ID A0A1I3R9J0_9FLAO Unreviewed; 357 AA.
AC A0A1I3R9J0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN04487893_10780 {ECO:0000313|EMBL:SFJ42329.1};
OS Myroides guanonis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=1150112 {ECO:0000313|EMBL:SFJ42329.1, ECO:0000313|Proteomes:UP000243887};
RN [1] {ECO:0000313|Proteomes:UP000243887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26542 {ECO:0000313|Proteomes:UP000243887};
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; FORU01000007; SFJ42329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3R9J0; -.
DR STRING; 1150112.SAMN04487893_10780; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000243887; 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.
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:UP000243887}.
FT DOMAIN 63..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT REGION 284..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40328 MW; 9222499D992C6AD5 CRC64;
MLDRLQIIKQ RFDEISDLII QPDVIADQKR YVQLNKEYKD LKQLVEKRDE YISLKGNIQE
ANEIIADGSD AEMVEMAALQ LSEAKSRLPQ LEEEIKFLLI PKDPEDAKNV MVEIRAGTGG
DEASIFAGDL YRMYTKYCES RGWRTSLVDA NEGTSGGFKE VIFEVTGDDV YGTLKFEAGV
HRVQRVPQTE TQGRVHTSAA TVMVLPEAEE FDVQIDMNDV RIDYFCSSGP GGQSVNTTKS
AVRMTHTPTG LVAQCQDEKS QHKNKDKALT VLRSRLYEME LAKKQEEDAK KRNSQVSSGD
RSAKIRTYNY PQGRVTDHRI GLTLYDLDGV MNGNIQKVIE ELQLVSNTEK LQESDVF
//
