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Database: UniProt
Entry: A0A094AQC5_9PEZI
LinkDB: A0A094AQC5_9PEZI
Original site: A0A094AQC5_9PEZI 
ID   A0A094AQC5_9PEZI        Unreviewed;      1354 AA.
AC   A0A094AQC5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=V493_00982 {ECO:0000313|EMBL:KFY31594.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY31594.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY31594.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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:KFY31594.1}.
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DR   EMBL; JPJV01000328; KFY31594.1; -; Genomic_DNA.
DR   STRING; 1420906.A0A094AQC5; -.
DR   HOGENOM; CLU_005548_0_0_1; -.
DR   OrthoDB; 148165at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000029327; 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:UP000029327};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1354
FT                   /note="Elongation factor G, mitochondrial"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001891901"
FT   DOMAIN          62..399
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          653..940
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          437..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..469
FT                   /note="Polar residues"
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         662..669
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         738..742
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         792..795
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   1354 AA;  145971 MW;  4487DF2281689BEC CRC64;
     MKTALLSGLA ATGYLLSSAA AAVHVPIVKN RHVEAEQLQR AQLRRRGTVT ESLGNAQHFG
     LYYANVTAGT PPQELSLQID TGSSDVWLPS STAQLCNMRR GCEGGSFNTS ASSTFRVVGR
     DDFNISYVDG TGSLGSYFTD SFGIGGKTLQ NFQMGLGEDT TISIGILGIG YANSVANIFT
     GSGTSYVNLP PAMVDAGFIN TPAYSLWLDD IKASAGSILF GGIDTTKFTG ELQSIKAYPS
     TRSGNVTSFT VAFTSLEATS SSGTDLLTPS TYAQPAILDS GTTLTLLPDN IAALVFQELG
     AINDPDLEAV VIPCSLAQNS GSLKFGFGGV GGPVIDVPVN ELVLPLTLTT GGTPKFENGA
     DACQLGIQAA GDLPILFGDT FLRSAYVVYD LANNQVGLAQ TDFNAKGSNI VEFASMGAQI
     PEAVTATGQD QIGVAQTKTG IPRGGEASQT ATGDGVIEGN TSPTGGLNAA GGFASNEDGD
     ESAGGRLEPP KWGAIPFLGA AGAAIVYGTR IALPPFPIPS FSATYIRDDE GSTSSRDSGG
     GWRSGAPEDF TERADGGQVP VSLCEGERDG EGWWIEGWGG GDAEEGIFRD EADEERGCGR
     GIVALAFERS HDRMNCADRD FYYRAKPEPV VPMGPSLEQI QIDMSPAEKG RLSKLRNIGI
     AAHIDSGKTT CTERVLFYTG RIKAIHEVRG RDSVGAKMDS MDLEREKGIT IQSAATFCDW
     KKKNVDGVEE MFHFNLIDTP GHIDFTIEVE RALRVLDGAV MVLCAVSGVQ SQTITVDRQM
     KRYNVPRISF VNKMDRMGAN PFKAVDQINQ KLKLNAAAIQ VPIGGEDSFK GVVDLLRMKA
     IYFEGEQGTT IRETDEIPPD VLPIAQERYR MLIEAVADVD DEIAELFLDE KLPTTAQLKA
     AIRRTTIALK FTPVMMGSAL ANKGIQPVLD AVCDYLPDPS EVPNLALDQR KAEAPVQLVP
     YNTLPFVGLA FKLEESNFGQ LTYIRVYQGS LKKSMNVFNA RNDKKVKIPR IVRMHSNEME
     EVPEVGAGEI CAVFGVDCAS GDTFTDGNLP YTMSSMFVPE PVISLSITPK NKTDTNNFSK
     AMNRFQREDP TFRVHVDSES SENIISGMGE LHLEVYVERM RREYRVDCVT GQPRVAYRET
     ITKHVEFDHT LKKQTGGAGD YARVVGYVEP TGSLTSNKFE QQVTGGSIDE KFLFACDKGF
     QASCEKGPML QHRVLGTSMV INDGATHMTD SSEMAFKMAT QQAFRKAFLQ ASPVVLEPLM
     KTTITAPNEF QGNIVGLLNK RNGVILDTEI GPEDFTLTAD CSLHAMFGFS SQLRAATQGK
     GEFGMEFSHY APAPMQIQKE LIAKHEKMLA EKRK
//
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