ID A0A1G6GW44_9ACTN Unreviewed; 371 AA.
AC A0A1G6GW44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=GA0111570_105164 {ECO:0000313|EMBL:SDB86161.1};
OS Raineyella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Raineyella.
OX NCBI_TaxID=1577474 {ECO:0000313|EMBL:SDB86161.1, ECO:0000313|Proteomes:UP000199086};
RN [1] {ECO:0000313|EMBL:SDB86161.1, ECO:0000313|Proteomes:UP000199086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ-22 {ECO:0000313|EMBL:SDB86161.1,
RC ECO:0000313|Proteomes:UP000199086};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMYF01000005; SDB86161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6GW44; -.
DR STRING; 1577474.GA0111570_105164; -.
DR OrthoDB; 9806673at2; -.
DR Proteomes; UP000199086; 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:UP000199086}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 59..115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 371 AA; 41223 MW; 352442A7B7C38A7B CRC64;
MAAEDISETI TALDRALGQI ESVSDPAAMA TEIADLEQQV SAPDLWDDQE NAQRVTSRLS
FLQAELKRLT GLRQRLEDLQ VMVQLAEEEN DASVLEDAVQ EAASLRTTLD ALEVRTLLSG
EYDERDAVVT IRSEAGGVDA ADFAEMLMRM YLRWSERHGY PTEVYDISYA EEAGIKSATF
QVKAPYAYGT LSVEQGTHRL VRISPFDNQG RRQTSFAGVE VLPVVEETDH IDIPEQDIRV
DVFRSSGPGG QSVNTTDSAV RITHLPTGLV VSCQNEKSQI QNKAAALRVL QARLLEKARK
DREAEMNALK SDGGNSWGSQ MRSYVLHPYQ MVKDLRTDCE VGNPEAVFDG AIDEFVDAGI
RWRKQQELAA R
//
