RF1_HALS3
ID RF1_HALS3 Reviewed; 416 AA.
AC B0R748;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Peptide chain release factor subunit 1 {ECO:0000255|HAMAP-Rule:MF_00424};
DE AltName: Full=Translation termination factor aRF1 {ECO:0000255|HAMAP-Rule:MF_00424};
GN Name=prf1 {ECO:0000255|HAMAP-Rule:MF_00424}; OrderedLocusNames=OE_3973F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00424}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_00424}.
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DR EMBL; AM774415; CAP14567.1; -; Genomic_DNA.
DR RefSeq; WP_012289438.1; NC_010364.1.
DR PDB; 4AF1; X-ray; 2.00 A; A=1-416.
DR PDBsum; 4AF1; -.
DR AlphaFoldDB; B0R748; -.
DR SMR; B0R748; -.
DR EnsemblBacteria; CAP14567; CAP14567; OE_3973F.
DR GeneID; 5954067; -.
DR GeneID; 62885298; -.
DR KEGG; hsl:OE_3973F; -.
DR HOGENOM; CLU_035759_3_0_2; -.
DR OMA; GQEMEVV; -.
DR PhylomeDB; B0R748; -.
DR Proteomes; UP000001321; 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; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR Gene3D; 3.30.960.10; -; 1.
DR HAMAP; MF_00424; Rel_fact_arch_1; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR024049; eRF1_1_sf.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR020918; Peptide_chain-rel_aRF1.
DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR PANTHER; PTHR10113; PTHR10113; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF55481; SSF55481; 1.
DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Protein biosynthesis.
FT CHAIN 1..416
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_1000193543"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:4AF1"
FT TURN 136..142
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 193..215
FT /evidence="ECO:0007829|PDB:4AF1"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 222..230
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:4AF1"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 282..296
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 305..313
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:4AF1"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4AF1"
FT HELIX 394..401
FT /evidence="ECO:0007829|PDB:4AF1"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:4AF1"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:4AF1"
SQ SEQUENCE 416 AA; 46638 MW; DB239CB58F4ABE89 CRC64;
MSEQDEVPSE DRRKYEFRKV IEELKDYEGS GTQLVTIYIP PDKQISDVVA HVTQEHSEAS
NIKSKQTRTN VQDALTSIKD RLRYYDTFPP DNGMVVFSGA VDSGGGRTDM VTEVLESPPQ
PIESFRYHCD SAFLTEPLAE MLGDKGLYGL IVLDRRESNV GWLKGKRVQP VKSAESLVPG
KQRKGGQSAQ RFARLRLEAI DNFYQEVAGM ADDLFVPKRH EIDGILVGGP SPTKDEFLDG
DYLHHELQDK VLGKFDVSYT DESGLSDLVD AGQAALAEAD LMDDKSDMEE FFEELNGGKL
ATYGFEQTRR NLIMGSVDRL LVSEDLREDV VIYECPNDHE EYETIDRRNT SPEHTCSDCG
EEATEVDRED AIDHLMSIAD QRGTETHFIS TDFEKGEQLL TAFGGYAGIL RYSTGV
