RF1_AERPE
ID RF1_AERPE Reviewed; 373 AA.
AC Q9YAF1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Peptide chain release factor subunit 1;
DE AltName: Full=Translation termination factor aRF1;
GN Name=prf1; OrderedLocusNames=APE_1988.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9YAF1; Q9YAV0: tuf; NbExp=3; IntAct=EBI-15887661, EBI-15880729;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; BA000002; BAA80998.2; -; Genomic_DNA.
DR PIR; F72501; F72501.
DR PDB; 3AGK; X-ray; 2.10 A; A=1-373.
DR PDB; 3VMF; X-ray; 2.30 A; B=1-373.
DR PDBsum; 3AGK; -.
DR PDBsum; 3VMF; -.
DR AlphaFoldDB; Q9YAF1; -.
DR SMR; Q9YAF1; -.
DR DIP; DIP-59468N; -.
DR IntAct; Q9YAF1; 1.
DR STRING; 272557.APE_1988.1; -.
DR EnsemblBacteria; BAA80998; BAA80998; APE_1988.1.
DR KEGG; ape:APE_1988.1; -.
DR PATRIC; fig|272557.25.peg.1327; -.
DR eggNOG; arCOG01742; Archaea.
DR OMA; GQEMEVV; -.
DR EvolutionaryTrace; Q9YAF1; -.
DR Proteomes; UP000002518; 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; 2.
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; Reference proteome.
FT CHAIN 1..373
FT /note="Peptide chain release factor subunit 1"
FT /id="PRO_0000143168"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3AGK"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3VMF"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 188..215
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:3AGK"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:3AGK"
FT HELIX 352..359
FT /evidence="ECO:0007829|PDB:3AGK"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:3AGK"
SQ SEQUENCE 373 AA; 41950 MW; 6BFD39299E876477 CRC64;
MSQGRLEERL TISKRELARL LKELKKWSAP ATVLLSLYIP PGRPLSDVMT LLRQEYSITD
NIKLKRTRQA VKRALSAAMD RLQMLTSTPP NGLVLFCGED MSTGKFECFM FSPPEPIRVF
YYRTDKRFIT DFLEDMVEDN NAIGIIIVER DQATIGLLKG ARLEVLKELE GFVPGKHKMG
GQSQRRYERI IEQMVDEFFK KVGEEASNLL VPLAEKGVLK GVIVAGPGLA KQEFVEGNYL
DYRLKKILAP ELVDVAYQGL QGLKEAVMKA EKVVEAQMYR DAVNAMEEFK LHLAKGTGMI
VYGEKDVEAA LEMGAVKTLL IHESREDLEE WVEKAKSSGA QVIVVPESLA EAEWFLKTFG
GLAGILRFRI STV
