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RRF2M_YEAS1
ID   RRF2M_YEAS1             Reviewed;         819 AA.
AC   B3LQ11;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=SCRG_03569;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408050; EDV12664.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LQ11; -.
DR   SMR; B3LQ11; -.
DR   EnsemblFungi; EDV12664; EDV12664; SCRG_03569.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   Proteomes; UP000008335; Unassembled WGS sequence.
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   Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   CHAIN           31..819
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385624"
FT   DOMAIN          39..327
FT                   /note="tr-type G"
FT   BINDING         48..55
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         113..117
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   819 AA;  91283 MW;  DDACCD85FC6F6798 CRC64;
     MWKWNVRRWA GARVNISKNR LSVINVGSRY LSTARSPLSK VRNIGIIAHI DAGKTTTTER
     MLYYAGISKH IGDVDTGDTI TDFLEQERSR GITIQSAAIS FPWRNTFAIN LIDTPGHIDF
     TFEVIRALKV IDSCVVILDA VAGVEAQTEK VWKQSKSKPK ICFINKMDRM GASFNHTVND
     LINKFMRGTT TKPVLVNIPY YRKQPTSNDY VFQGVIDVVN GKRLTWNPEN PDEIIVDELD
     GTSLEQCNRC RESMIETLTE YDEDLVQHFL EEAEGDYSKV SAQFLNASIR KLTMKNMIVP
     VLCGASFKNI GVQPLLDAIV NYLPSPIEAE LPELNDKTVP MKYDPKVGCL VNNNKNLCIA
     LAFKVITDPI RGKQIFIRIY SGTLNSGNTV YNSTTGEKFK LGKLLIPHAG TSQPVNILTA
     GQIGLLTGST VENNISTGDT LITHSSKKDG LKSLDKKKEL TLKINSIFIP PPVFGVSIEP
     RTLSNKKSME EALNTLITED PSLSISQNDE TGQTVLNGMG ELHLEIAKDR LVNDLKADVE
     FGQLMVSYKE TINSETNIET YESDDGYRFS LSLLPNSDAL PNCLAYPLGV NENFLIMEKN
     GNWDKEWKYQ VSFESILNSI IASCIVGLQR GGKIANFPLY ACSIKINSDW SVPPDIETPQ
     EILKITRNLI FKALNDLKPE KYNLLEPIMN LDLTIPQSDV GTVLQDLTGA RKAQILSIED
     ESSVSNSGAS TCNSPENSNR IYIPSDAVTT LHATKDKKNT QETSSNVKKI IKAKVPLREI
     TTYTNKLRSL SQGRGEFNIE YSDMEKVTND RLQSILHDL
 
 
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