ID A0A1H0PYB8_9PSED Unreviewed; 360 AA.
AC A0A1H0PYB8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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 ORFNames=SAMN05216193_12235 {ECO:0000313|EMBL:SDP10093.1};
OS Pseudomonas jinjuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=198616 {ECO:0000313|EMBL:SDP10093.1, ECO:0000313|Proteomes:UP000242957};
RN [1] {ECO:0000313|Proteomes:UP000242957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21621 {ECO:0000313|Proteomes:UP000242957};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNIJ01000022; SDP10093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0PYB8; -.
DR STRING; 198616.SAMN05216193_12235; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000242957; Unassembled WGS sequence.
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:UP000242957}.
FT DOMAIN 230..246
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 360 AA; 40198 MW; F5BF1602799D98D3 CRC64;
MKASLLKKLD ILSDRYEELT ALLGDAEVIS DQTKFRAYSR EYAEVEPVIL AFREFRKVQD
DLEGAQALLK DSDPDLREMA EEEVASARAR IAGLEDSLQR MLLPKDPNDQ RNVFLEIRAG
TGGDEAAIFS GDLFRMYSRY AERQGWRVEI LSENEGEYGG FKEVIARVEG DNVYAKLKFE
SGAHRVQRVP ETESQGRIHT SACTVAVLPE PDEQAAIEIN PADLRVDTYR SSGAGGQHVN
KTDSAVRITH IPSGIVVECQ EERSQHKNRA KAMSWLAAKL NDQQQAAAQQ AIASTRKLLV
GSGDRSERIR TYNFPQGRVT DHRINLTLYS LGEVMEGSVE QVIEPLLQEY QADQLAALGD
//
