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RRF2M_ASPNC
ID   RRF2M_ASPNC             Reviewed;         861 AA.
AC   A2R994;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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; ORFNames=An17g00570;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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; AM270385; CAK42985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2R994; -.
DR   SMR; A2R994; -.
DR   PaxDb; A2R994; -.
DR   EnsemblFungi; CAK42985; CAK42985; An17g00570.
DR   VEuPathDB; FungiDB:An17g00570; -.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   Proteomes; UP000006706; Chromosome 5L.
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:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:EnsemblFungi.
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; 3.30.230.10; -; 2.
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; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_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   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 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..17
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   CHAIN           18..861
FT                   /note="Ribosome-releasing factor 2, mitochondrial"
FT                   /id="PRO_0000385610"
FT   DOMAIN          63..353
FT                   /note="tr-type G"
FT   BINDING         72..79
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         137..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
FT   BINDING         191..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03059"
SQ   SEQUENCE   861 AA;  93544 MW;  CDD94D12419A1E9E CRC64;
     MVTALFLRAS HQTVRPTGLR QCQAAASRLG CNASLIPGVK KGQFPKIQML STSASKLQAD
     TLDRTRNIGI IAHIDAGKTT TTERMLYYSG FTRRIGDVDE GSTVTDFLPA ERARGITIQS
     AAITFHWPPQ AAVNLIDTPG HADFTFEVMR SLRILDGAVC ILDGVAGVEA QTERVWHQAS
     TYRIPRIVYI NKLDRDGAAF GRTVREISSR LAGYPAVCQV PWFEGGNGRF VGVGDAINLQ
     GLRWQDGDGK AVKMFNLQEL DGEEPGLAQE IKRARTALVE LLSEHDETMI EKFFEHDEDH
     LAVPPNDILD SLRRCLLQEQ GRKIIPIFAG ASFRNIGVQP LLDAVTNLLP SPLETPDAEK
     KSVTQAESQN AIEKLQSCAL AFKVVNDAKR GVLVYVRVYS GSLDRNSAIF NTNLKITERA
     PRLLKMYAND AVEVDSIPEG HIGVVAGLKH ARTGDTLVSY AGNKLTPPEP LDTLQLRPIQ
     VPPPVFFASI EPHSLSEEKK IHECLALLLR EDPSLHVTVD EDSGQTLLSG MGELHLEIAR
     DRLINDLKAK ATMGRIEIGY RECPLGESPV VTKMFDKEIA GRKGKAGCTA VVEPFDPDNA
     PPVPEDALSV ETKEGNQIII IAPELQVETN RKGIEESPVL PPGLDMQSFR ASLHNGCLAA
     LARGPQFTFP MHHTRVTLTI NPTEHLFGTD TTPAALSSAA RLATSAALRD LLSSGPGTSL
     MEPVMNVIIS IDEASLGAVV HDISSSRGGH IVSLDEEIPL TSTDLSASPQ PVEDLPPIDP
     KKVYAPADPF ESGSVGASLP DTANRPRTIT AKVPLKEMVG YLKHLRSLSA GHGTFVMSVD
     RFEKMSTPRQ KAVLTELRGG F
 
 
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