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RF1_METMA
ID   RF1_METMA               Reviewed;         415 AA.
AC   Q8PX75;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Peptide chain release factor subunit 1 {ECO:0000255|HAMAP-Rule:MF_00424};
DE   AltName: Full=Translation termination factor aRF1 {ECO:0000255|HAMAP-Rule:MF_00424};
GN   Name=prf1 {ECO:0000255|HAMAP-Rule:MF_00424}; OrderedLocusNames=MM_1347;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00424}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00424}.
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DR   EMBL; AE008384; AAM31043.1; -; Genomic_DNA.
DR   RefSeq; WP_011033293.1; NC_003901.1.
DR   PDB; 3IR9; X-ray; 2.21 A; A/B=252-415.
DR   PDBsum; 3IR9; -.
DR   AlphaFoldDB; Q8PX75; -.
DR   SMR; Q8PX75; -.
DR   STRING; 192952.MM_1347; -.
DR   DNASU; 1479689; -.
DR   EnsemblBacteria; AAM31043; AAM31043; MM_1347.
DR   GeneID; 24879663; -.
DR   KEGG; mma:MM_1347; -.
DR   PATRIC; fig|192952.21.peg.1561; -.
DR   eggNOG; arCOG01742; Archaea.
DR   HOGENOM; CLU_035759_3_0_2; -.
DR   OMA; GQEMEVV; -.
DR   EvolutionaryTrace; Q8PX75; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   Gene3D; 3.30.960.10; -; 1.
DR   HAMAP; MF_00424; Rel_fact_arch_1; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR024049; eRF1_1_sf.
DR   InterPro; IPR005141; eRF1_2.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR020918; Peptide_chain-rel_aRF1.
DR   InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR   PANTHER; PTHR10113; PTHR10113; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03464; eRF1_2; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
DR   SUPFAM; SSF55481; SSF55481; 1.
DR   TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..415
FT                   /note="Peptide chain release factor subunit 1"
FT                   /id="PRO_0000143176"
FT   HELIX           259..290
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          296..299
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   HELIX           300..307
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   TURN            308..310
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          312..318
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          324..334
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          336..341
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   TURN            356..358
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          361..369
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   HELIX           370..380
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          384..388
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   HELIX           393..400
FT                   /evidence="ECO:0007829|PDB:3IR9"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:3IR9"
SQ   SEQUENCE   415 AA;  46190 MW;  97EDFE1C4411E816 CRC64;
     MTEQSAHEKY EFKKKLEGLR DKKGRSTELI SLYIPPDKQI FDVTNQLKDE HGQAANIKSK
     LTRTNVQGAI ESLLSRLRYL DKVPENGIVY FTGAVDIGAN KTSMESEVIV PPDPITVYKY
     HCDSSFYLEP LEDMLKDKNT YGLLVLDRRE ATIGLLVGKR IQPFRNLTST VPGKQRKGGQ
     SAHRFQQLRL IAIHDFYKRI GDAASEVFMA VDHKDLKGVL IGGPSPTKEE FHAGEFLHHE
     LMKKILGLFD TAYTDESGLS ELVNAAGEKL QDLELMGQKN AVRDFFKELI ADSGKVAYGE
     SQVRANLEIN SVDVLLLSED LRAERVTTKC SVCGYENKWT RRWKPGEPAP AAGNCPKCGS
     SLEVTDVTDI VDEFSELADK SNAKVVFVST DFDEGSQLMN AFGGIAAILR YNTGV
 
 
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