ID A0A0G3XLA8_9SPHN Unreviewed; 355 AA.
AC A0A0G3XLA8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AB433_00210 {ECO:0000313|EMBL:AKM11389.1};
OS Croceicoccus naphthovorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM11389.1, ECO:0000313|Proteomes:UP000035287};
RN [1] {ECO:0000313|EMBL:AKM11389.1, ECO:0000313|Proteomes:UP000035287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PQ-2 {ECO:0000313|EMBL:AKM11389.1,
RC ECO:0000313|Proteomes:UP000035287};
RA Zeng Y., Huang Y.;
RL Submitted (JUN-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011770; AKM11389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3XLA8; -.
DR STRING; 1348774.AB433_00210; -.
DR KEGG; cna:AB433_00210; -.
DR PATRIC; fig|1348774.3.peg.50; -.
DR Proteomes; UP000035287; 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; -; 2.
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:UP000035287}.
FT DOMAIN 222..238
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 229
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 355 AA; 38452 MW; A3EAF72F42393A4E CRC64;
MSDERLAQIA QRFSELEARL ASGTLEGDAF IQASRDYAEL ERVAREAADV AAMRAELAGL
QEMLADPEMK AMAAEDIARI EADLPDAEQR LAIALLPRDS ADARPAMLEI RAGTGGDEAA
LFAADLFRMY ERFAAEQGWK VETISVNASD IGGFKEVVAN VSGTGVFAKL KFESGVHRVQ
RVPVTESGGR IHTSAATVAV LPEPDEVDVQ IADNDLKIDI YRASGAGGQH VNTTDSAVRI
THLPSGIVVT QQDERSQHKN KAKAMQVLRA RLYEKMRDEA HGAEAEARKA MVGSGDRSER
IRTYNFPQGR VTDHRIGLTL HKLPEILEGT GLGELVDALI SEDQAARLAA QNEAA
//
