ID A0A3L7DW89_9GAMM Unreviewed; 361 AA.
AC A0A3L7DW89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ECO:0000313|EMBL:RLQ21396.1};
GN ORFNames=DWB85_12785 {ECO:0000313|EMBL:RLQ21396.1};
OS Seongchinamella sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Seongchinamella.
OX NCBI_TaxID=2283635 {ECO:0000313|EMBL:RLQ21396.1, ECO:0000313|Proteomes:UP000265509};
RN [1] {ECO:0000313|EMBL:RLQ21396.1, ECO:0000313|Proteomes:UP000265509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0301 {ECO:0000313|EMBL:RLQ21396.1,
RC ECO:0000313|Proteomes:UP000265509};
RA Ye M.-Q., Du Z.-J.;
RT "Halioglobus sp. genome submission.";
RL Submitted (JUL-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:RLQ21396.1}.
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DR EMBL; QRAN01000013; RLQ21396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7DW89; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000265509; 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.
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}.
FT DOMAIN 230..246
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 361 AA; 40397 MW; A142DF232A53C5D5 CRC64;
MKASLLTKLE TLTDRHEEVS ALLGDSETIA DQDRFRDLSR EYAELEAVVK CYAGYSQVKA
DLEEARLMLE DADPDLRDMA REEIESGTER LAVLETELQT LLLPRDPNDS HNVFLEIRAG
TGGDEAAIFS GDLFRMYSRY AENMGWKVEV LSERPGEHGG FKEIITRVEG RDVYAHLKFE
SGAHRVQRVP ETESQGRIHT SACTVAIMPE AEAVDEIEIN KADLRIDTYR ASGAGGQHVN
KTDSAVRITH LPSGIVVECQ DERSQHKNRA RAMSLLQAKL LTSAQDKVAE EQAEQRRNLV
GTGDRSDRIR TYNFPQGRLT DHRINLTLYK LGEVMEGDLG AVVEPLRQEY QADQLAALGE
G
//
