVPFS YLHKKQSGGA GQYAKVEGYI EYMDGVEDES GNVVDCEFIN
KVTGGTVPTQ YIPACEKAFY EALKKGFLIG HPIKNCRFVL EDGAYHPVDS SELAFRLATI
SAFRTAFLQA NPMVLEPIMN VSITAPVEHQ GGVIGNLDKR KATIVDSDTD EDEFTLQAEV
PLNSMFSYSS DIRALTKGKG EFSMEFLKYL PAPKYVQKEL VDAYNKQQQK
