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RF1_MYCAP
ID   RF1_MYCAP               Reviewed;         358 AA.
AC   A5IZH6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=MAG7350;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; CU179680; CAL59435.1; -; Genomic_DNA.
DR   RefSeq; WP_004024169.1; NC_009497.1.
DR   AlphaFoldDB; A5IZH6; -.
DR   SMR; A5IZH6; -.
DR   STRING; 347257.MAG7350; -.
DR   PRIDE; A5IZH6; -.
DR   EnsemblBacteria; CAL59435; CAL59435; MAG7350.
DR   KEGG; maa:MAG7350; -.
DR   HOGENOM; CLU_036856_0_1_14; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000007065; 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   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..358
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_1000093476"
FT   REGION          291..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         237
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   358 AA;  40472 MW;  AFFA6E218F003FDA CRC64;
     MEKTMFKSLS EIKQSYLELL KKIDDPEVIS NIKEYSAINK EIAKIREISE KFITYENILK
     DVEQAKIMLE SKNEEEVEFA KMIIDENSLK LDELEEKLKI LILPQDENDD KNIIVEIRGA
     AGGDEANIFA GDLFRMYSKF ADELGFRLKI LSTNSASAGG FSQIVFSIKG EKAYSKFKFE
     SGVHRVQRVP VTESQGRIHT STTTVTVMPE IDDSVEIEIK PSDLKIDVFR SSGAGGQSVN
     TTDSAVRITH LPTNIVVTSQ DERSQIANRE TALTILKSKL YDLEMQKKAE EESGYRKLAG
     HGDRSEKIRT YNYPQDRVTD HRISFSTSLK PIMEGKLTPI IDALLAEEQN QKIKESGF
 
 
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