ID A0A2R3Z5Z7_9FLAO Unreviewed; 358 AA.
AC A0A2R3Z5Z7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=C7S20_10655 {ECO:0000313|EMBL:AVR45678.1};
OS Christiangramia fulva.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Christiangramia.
OX NCBI_TaxID=2126553 {ECO:0000313|EMBL:AVR45678.1, ECO:0000313|Proteomes:UP000241507};
RN [1] {ECO:0000313|Proteomes:UP000241507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH35 {ECO:0000313|Proteomes:UP000241507};
RA Hwang S.H., Hwang W.M., Kang K., Ahn T.-Y.;
RT "Gramella fulva sp. nov., isolated from a dry surface of tidal flat.";
RL Submitted (MAR-2018) 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; CP028136; AVR45678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R3Z5Z7; -.
DR KEGG; grs:C7S20_10655; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000241507; 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; 3.30.160.20; -; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000241507}.
FT DOMAIN 62..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT COILED 34..94
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 358 AA; 40908 MW; 51D0E956A33476B3 CRC64;
MIDKLNIVKQ RFDEVNDLII QPDVISDQKR YIELNKEYKD LKALMNEREK YMRLTDNIKE
AEEIIADGSD PEMTEMAKLQ LEEAKAQLPE LEEKIRMMLV PKDPEDAKNV VMEIRAGTGG
DEASIFAGDL YRMYTKYVES KGWKHNIVDF SEGTSGGFKE IIFEISGEEV YGTMKFEAGV
HRVQRVPQTE TQGRVHTSAA TVMVLPEAEE FDVEIDPKDV RIDYFCSSGP GGQSVNTTYS
AVRLTHEPTG LVAQCQDQKS QHKNKEKAFR VLRSRLYEME LAKKQEADAA KRNSMVSSGD
RSAKIRTYNY AQSRVTDHRI NLTLYDLSNI INGDIQKIID ELRFAENTEK LKENSDIL
//
