ID A0A2T5JCX0_9SPHI Unreviewed; 357 AA.
AC A0A2T5JCX0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=C8P68_102431 {ECO:0000313|EMBL:PTQ99604.1};
OS Mucilaginibacter yixingensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1295612 {ECO:0000313|EMBL:PTQ99604.1, ECO:0000313|Proteomes:UP000244168};
RN [1] {ECO:0000313|EMBL:PTQ99604.1, ECO:0000313|Proteomes:UP000244168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26809 {ECO:0000313|EMBL:PTQ99604.1,
RC ECO:0000313|Proteomes:UP000244168};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTQ99604.1}.
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DR EMBL; QAOQ01000002; PTQ99604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5JCX0; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000244168; 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:UP000244168}.
FT DOMAIN 63..177
FT /note="Peptide chain release factor"
FT /evidence="ECO:0000259|SMART:SM00937"
FT MOD_RES 233
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 357 AA; 40817 MW; E0ABCF80283C087F CRC64;
MLDKLELIYE RWKTVEGELS SPEAMADMKR FAQLNREYKD LGKIVDEYLV YRNIMSNIDS
SKAILATEKD EEFREMAKME LDELLTQQEE KEEQIRVMLI PKDPEDSKNA IVEIRGGTGG
DEAALFAGDL YRMYMRYCEK RGWRTELVDY TEGTSGGYKE IVFNVLAEDA YGTLKYESGV
HRVQRVPDTE TQGRVHTSAA SVVVLPEVDE FDIDLQVSDI RKDLFCASGP GGQSVNTTYS
AVRLTHIPTG IVAQCQDQKS QLKNYDKALQ VLRSRVYEME LQKHMEEVSK KRKTMVSTGD
RSAKVRTYNY PQGRVTEHRI GLTIYNLPNV MNGDLQEIME QLQFAENAEK LKEGTIA
//
