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Database: UniProt
Entry: A0A0V0VDY7_9BILA
LinkDB: A0A0V0VDY7_9BILA
Original site: A0A0V0VDY7_9BILA 
ID   A0A0V0VDY7_9BILA        Unreviewed;      1076 AA.
AC   A0A0V0VDY7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   08-NOV-2023, entry version 39.
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   ORFNames=T09_11609 {ECO:0000313|EMBL:KRX61712.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61712.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX61712.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX61712.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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 universal ribosomal protein uS5 family.
CC       {ECO:0000256|RuleBase:RU003823}.
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:KRX61712.1}.
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DR   EMBL; JYDN01000045; KRX61712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VDY7; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; 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   CDD; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.30.230.10; -; 2.
DR   Gene3D; 3.30.70.240; -; 1.
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; 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; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR005324; Ribosomal_uS5_C.
DR   InterPro; IPR005711; Ribosomal_uS5_euk/arc.
DR   InterPro; IPR013810; Ribosomal_uS5_N.
DR   InterPro; IPR018192; Ribosomal_uS5_N_CS.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00231; small_GTP; 1.
DR   NCBIfam; TIGR01020; uS5_euk_arch; 1.
DR   PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 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; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 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; 2.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
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}; Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03061};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03061}; Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Ribonucleoprotein {ECO:0000256|PROSITE-ProRule:PRU00268,
KW   ECO:0000256|RuleBase:RU003823};
KW   Ribosomal protein {ECO:0000256|PROSITE-ProRule:PRU00268,
KW   ECO:0000256|RuleBase:RU003823}.
FT   DOMAIN          35..312
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   DOMAIN          893..956
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
FT   REGION          818..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         111..115
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         165..168
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   1076 AA;  118227 MW;  51BA26B0F96F536F CRC64;
     MNCIVKTIQY ALFKQRAQKF QLRYFCGEAE IIPSDKIRNI GISAHIDSGK TTVTERILYY
     AGRIKEMHEV KGKDQVGATM DFMELERQRG ITIQSAATYV HWKNVMVNII DTPGHVDFTV
     EVERALRVLD GAVLILCGVA GVQSQTFTVY RQINRYNVPF IAFVNKLDRQ NANAHRVLNS
     MRQRLGLNTA FLHLPIGTEN NFSGLVDIIN QHALFFDGPQ GEIIRKDEIP KEMRAESQDR
     LFELIEHVSN VDDILGELFL LEKKPTADQL RAAIRRAVLG RKFIPVCLGS ALKNKGVQPL
     LDAIIDYLPN PSEVENLANV EIDGHVVQER LDPSRTDQKP FVGLAFKLEA GKFGQLTYFR
     IYQGRLGRGS AIVNSRTWKR TRDIEEAYAG DICATFGLEC ASGDTFLSDA SRKLALDADN
     FLKALNRFCK EDPTFHREYN VEAKEVIVSG MGELQLEVYA QRMKAEYNCE VELGKPKVAF
     RETLTEKCAF DYWHRKQTGG HGQYGRVIGV CEPLPPNQNL DLIFTDECIG TNVPKQFMPA
     IDKGFREACQ KGPLIGAPVT GIRFRLKDGA HHIVDSTEIA FILTAKYAMN DVFSDGRWHI
     IEPVMKVEAT CPTEFQGSVM AALSKRQAVI ISTDLIENFF SVVCEAPLNC MFGFVTELRS
     LTEGKGEYSM EYSRYAPLKP EIAEQLISES SRAQSEKVKS YFECFARCPP FQLLINTPLY
     LFAHICRQRV SYIHMTDRGG FHGGFGTSAF GEATAGFGDA GAGFGDPGVG FGEAGFGSAG
     GFGDSAGGGF GGSGFRGGNF AYSRGGSSGG FGRASFYGSG RGGRGGRGRG SRGRGRGGRG
     GARGKEGAKE WIPVTKLGRL VKDGKIKSLE EIYLHSLPIK EFEIIDFLLG EQLKDDVLKI
     MPVQKQTRAG QRTRFKAFVA IGDYNGHVGL GVKCSKEVAT AIRGAIIAAK LSVIPVRRGY
     WGNKIGKPHT VPCKVTGKCG SVLVRLIPAP KGTGIVSAPV PKKLLQMAGI DDCYTCAKGS
     TGTLGNFAKA TYAAIAATYS YLTPDLWKGA ALSRSPYQAF AEFLKSNPLS VAQEKD
//
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