RF1_THEMA
ID RF1_THEMA Reviewed; 342 AA.
AC Q9X183;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Peptide chain release factor 1;
DE Short=RF-1;
GN Name=prfA; OrderedLocusNames=TM_1363;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36433.1; -; Genomic_DNA.
DR PIR; D72263; D72263.
DR RefSeq; NP_229164.1; NC_000853.1.
DR PDB; 1RQ0; X-ray; 2.65 A; A/B/C=1-342.
DR PDB; 2FVO; EM; 12.80 A; A=1-333.
DR PDBsum; 1RQ0; -.
DR PDBsum; 2FVO; -.
DR AlphaFoldDB; Q9X183; -.
DR SMR; Q9X183; -.
DR STRING; 243274.THEMA_07525; -.
DR EnsemblBacteria; AAD36433; AAD36433; TM_1363.
DR KEGG; tma:TM1363; -.
DR eggNOG; COG0216; Bacteria.
DR InParanoid; Q9X183; -.
DR OMA; ISDHRVG; -.
DR OrthoDB; 928964at2; -.
DR EvolutionaryTrace; Q9X183; -.
DR Proteomes; UP000008183; 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;
KW Reference proteome.
FT CHAIN 1..342
FT /note="Peptide chain release factor 1"
FT /id="PRO_0000177761"
FT REGION 262..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT TURN 2..6
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 19..49
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 50..57
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 62..80
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 99..119
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 174..184
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 239..263
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:1RQ0"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:1RQ0"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1RQ0"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:1RQ0"
SQ SEQUENCE 342 AA; 39657 MW; BEA59866A68F12F3 CRC64;
MKEKKKEIEK LLARPDLTPE QMKNYGMEYA KIEEIENITN RIKETQEFIE LLREEGENEL
EIEKYEKELD QLYQELLFLL SPEASDKAIV EIRPGTGGEE AALFARDLFR MYTRYAERKG
WNLEVAEIHE TDLGGIREVV FFVKGKNAYG ILKYESGVHR VQRVPVTESG GRIHTSTATV
AVLPEIEEKD IEIRPEDLKI ETFRASGHGG QYVNKTESAV RITHLPTGIV VSCQNERSQY
QNKQTALRIL RARLYQLQKE QKEREISQKR KSQIGTGERS EKIRTYNFPQ NRVTDHRINY
TSYRLQEILD GDLDEIISKL IEHDIENNLE EVLGIGASVE EK
