ID A0A1W7M9H5_9SPHN Unreviewed; 356 AA.
AC A0A1W7M9H5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-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=NMD1_01540 {ECO:0000313|EMBL:GAO54443.1};
OS Novosphingobium sp. MD-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1630648 {ECO:0000313|EMBL:GAO54443.1, ECO:0000313|Proteomes:UP000266860};
RN [1] {ECO:0000313|EMBL:GAO54443.1, ECO:0000313|Proteomes:UP000266860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-1 {ECO:0000313|EMBL:GAO54443.1,
RC ECO:0000313|Proteomes:UP000266860};
RA Okano K.;
RT "Draft Genome Sequence of the microcystin-degrading bacterium
RT Novosphingobium sp. MD-1.";
RL Submitted (APR-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 -!- 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:GAO54443.1}.
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DR EMBL; BBXA01000022; GAO54443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7M9H5; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000266860; 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:UP000266860}.
FT DOMAIN 225..241
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT MOD_RES 232
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 356 AA; 38425 MW; B4FD84BB0A964E5C CRC64;
MSISDTRLAQ IGARFAELEA RLASGTLEGA EFIAASRDYA ELEPVARAAA AVGAMRGELA
SLSALDEPDP DMRALAEEEM ARLSADLPEA EHRLAVAMLP RDTADSRPAM LEIRAGTGGD
EAALFAADLF RMYEKYAAEQ GWRVEVVSVN ANDLGGYKEV VANVTGSGVF AKLKFESGVH
RVQRVPVTES GGRIHTSAAT VAVLPEPDEV DIRIEDKDLK IDVYRASGAG GQHVNTTDSA
VRITHLPTGT VVTCQDGRSQ HKNKDKAMQV LRARLFEAQR EAAQGEEAEA RKAMVGSGDR
SERIRTYNFP QGRVTDHRIN LTLHRLPEIL EGPGLGELID ALTAEDQAKR LAAMDA
//
