ID A0A1W1ZU01_9FLAO Unreviewed; 362 AA.
AC A0A1W1ZU01;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN06296427_103235 {ECO:0000313|EMBL:SMC51846.1};
OS Moheibacter sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Moheibacter.
OX NCBI_TaxID=1434700 {ECO:0000313|EMBL:SMC51846.1, ECO:0000313|Proteomes:UP000192393};
RN [1] {ECO:0000313|EMBL:SMC51846.1, ECO:0000313|Proteomes:UP000192393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12708 {ECO:0000313|EMBL:SMC51846.1,
RC ECO:0000313|Proteomes:UP000192393};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWXS01000003; SMC51846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1ZU01; -.
DR STRING; 1434700.SAMN06296427_103235; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000192393; 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; -; 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:UP000192393}.
FT DOMAIN 231..247
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 238
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 362 AA; 41085 MW; 2A7DB5E93891CC9C CRC64;
MADKGLLEKL RAIKQRFDEV ADLIIQPDII SDQARYAKLN KEYSDLKDLV DVQQHYESLL
NAITEADEII ADGSDPEMTE MAKEEKDEAI NKIPQVEEEI KFLLIPKDPE DEKNIIVELR
AGTGGDEAAI FVEDVFRMYS MYFKNRGWKF EILNTSEGSV KGYKELIMEV QGATVFGTMK
YESGVHRVQR VPETESQGRV HTSAITVAVL PEAEEVDVEI NPADLEYQTA RSSGAGGQNV
NKVETKVQLT HKPSGIVIVC QEARSQHQNR ERALQLLRTK LYEIEYEKKH AERSAQRKSL
VSTGDRSAKI RTYNYPQGRV TDHRINKSIY NLDNFMNGDI QEMIDSLKLA ENAEKLKGSD
DI
//
