ID E6VWK1_PSEA9 Unreviewed; 391 AA.
AC E6VWK1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=Daes_1488 {ECO:0000313|EMBL:ADU62502.1};
OS Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS (Desulfovibrio aespoeensis).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU62502.1, ECO:0000313|Proteomes:UP000002191};
RN [1] {ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA Hazen T., Woyke T.;
RT "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU62502.1, ECO:0000313|Proteomes:UP000002191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC {ECO:0000313|Proteomes:UP000002191};
RX PubMed=24874683;
RA Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA Goodwin L., Shapiro N.;
RT "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL Genome Announc. 2:e00509-14(2014).
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; CP002431; ADU62502.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VWK1; -.
DR STRING; 643562.Daes_1488; -.
DR KEGG; das:Daes_1488; -.
DR eggNOG; COG1186; Bacteria.
DR HOGENOM; CLU_036856_6_0_7; -.
DR Proteomes; UP000002191; 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 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 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}.
FT DOMAIN 264..280
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 271
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 391 AA; 43980 MW; FFEF0226B7A16316 CRC64;
MLRLGRPAHK KQRERIVFPC SNTTNSKPFP QDSSTSSGRF GGGFDYAETK TRLEAIEHQL
SKPGAWDKPG ALTPLLREKT QLSDKLAMYE SLAQAKDDLD AWLELAHESR DEEAMAGLDG
QISVFKERLG ITELATMFAF EHDKGNAILE IHPGAGGVES QDWAEMLLRM YTRFAERKGF
KITQLDYQVG EEAGIKSVTL QIEGLYSYGL LKGESGVHRL IRISPFDSSG RRHTSFASVD
VYPDMDDDIE IEVRDEDLRI DVFRSSGPGG QSVNKTSSAV RITHLPTGIV AQCQNEKSQH
RNKATALRLV KARLYERELQ KIEESRRQDY QAKGAIAWGS QIRTYTLQPY RLVKDHRSNS
ETGNVDAFLD GDLDAMIRNH LLFVHAQGKH D
//
