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PELO_AERPE
ID   PELO_AERPE              Reviewed;         356 AA.
AC   Q9YAZ5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Protein pelota homolog {ECO:0000255|HAMAP-Rule:MF_01853};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01853};
GN   Name=pelA {ECO:0000255|HAMAP-Rule:MF_01853}; OrderedLocusNames=APE_1800.1;
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: May function in recognizing stalled ribosomes, interact with
CC       stem-loop structures in stalled mRNA molecules, and effect
CC       endonucleolytic cleavage of the mRNA. May play a role in the release
CC       non-functional ribosomes and degradation of damaged mRNAs. Has
CC       endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01853};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC   -!- INTERACTION:
CC       Q9YAZ5; Q9YAV0: tuf; NbExp=3; IntAct=EBI-15880754, EBI-15880729;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01853}.
CC   -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC       the endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01853}.
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DR   EMBL; BA000002; BAA80803.2; -; Genomic_DNA.
DR   PIR; F72564; F72564.
DR   PDB; 3WXM; X-ray; 2.30 A; B/D/F/H=1-356.
DR   PDB; 6JI2; X-ray; 3.00 A; B/F=1-356.
DR   PDBsum; 3WXM; -.
DR   PDBsum; 6JI2; -.
DR   AlphaFoldDB; Q9YAZ5; -.
DR   SMR; Q9YAZ5; -.
DR   DIP; DIP-59400N; -.
DR   IntAct; Q9YAZ5; 1.
DR   STRING; 272557.APE_1800.1; -.
DR   EnsemblBacteria; BAA80803; BAA80803; APE_1800.1.
DR   KEGG; ape:APE_1800.1; -.
DR   eggNOG; arCOG01741; Archaea.
DR   OMA; DDLWHLK; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:InterPro.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR   GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR   Gene3D; 2.30.30.870; -; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.420.60; -; 1.
DR   HAMAP; MF_01853; PelO; 1.
DR   InterPro; IPR042226; eFR1_2_sf.
DR   InterPro; IPR005140; eRF1_1_Pelota.
DR   InterPro; IPR005142; eRF1_3.
DR   InterPro; IPR029064; L30e-like.
DR   InterPro; IPR038069; Pelota/DOM34_N.
DR   InterPro; IPR023521; Pelota_arc.
DR   InterPro; IPR004405; Transl-rel_pelota.
DR   PANTHER; PTHR10853; PTHR10853; 1.
DR   Pfam; PF03463; eRF1_1; 1.
DR   Pfam; PF03465; eRF1_3; 1.
DR   SMART; SM01194; eRF1_1; 1.
DR   SUPFAM; SSF159065; SSF159065; 1.
DR   SUPFAM; SSF55315; SSF55315; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..356
FT                   /note="Protein pelota homolog"
FT                   /id="PRO_0000361779"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           20..29
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          52..67
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          73..82
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          92..99
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          136..145
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          148..156
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           167..189
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          192..199
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           202..213
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           228..235
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           239..244
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           249..266
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          271..274
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           275..284
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          287..293
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           294..298
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           302..317
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          321..325
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           330..335
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           336..338
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   STRAND          341..347
FT                   /evidence="ECO:0007829|PDB:3WXM"
FT   HELIX           351..353
FT                   /evidence="ECO:0007829|PDB:3WXM"
SQ   SEQUENCE   356 AA;  39238 MW;  389A5D27B7752986 CRC64;
     MRVEVLDNKR RIVRLRPESE EDLWLLRITL RPGDVVRIRT SRDVPVGSGR KERVVMTLRI
     RLDSIEFQPF TGKLRISGIV VEGPDEFGVK GRRHSTAVSI GTWLVVERDK GWSEQELERL
     ASGRARGTAV IAAVDYDEFA LAVLAGHGMK ILEDTSARLP GKDDPSREQE VEKYVDRAAK
     RIVEEAARHR SPIAVIAGPG QLKTSVAEKV QRAMPSLKVA TVDTSMGGVA GVREALRRES
     VTRILRELSI VEAEGVLEEF LRRIAKSRDT VAYTPGEVLA VARMGAVDTV LLVDTLLHSP
     DDAVREAVDE ALRLVESMGG RVIIIPGDSP AGERLVSFGG VIALLRYPVP QEARRL
 
 
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