RF1_STRCO
ID RF1_STRCO Reviewed; 358 AA.
AC Q9K4E4;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
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=SCO5360;
GN ORFNames=2SC6G5.04;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939123; CAB94531.1; -; Genomic_DNA.
DR RefSeq; NP_629499.1; NC_003888.3.
DR RefSeq; WP_003973637.1; NZ_VNID01000011.1.
DR AlphaFoldDB; Q9K4E4; -.
DR SMR; Q9K4E4; -.
DR STRING; 100226.SCO5360; -.
DR GeneID; 1100800; -.
DR KEGG; sco:SCO5360; -.
DR PATRIC; fig|100226.15.peg.5440; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_11; -.
DR InParanoid; Q9K4E4; -.
DR OMA; ISDHRVG; -.
DR PhylomeDB; Q9K4E4; -.
DR Proteomes; UP000001973; 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_0000177749"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 39460 MW; 9E077D6BB92C70B0 CRC64;
MFEAVEELVA EHADLEKKLA DPSVHSDQAN ARKLNKRYAE LTPIVATFRS WKQTGDDMET
AREFAADDPD FAAEVKELDK QRDELTEKLR LLLVPRDPSD DKDVILEIKA GAGGDESALF
AGDLLRMYLR YAERIGWKTE IIDSTESELG GYKDVQVAVK TKGGQGATEP GQGVWARLKY
EGGVHRVQRV PATESQGRIH TSAAGVLVTP EAEEIDVEIN PNDLRIDVYR SSGPGGQSVN
TTDSAVRITH IPTGVVASCQ NEKSQLQNKE QAMRILRSRL LAAAQEEAEK EAADARRSQV
RTVDRSEKIR TYNFPENRIS DHRVGFKAYN LDQVLDGDLD SVIQACVDAD SAAKLAAA
