ID A0A2W7ICN1_9PROT Unreviewed; 351 AA.
AC A0A2W7ICN1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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=C8P66_1145 {ECO:0000313|EMBL:PZW44716.1};
OS Humitalea rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Humitalea.
OX NCBI_TaxID=990373 {ECO:0000313|EMBL:PZW44716.1, ECO:0000313|Proteomes:UP000249688};
RN [1] {ECO:0000313|EMBL:PZW44716.1, ECO:0000313|Proteomes:UP000249688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24525 {ECO:0000313|EMBL:PZW44716.1,
RC ECO:0000313|Proteomes:UP000249688};
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 (JUN-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:PZW44716.1}.
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DR EMBL; QKYU01000014; PZW44716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W7ICN1; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000249688; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000249688}.
FT DOMAIN 221..237
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 228
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 351 AA; 38870 MW; DB5D6ECDDC21DF7E CRC64;
MSLADKLDVL VSRAEELRAS LETADGARVG TLSKELSDLE PLVARVNALR AAEQARDEAR
AMLDDPEMRE LAEADLADIE KTLPALEREV RLMLLPRDLA DERNAILEIR PAAGGDEAGL
FAAELFGAYR RYAENRRWTF EVLEYDETEL GGLKGGTAEI GGKGVFAKLK FESGVHRVQR
VPSTETQGRI HTSTVTVAVL PEAEEVDVQI NDNDLRIDTY RASGAGGQHV NKTDSAVRIT
HLPTGIVVAM QEERSQHKNR AKAMKILRAR MFEQQRSRLA DTRAADRRGQ IGTGDRSERI
RTYNFPQGRV TDHRIGLTLH KIDRVMLGEL DEIIDALTAE DEAARLAAEG V
//
