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Database: UniProt
Entry: C4R1X6_KOMPG
LinkDB: C4R1X6_KOMPG
Original site: C4R1X6_KOMPG 
ID   C4R1X6_KOMPG            Unreviewed;       749 AA.
AC   C4R1X6;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 89.
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   OrderedLocusNames=PAS_chr2-2_0409 {ECO:0000313|EMBL:CAY69500.1};
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY69500.1, ECO:0000313|Proteomes:UP000000314};
RN   [1] {ECO:0000313|EMBL:CAY69500.1, ECO:0000313|Proteomes:UP000000314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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}.
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DR   EMBL; FN392320; CAY69500.1; -; Genomic_DNA.
DR   RefSeq; XP_002491780.1; XM_002491735.1.
DR   AlphaFoldDB; C4R1X6; -.
DR   SMR; C4R1X6; -.
DR   STRING; 644223.C4R1X6; -.
DR   EnsemblFungi; CAY69500; CAY69500; PAS_chr2-2_0409.
DR   GeneID; 8198298; -.
DR   KEGG; ppa:PAS_chr2-2_0409; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   InParanoid; C4R1X6; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 148165at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000314; Chromosome 2.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   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   Gene3D; 3.30.230.10; -; 1.
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; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
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; 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; 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; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 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; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 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};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW   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:UP000000314}.
FT   DOMAIN          59..340
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         68..75
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         139..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
FT   BINDING         193..196
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   749 AA;  83130 MW;  0AF83F01D52FC6B0 CRC64;
     MMFVRRVVSS YGGVVTKMFD SPIRRSFTCG RISKSYEEDS VVLSEISKSI SSADTESLVR
     MRNIGISAHI DSGKTTFTER VLFYTGRINS IHEVRGRDKV GATMDSMELE REKGITIQSA
     ATYCNWQKED KNYHFNLIDT PGHIDFTIEV ERALRVLDGA VLVVCAVAGV QSQTVTVDRQ
     MRRYDIPRIT FINKMDRMGA DPFKAIDQIN SKLKIPAAAI QVPIGNEKDL KGVVNIIDRL
     ALYNEGNQGE TLRVSDIPPE LKNLVEEKRK ILIETLADVD DEIAECFIEE VDPTVEQIKN
     AIRRSTISRK FTPVLMGSAL ANTGIQPVLD AVVDYLPNPA EVLNTGLDIS NNEMKVNLVP
     SSKEPFVGLA FKLEEGKYGQ LTYLRVYQGK LKKGGYISNV KDGKKIKVAR LVRMHADDME
     DVDSIGAGEI CATFGIDCAS GDTFTDGSLK YAMSSMYVPD AVVSLSISPK TKDVANFSKA
     MNRFQKEDPT FRVKFDSESK ETIISGMGEL HLEIYVERMK REYNVECSTG RPQVSYRESI
     QGSSSFDYTH KKQSGGAGQF ARVIGEMTAE TQPRNVFETK VVGGRISEKF LQACARGFEE
     ACEKGPLIGH RVIGVNMLIN DGATHVVDSN EMSFKTATQA AFKQAFQNSN PVILEPIMNT
     AVTAPAEFQG SIISLLNKLQ AIIQDTENSA EEFTVTADCS LNELFGFASS LRAVTQGKGE
     FSMEFKEYQP CPPQLQRQLI EEHNKKGKK
//
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