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
//