RF2_SULSY
ID RF2_SULSY Reviewed; 369 AA.
AC B2V5M0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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};
GN OrderedLocusNames=SYO3AOP1_1356;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD66964.1; -; Genomic_DNA.
DR RefSeq; WP_012460023.1; NC_010730.1.
DR AlphaFoldDB; B2V5M0; -.
DR SMR; B2V5M0; -.
DR STRING; 436114.SYO3AOP1_1356; -.
DR EnsemblBacteria; ACD66964; ACD66964; SYO3AOP1_1356.
DR KEGG; sul:SYO3AOP1_1356; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_0; -.
DR OMA; YVFHPYQ; -.
DR OrthoDB; 928964at2; -.
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.
FT CHAIN 1..369
FT /note="Peptide chain release factor 2"
FT /id="PRO_1000093559"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 42608 MW; 5DC84C0A73BB5E01 CRC64;
MIVEEIKTKW EEIKEKWDNL KEILKPEKLE EEIKQLDDLM ADPNFWNDTK KAQEISSRRN
YLGEKLEEIL TVDKKVNNLL DYITLLEMEE DQELYNEVEK ELKEIEKEIS RLELGSLLSD
EMDSKNAILT VQAGSGGVEA CDWTEMLLRM YTRWAEKRGY QVELVDFQPD DVAGVKSATL
IIKGPYAYGY LKGEQGVHRL VRISPFDANK RRHTSFSAVS VIPEIDEDIK VEINEEDLRI
DTYRASGAGG QHVNKTDSAV RITHIPTGIV VACQSERSQL QNKLKATNML KAKLYQLELE
KRKEKQKELE GEKKDITWGS QIRSYVFQPY QMVKDLRTGF ETGNIEAVMD GEIDDFIESY
LKWKAKGGQ