RRF2M_KLULA
ID RRF2M_KLULA Reviewed; 800 AA.
AC Q6CK29;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribosome-releasing factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=RRF2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE AltName: Full=Elongation factor G 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=EF-G2mt {ECO:0000255|HAMAP-Rule:MF_03059};
DE Short=mEF-G 2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN Name=MEF2 {ECO:0000255|HAMAP-Rule:MF_03059};
GN OrderedLocusNames=KLLA0F13992g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC ribosomes from messenger RNA at the termination of mitochondrial
CC protein biosynthesis. Not involved in the GTP-dependent ribosomal
CC translocation step during translation elongation. {ECO:0000255|HAMAP-
CC Rule:MF_03059}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03059}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03059}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03059}.
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DR EMBL; CR382126; CAG98418.1; -; Genomic_DNA.
DR RefSeq; XP_455710.1; XM_455710.1.
DR AlphaFoldDB; Q6CK29; -.
DR SMR; Q6CK29; -.
DR STRING; 28985.XP_455710.1; -.
DR EnsemblFungi; CAG98418; CAG98418; KLLA0_F13992g.
DR GeneID; 2894883; -.
DR KEGG; kla:KLLA0_F13992g; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q6CK29; -.
DR OMA; AVCQIPW; -.
DR Proteomes; UP000000598; Chromosome F.
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:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0032790; P:ribosome disassembly; IEA:UniProtKB-UniRule.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd03713; EFG_mtEFG_C; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_03059; mEF_G_2; 1.
DR InterPro; IPR030851; EFG2.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
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; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 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 SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..800
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385616"
FT DOMAIN 21..307
FT /note="tr-type G"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 95..99
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 800 AA; 89519 MW; 7ECA382C358DE182 CRC64;
MQHTMSFRIF LRRYATKHDL SKVRNIGIIA HIDAGKTTTT ERMLYYSGKI NRIGDVDQGD
TITDYLPQER SRGITIQSAA ISFNWKKDYK INLIDTPGHA DFTFEVIRSL KVLDSCVTIL
DSVAGVEAQT EKVWKQSSGL PKICFLNKMD RVGAGFSRTV KELVVKMNTR ALLINTPIFQ
VDPVTNESKF SGVLDLIYGK QLIWDTNDPD KINVTDVDEN HDCYEYLVRG REALVETLGE
TDESIVEHFF NDADGEYLNV SPEVLNASIR KATISLSATP VLCGASFRNI GVQPLLDAIA
NYLPSPSEAR PPELNHKNVP ITQNPLTGLV LNKNPNLCVA LAFKVITDAI RGTMIFIRVY
SGVLRSNHTV YNTTTGTKFK IGKLVRMHAN VPEEVNELYP GDIGVLTGSN VSEHIRTGDT
IVTHVTKKDG LRSFDKNVEL TLKINPIEIP PPVFNAAIEP KTLGNKKPME QALSQLTRED
PSLVVTHDEE TGQTLLSGMG ELHLDIARDR LLNELNAQVD VERVIVSYKE TLNHSTQEKT
LETDDGYKIT AVIEPLDEEM KAKAKKDEEW FSLANDNNFM IMEKHTKYDP DKNWPFQVPY
VAVVNALLPS SLVALQRGGK IGGFPLSSCV IRIKNDWDLP IDAPSISPLL TLSRQLFTQI
LLGEDQSNYS VLEPVMNVDV TVQQQDMGPV IQDLSSARKA NILSIEDENT NTVSESNIRF
QHIADKMWLP EDPTLEFAKL GKEGQAPKMV KAQAPLKEMV AYNNKIRSIT QGRGSFNMYY
HGMQPVTHDR LQSVLADYHQ
