ID A0A094JIQ7_9PEZI Unreviewed; 1365 AA.
AC A0A094JIQ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000256|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000256|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000256|HAMAP-Rule:MF_03061};
GN Name=MEF1 {ECO:0000256|HAMAP-Rule:MF_03061};
GN ORFNames=V502_09086 {ECO:0000313|EMBL:KFZ08883.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ08883.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ08883.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000256|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03061}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC G/EF-2 subfamily. {ECO:0000256|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:0000256|ARBA:ARBA00005870}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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:KFZ08883.1}.
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DR EMBL; JPKE01003008; KFZ08883.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094JIQ7; -.
DR HOGENOM; CLU_005548_0_0_1; -.
DR OrthoDB; 148165at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070125; P:mitochondrial translational elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01886; EF-G; 1.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04091; mtEFG1_II_like; 1.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR047872; EFG_IV.
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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR033876; SAP-like.
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 NCBIfam; TIGR00484; EF-G; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR Pfam; PF00026; Asp; 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; PR00792; PEPSIN.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW Rule:MF_03061};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03061}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03061}; Protease {ECO:0000256|RuleBase:RU000454};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03061}; Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1365
FT /note="Elongation factor G, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001905311"
FT DOMAIN 62..399
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 664..951
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 427..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT BINDING 673..680
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 749..753
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT BINDING 803..806
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ SEQUENCE 1365 AA; 146750 MW; FEA26206F9FFA160 CRC64;
MKTALLSGLA ATGYLLSSAT AAVHVPIVKN RHVEAEQLQA AQLRRRGTVT ESLGNAQHFG
LYYANITAGT PPQELSLQID TGSSDVWLPS STAQLCNTRE GCEGGSFDSS ASSTFEVVGQ
DEFNISYVDG TGSAGSYFTD SFGIGGKTIK NFEMGLGEDT TISIGILGIG YANSVANVFT
GTGTSYVNLP LALVNAGLIN TPAYSLWLDD IQSSAGSILF GGIDTAKYTG QLQSIKVYPS
SRSGNVTSFT VAFTSLHASS SSGTDLLTPS TYAQPAILDS GTTLTLLPDD VAALVFEELG
AIDDKDIEAV VVPCSLASNS GSLKFGFGGA SGPVITVAVS ELVLPLTLTN GGTPKFENGA
DACQLGIQAA GDLPILFGDT FLRSAYVVYD LANNQIGLAQ TDFNATGSNI VEFASMGAAI
PQATTASGQD QIGVSQTKTG IPRGGEATQT ASGDGIVQGN PTSTGGLTAA SGFASNEATT
ADESAGGRLE PPRWGGAVFL GAWMGIMGAA IVVWTRIALT PFPIPSFPAT YIRRDEGSTS
SRDSGGSRRS GAPADFTERA DGGQVPVSLC EGERDGEGWW IEGWGGGDAE EGVFGDEGDE
ERGGCGMFRE GERRIGFREI SRLNELRANR DFYYRAKPEP VVPLGPSLEQ IQIDMSPSEK
GRLSKIRNIG IAAHIDSGKT TCTERVLFYT GRINAIHEVR GKDAVGAKMD SMDLEREKGI
TIQSAATFCD WKKKNVDGVE ELFHFNLIDT PGHIDFTIEV ERALRVLDGA VMVLCAVSGV
QSQTITVDRQ MKRYNVPRIS FVNKMDRMGA NPFKAVDQIN HKLKLNAAAI QVPIGGEDSF
KGVVDLLRMK AIYFEGEQGT TIRETDEIPP DVLPIAEERK RMLIEAVADV DDEIAELFLE
EKVPTTAQLK AAIRRTTIAL KFTPVMMGSA LANKGLQPVL DAVCDYLPDP SEVPNLALDQ
RKAEAPVQLV PYNTLPFVGL AFKLEESNFG QLTYIRVYQG SLKKAMNVYN ARNDKKVKIP
RIVRMHSNEM EEVPEVGAGE ICAVFGVDCA SGDTFTDGSL PYTMSSMFVP EPVISLSITP
KNKTDTNNFS KAMNRFQRED PTFRVHVDSE SHENIISGMG ELHLEVYVER MRREYRVDCV
TGQPRVAYRE TITKHVDFDH TLKKQTGGAG DYARVVGYLE PTGSLTTNKF EQQVTGGSID
EKFLFACDKG FQAACDKGPL LQHRVLGTSM VINDGATHMT DSSEMAFKIA TQQAFRKAFL
QAGPVVLEPL MKTTITAPNE FQGNIVGLLN KRNGVILDTE IGPEDFTLTA DCSLHAMFGF
SSQLRAATQG KGEFGMEFSH YAPAPMQIQK ELIAKHEKAL ADKRK
//