ID   RF2_MAGSA               Reviewed;         371 AA.
AC   Q2W3F8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Peptide chain release factor 2 {ECO:0000255|HAMAP-Rule:MF_00094};
DE            Short=RF-2 {ECO:0000255|HAMAP-Rule:MF_00094};
GN   Name=prfB {ECO:0000255|HAMAP-Rule:MF_00094}; OrderedLocusNames=amb2813;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
CC   -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC       translation in response to the peptide chain termination codons UGA and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF2. {ECO:0000255|HAMAP-Rule:MF_00094}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00094}.
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DR   EMBL; AP007255; BAE51617.1; -; Genomic_DNA.
DR   RefSeq; WP_011385191.1; NC_007626.1.
DR   AlphaFoldDB; Q2W3F8; -.
DR   SMR; Q2W3F8; -.
DR   STRING; 342108.amb2813; -.
DR   EnsemblBacteria; BAE51617; BAE51617; amb2813.
DR   KEGG; mag:amb2813; -.
DR   HOGENOM; CLU_036856_6_0_5; -.
DR   OMA; YVFHPYQ; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000007058; 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_00094; Rel_fac_2; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004374; PrfB.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00020; prfB; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..371
FT                   /note="Peptide chain release factor 2"
FT                   /id="PRO_1000004997"
FT   MOD_RES         250
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ   SEQUENCE   371 AA;  41729 MW;  9CD03A9C12FEC253 CRC64;
     MRAEIEALAQ DIRRSAALLK RHLNWDEALM RLDELNASAE NPDLWNDAGA AQKIMRERNE
     LDSAIQGCRA LERELADLAE LIELGEMEGD QTVIDDAEEQ VRALKERAAK MELETLLSGE
     ADHNDCYMEI NAGAGGTESQ DWAEMLLRMY TRWAEKHGYK VEWLEESAGE QAGIKSATIR
     ILGHNAYGWL KTESGVHRLV RISPYDSAAR RHTSFSSAWV YPVIDDTIDI QINESECRID
     TYRASGAGGQ HINKTDSAVR ITHIPTGIAV ACQMERSQHQ NRARAWDMLR ARLYEAELQK
     REAAAQALED QKTDIGWGHQ IRSYVLQPYQ MVKDLRTNVE TSDTQGVLDG DLDMFMAASL
     AARVQGQVDQ G