ID A0A1R4KTH1_9SPHI Unreviewed; 324 AA.
AC A0A1R4KTH1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptide chain release factor 2 {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=FM107_15670 {ECO:0000313|EMBL:SJN47447.1};
OS Sphingobacterium sp. JB170.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1434842 {ECO:0000313|EMBL:SJN47447.1, ECO:0000313|Proteomes:UP000195951};
RN [1] {ECO:0000313|EMBL:SJN47447.1, ECO:0000313|Proteomes:UP000195951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB170 {ECO:0000313|EMBL:SJN47447.1,
RC ECO:0000313|Proteomes:UP000195951};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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|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; FUKU01000057; SJN47447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4KTH1; -.
DR Proteomes; UP000195951; 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}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000195951}.
FT DOMAIN 202..218
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 231..258
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 209
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 324 AA; 37047 MW; 8C93757C50CCEBF0 CRC64;
MQPDFWDDPK SAEKLLHEIQ NLKIWTDQFD RISSLVEDAE TMYEFVQSGD ATQQEAEEHY
QKALIEVEEL EFKNMLSAEE DQLDAILQIT AGAGGTESCD WASMLMRMYI MWGEKHGCKV
SEQDYQEGEV AGIKTVTLQI SGNFAYGYLK GENGVHRLVR ISPFDSNAKR HTSFASVYVY
PLVDDNIQIE VKDAEVEWDT FRSGGAGGQN VNKVETAVRL HHKPTGIIIK NQESRSQLQN
KENAMRLLKS QLYEIEMRKR REATAIIEGS KKKIEWGSQI RNYVLHPYKL IKDLRTSQET
SNTQAVLDGD LDEFLKSYLM EFGG
//
