ID F8L7A9_SIMNZ Unreviewed; 344 AA.
AC F8L7A9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000256|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000256|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000256|HAMAP-Rule:MF_00093,
GN ECO:0000313|EMBL:CCB88631.1};
GN OrderedLocusNames=SNE_A07540 {ECO:0000313|EMBL:CCB88631.1};
OS Simkania negevensis (strain ATCC VR-1471 / Z).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Simkaniaceae;
OC Simkania.
OX NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB88631.1, ECO:0000313|Proteomes:UP000000496};
RN [1] {ECO:0000313|EMBL:CCB88631.1, ECO:0000313|Proteomes:UP000000496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
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:0000256|ARBA:ARBA00002986, ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000256|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00093}.
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DR EMBL; FR872582; CCB88631.1; -; Genomic_DNA.
DR AlphaFoldDB; F8L7A9; -.
DR STRING; 331113.SNE_A07540; -.
DR KEGG; sng:SNE_A07540; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR Proteomes; UP000000496; Chromosome gsn.131.
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; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 6.10.140.1950; -; 1.
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 NCBIfam; TIGR00019; prfA; 1.
DR PANTHER; PTHR43804; LD18447P; 1.
DR PANTHER; PTHR43804:SF7; LD18447P; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00093};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00093}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00093};
KW Reference proteome {ECO:0000313|Proteomes:UP000000496}.
FT DOMAIN 227..243
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 344 AA; 38992 MW; 44539C2D2CB591AA CRC64;
MEDKVKELLG RLPDLEAKLG DPKVTQDQKK YRELSQEHAY LSDLKEAWTD FVKQSKDLKD
NRDLLKEETD PEFVQVVQDD IAKLETAVQN SRSRIESLLV PPDPNDHANV IMELRAGTGG
DEAAIFVGDC LRMYRLFADH MGWKYETLSC TDSEVGGYKE YILSLSGKNV HRFLQYEAGT
HRVQRVPVTE TQGRVHTSAI TIAVLMEPGE NEPIDIDESD LKIDTYRSSG AGGQHVNTTD
SAVRITHMPT GVVVYCQEER SQHKNKAKAM RVLAARLAEE KMRKAQQERA SLRSSQVGSG
DRSERIRTYN FSQNRLTDHR INLTLYKLDH CDGRGLRRSL SSPC
//