RRF2M_PICST
ID RRF2M_PICST Reviewed; 845 AA.
AC A3LWR2;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
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};
DE Flags: Precursor;
GN Name=MEF2 {ECO:0000255|HAMAP-Rule:MF_03059}; ORFNames=PICST_67982;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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 -!- 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; CP000500; ABN67321.2; -; Genomic_DNA.
DR RefSeq; XP_001385350.2; XM_001385313.1.
DR AlphaFoldDB; A3LWR2; -.
DR SMR; A3LWR2; -.
DR STRING; 4924.XP_001385350.2; -.
DR EnsemblFungi; ABN67321; ABN67321; PICST_67982.
DR GeneID; 4839873; -.
DR KEGG; pic:PICST_67982; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; A3LWR2; -.
DR OMA; AVCQIPW; -.
DR OrthoDB; 637899at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
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; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT CHAIN 29..845
FT /note="Ribosome-releasing factor 2, mitochondrial"
FT /id="PRO_0000385620"
FT DOMAIN 38..330
FT /note="tr-type G"
FT BINDING 47..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 111..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ SEQUENCE 845 AA; 94401 MW; 6E249D56344A4FBD CRC64;
MIIATSLRSQ TFCTWRAWRA VHSTAVRLES KLNEVPIDRT RNIGIIAHID AGKTTTTERM
LYYSGKTKRI GNVDEGDTVT DYLPSERQRG ITIQSAAISI PWNNHKINII DTPGHADFTF
EVTRSLRVLD GAVTILDGVA GVEAQTEKVW KQATSLNIPK IAYVNKMDRP GAGFSRTVME
IIEKLQTRVV LCNVPYFENS KDNDPVFCGV ADILHVKLLK WNPEIDPHGK NITVIDIEAE
RDTYPEVYET VVKSRESMVE TLGEFDEAII DSFLESNEDY MNIPINVLNE AIRKATLENY
LTPVYCGSSF RNIGVQPLMD GVVKYLPSPL QISVPEITSS ATKNVKIKHV KAKQAVKQDM
EVTTKMNNRT GLVVNANPNL TLALAFKVMT HATRGVMTFF RVYSGKLVSN SIITNTTTGK
KLHVKKLFMM HGDEPEEVKH ISSGNIGVIT GHEDDIQTGD TLVSHSHLKK GFSEMESNLK
LLPIEIPPPL FNSAIEPQTA GDEAYMKECV RILTREDPSL KVSVDEEMGQ TIISGMGELH
LDIVKERLVR DMKAKVTLRD VAVSYKETLL NPGSSYKQTS ESGSVSIEIE MDSFEGAAEE
SSFFEENGAM IIAEDNNIII IEPSAISQNM LKALEERRWK STYSLEDLQE IVIQGCLTAL
QMGGPIFGLS LHSTVIRVKS WDFPVADSSV ASTVLLDVSR SAVTSYIATN RDWFGILEPI
METRVYIDSD IMGEVSHDLT QRCQAVIKSI EDESTQDVDA LAWAKDEAEK TFLPPDYTMK
AGKDAISYKN KKIIIAETPL REMIGYLSRL RSITQGRGTF DMTYIGMRRA IKSRFDAISK
EFNFM
