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RRF2M_DEBHA
ID   RRF2M_DEBHA             Reviewed;         860 AA.
AC   B5RUN4;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=DEHA2F24662g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66412.1; -; Genomic_DNA.
DR   RefSeq; XP_002770895.1; XM_002770849.1.
DR   AlphaFoldDB; B5RUN4; -.
DR   SMR; B5RUN4; -.
DR   STRING; 4959.XP_002770895.1; -.
DR   EnsemblFungi; CAR66412; CAR66412; DEHA2F24662g.
DR   GeneID; 8999064; -.
DR   KEGG; dha:DEHA2F24662g; -.
DR   VEuPathDB; FungiDB:DEHA2F24662g; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   InParanoid; B5RUN4; -.
DR   OMA; AVCQIPW; -.
DR   OrthoDB; 637899at2759; -.
DR   Proteomes; UP000000599; 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..860
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385614"
FT   DOMAIN          45..337
FT                   /note="tr-type G"
FT   BINDING         54..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         118..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         172..175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   860 AA;  95795 MW;  26952D63D27EA84B CRC64;
     MTNTGPIVRR VFRYASVLDT ICYKRGIHSS RALLSESRLN SVPPDRTRNI GIIAHIDAGK
     TTTTERMLFY SGKTRRIGNV DEGDTVTDYL PSERERGITI QSAAITIPWN KNKINIIDTP
     GHADFTFEVT RSLRVLDSCV TILDAVAGVE AQTEKVWKQA QALGIPKIAY VNKMDRDGAG
     FSRTVKEIIQ KLQTRVVLCN IPYWETPVND VPIFKGVLDV LNKKLLKWNS DSNANGTDIS
     VTDLEKEMDK YPELYEMVSK SRESMVETLG EFDETIIDSF LENDEDYMKI PVAVLNSAIK
     RGTLANYVTP VFCGSSFRNI GVQPLMDAVV NFLPSPLETK VPDISSNAPK ALAKMKGKNR
     KKKVTSEPTD VPLSMDPKHG LVINKNPNLT TALAFKVITH PTRGVMTFFR VYSGKLTSNT
     TIMNTRTGKK LNLRKLLLMH GDEPEVVPSI SAGNIGVISG TDDDIVTGDT IVSHGPVNKP
     FNDLESSLKM LPIEIPPPLF NSSIEPLTAG DTRHLNSCIQ ILLREDPSLK VSVDEDLGQI
     ILSGMGELHL EIIKERLVTD MKANARLRDV AVSYKETLGK PNYKSVTQST GDNGCVSIEI
     SMDSFEGLAE ESSFADEDGA IVLEHENNIV ILEPSATPEY MQTAIDERRW KSDHSLEDLQ
     ESLVHGCITA LQLGGPVFGF ALHSTVIRIK NWHFPVDSKD YNSSSLLDIS RRAVTKNIKD
     LGESEKDLFS LLEPIMQTKV YINSDSLGEV VHDLTHRCQA TITSIDDESE NMDALNWANE
     ESERVYVPPD YTMKNTNNLQ VELRNKKVIV AETPLREMIG YLSRLRSITQ GRGVFDMSYL
     GMKRVIKSRL ASISNEFNFM
 
 
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