RF1_THET2
ID RF1_THET2 Reviewed; 354 AA.
AC Q72HB8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=TT_C1577;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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:0000255|HAMAP-Rule:MF_00093}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR EMBL; AE017221; AAS81919.1; -; Genomic_DNA.
DR RefSeq; WP_011173949.1; NC_005835.1.
DR PDB; 4V63; X-ray; 3.21 A; AX/CX=1-354.
DR PDB; 4V7P; X-ray; 3.62 A; AV/DV=1-354.
DR PDBsum; 4V63; -.
DR PDBsum; 4V7P; -.
DR AlphaFoldDB; Q72HB8; -.
DR SMR; Q72HB8; -.
DR IntAct; Q72HB8; 49.
DR STRING; 262724.TT_C1577; -.
DR PRIDE; Q72HB8; -.
DR EnsemblBacteria; AAS81919; AAS81919; TT_C1577.
DR GeneID; 3169506; -.
DR KEGG; tth:TT_C1577; -.
DR eggNOG; COG0216; Bacteria.
DR HOGENOM; CLU_036856_0_1_0; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR EvolutionaryTrace; Q72HB8; -.
DR Proteomes; UP000000592; 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 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 Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; SSF75620; 1.
DR TIGRFAMs; TIGR00019; prfA; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methylation; Protein biosynthesis.
FT CHAIN 1..354
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000263382"
FT MOD_RES 230
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
FT HELIX 2..8
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 28..62
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 68..96
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 117..138
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 258..292
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:4V63"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:4V63"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:4V63"
FT HELIX 333..351
FT /evidence="ECO:0007829|PDB:4V63"
SQ SEQUENCE 354 AA; 40093 MW; 49868D246BB3339E CRC64;
MLDKLDRLEE EYRELEALLS DPEVLKDKGR YQSLSRRYAE MGEVIGLIRE YRKVLEDLEQ
AESLLDDPEL KEMAKAEREA LLARKEALEK ELERHLLPKD PMDERDAIVE IRAGTGGEEA
ALFARDLFNM YLRFAEEMGF ETEVLDSHPT DLGGFSKVVF EVRGPGAYGT FKYESGVHRV
QRVPVTETQG RIHTSTATVA VLPKAEEEDF ALNMDEIRID VMRASGPGGQ GVNTTDSAVR
VVHLPTGIMV TCQDSRSQIK NREKALMILR SRLLEMKRAE EAERLRKTRL AQIGTGERSE
KIRTYNFPQS RVTDHRIGFT THDLEGVLSG HLTPILEALK RADQERQLAA LAEG
