ID A0A1H0JPY8_9BACI Unreviewed; 327 AA.
AC A0A1H0JPY8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|ARBA:ARBA00019192, ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=SAMN04488053_11448 {ECO:0000313|EMBL:SDO45777.1};
OS Alkalicoccus daliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=745820 {ECO:0000313|EMBL:SDO45777.1, ECO:0000313|Proteomes:UP000198778};
RN [1] {ECO:0000313|Proteomes:UP000198778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10369 {ECO:0000313|Proteomes:UP000198778};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002613, ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
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DR EMBL; FNIL01000014; SDO45777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0JPY8; -.
DR STRING; 745820.SAMN04488053_11448; -.
DR Proteomes; UP000198778; Unassembled WGS sequence.
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; 1.20.58.410; Release factor; 1.
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 NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 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_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Reference proteome {ECO:0000313|Proteomes:UP000198778}.
FT DOMAIN 205..221
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 23..76
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 212
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 327 AA; 37211 MW; A3C2B2567D425A59 CRC64;
MADPSFWENQ NEAQEVIAEN NALKAITNEY RSIESQLENM DVSYELVKEE ADEDLRKELE
ENVTKVKKQL DKFELQLLLS GKHDANNAML ELHPGAGGTE SQDWASMLLR MYTRWAEAQN
YKVETLDYLP GDEAGVKSVT LKISGHNAYG FLKAEKGVHR LVRISPFDSS GRRHTSFASC
DIMPEIDDNF EVNLSPEDIR VDTFRASGAG GQHINTTDSA VRMTHIPTNT VVSCQAERSQ
IKNREQAMKM LRAKLYQQEL DRKRAEADEL RGEQTDIGWG SQIRSYVFHP YNMVKDHRTD
EETGNTQAVM DGEITPFIDA YLRSQIE
//
