ID A0A1X4ND13_9RHOB Unreviewed; 349 AA.
AC A0A1X4ND13;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, 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 ORFNames=MGEO_18720 {ECO:0000313|EMBL:OSQ44654.1};
OS Marivita geojedonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Marivita.
OX NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ44654.1, ECO:0000313|Proteomes:UP000193926};
RN [1] {ECO:0000313|EMBL:OSQ44654.1, ECO:0000313|Proteomes:UP000193926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ44654.1,
RC ECO:0000313|Proteomes:UP000193926};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL Submitted (MAR-2014) 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:OSQ44654.1}.
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DR EMBL; JFKC01000029; OSQ44654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4ND13; -.
DR STRING; 1123756.MGEO_18720; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000193926; 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:UP000193926}.
FT DOMAIN 220..236
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 276..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 349 AA; 38719 MW; 4D55AC01FC6BC876 CRC64;
MIPEDRLHQI TSRFEYLEAQ MAEGSGDIAA IGKEYSDLRP VVDQITEWKQ VRADIAEAEA
MLDDPEMREL AQEELPALKA RLPEVEHALQ LALLPKDKAD ARPAMLEIRP GTGGEEAALF
AGDLLRMYQR YSEARGWRFE IIEEQATELG GIKEVVAHIT GDNVFARLKF ESGVHRVQRV
PETESGGRIH TSAATVAVLP EAEDVDIQIN ANDLRIDTMR SSGAGGQHVN TTDSAVRITH
IPSGIVVTSS EKSQHRNREI AMQVLRTRLF DMERQKVDAE RSANRKSQVG SGDRSERIRT
YNFPQGRLTD HRIGLTLYKL DAVMAGDLDE IIDALTADAQ ATLLAEMGA
//
