ID A0A3D8I161_9HELI Unreviewed; 352 AA.
AC A0A3D8I161;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:RDU58464.1};
GN ORFNames=CQA42_01350 {ECO:0000313|EMBL:RDU58464.1};
OS Helicobacter sp. MIT 99-5507.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=152489 {ECO:0000313|EMBL:RDU58464.1, ECO:0000313|Proteomes:UP000256421};
RN [1] {ECO:0000313|EMBL:RDU58464.1, ECO:0000313|Proteomes:UP000256421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 99-5507 {ECO:0000313|EMBL:RDU58464.1,
RC ECO:0000313|Proteomes:UP000256421};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-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:RDU58464.1}.
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DR EMBL; NXLO01000001; RDU58464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8I161; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000256421; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000256421}.
FT DOMAIN 224..240
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 284..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..92
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 352 AA; 39758 MW; 078C6BC85A838A14 CRC64;
MIVDKLLPLI ERYDNINQEL IKPEVLSNVK LLSKLTKEQS DLSSLVEKAK EYLAVLKSLE
DNKELLDDKE LGDLVKEEIK ILESKKVDLE EEIKLLLIPK DPNSNKNVYL EIRAGTGGDE
AGIFVGDLFK AYCRYAESKR WKVEIISSSE NNVGGYKEVI ALIKGDSVYS RLKYEGGTHR
VQRVPDTESQ GRIHTSAVTV AIMPEVEDIE ININPNDLQI DVFRSGGHGG QSVNTTDSAV
RITHIPTGIS VSMQDEKSQH KNKDKALKIL KARIYEKELE EKMQLESQNR KEQVGSGDRS
ERIRTYNYPQ NRLSDHRAGI TLYSLEEIML SGNLDLVINP LLAHMQSLSV QE
//
