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Database: UniProt
Entry: A0A094JIQ7_9PEZI
LinkDB: A0A094JIQ7_9PEZI
Original site: A0A094JIQ7_9PEZI 
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
//
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