ID A0A0U5BDP4_9MICO Unreviewed; 362 AA.
AC A0A0U5BDP4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=MalAC0309_1857 {ECO:0000313|EMBL:BAU32705.1};
OS Microcella alkaliphila.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microcella.
OX NCBI_TaxID=279828 {ECO:0000313|EMBL:BAU32705.1, ECO:0000313|Proteomes:UP000218965};
RN [1] {ECO:0000313|Proteomes:UP000218965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM AC0309 {ECO:0000313|Proteomes:UP000218965};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAU32705.1, ECO:0000313|Proteomes:UP000218965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM AC0309 {ECO:0000313|EMBL:BAU32705.1,
RC ECO:0000313|Proteomes:UP000218965};
RA Kurata A., Hirose Y., Kishimoto N., Kobayashi T.;
RT "Microcella alkaliphila JAM AC0309 whole genome shotgun sequence.";
RL Submitted (JAN-2016) 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}.
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DR EMBL; AP017315; BAU32705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5BDP4; -.
DR KEGG; malk:MalAC0309_1857; -.
DR Proteomes; UP000218965; Chromosome.
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}.
FT DOMAIN 230..246
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 259..301
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 237
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00093"
SQ SEQUENCE 362 AA; 39885 MW; 12054DC61855382D CRC64;
MTHVFDSVEA LIAEHAELQE QLADPAVHAD PARSKKLNRR YAELNQIVHA HDVWQQAGDD
LAAARELAKD DEAFADEVPA LEEALAEAQE KLRRLLIPRD PDDGRDVIME IKGGEGGEES
ALFAADLLRM YSYYAESRGW KVELLDSTTS DLGGYKNVQV AIKSTSSDPA DGVWASLKYE
GGVHRVQRVP ATESQGRIHT STTGVLVFPE VDEPEEVDIN QNDLKIDVYR SSGPGGQSVN
TTDSAVRITH LPTGIVVAMQ NEKSQLQNRE AAMRVLRARI LAKQQEEIAA AQSDARKSQI
RGMDRSERIR TYNFPENRIA DHRTGYKAYN LDAVMNGALG PVVEACIQAD EEARLAALGD
ET
//
