PELO_THEAC
ID PELO_THEAC Reviewed; 339 AA.
AC Q9HJ74;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein pelota homolog;
DE EC=3.1.-.-;
DE AltName: Full=Cell division protein pelota-related protein;
GN Name=pelA; OrderedLocusNames=Ta1098;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), COFACTOR, SUBUNIT, DOMAIN, FUNCTION,
RP AND MUTAGENESIS OF GLU-18; ASP-21; ASP-22 AND GLU-231.
RX PubMed=17889667; DOI=10.1016/j.molcel.2007.07.019;
RA Lee H.H., Kim Y.-S., Kim K.H., Heo I., Kim S.K., Kim O., Kim H.K.,
RA Yoon J.Y., Kim H.S., Kim do J., Lee S.J., Yoon H.J., Kim S.J., Lee B.G.,
RA Song H.K., Kim V.N., Park C.-M., Suh S.W.;
RT "Structural and functional insights into Dom34, a key component of no-go
RT mRNA decay.";
RL Mol. Cell 27:938-950(2007).
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:0000269|PubMed:17889667}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17889667};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17889667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000269|PubMed:17889667}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000305}.
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DR EMBL; AL445066; CAC12225.1; -; Genomic_DNA.
DR RefSeq; WP_010901508.1; NC_002578.1.
DR PDB; 2QI2; X-ray; 2.90 A; A=1-339.
DR PDBsum; 2QI2; -.
DR AlphaFoldDB; Q9HJ74; -.
DR SMR; Q9HJ74; -.
DR STRING; 273075.Ta1098; -.
DR EnsemblBacteria; CAC12225; CAC12225; CAC12225.
DR GeneID; 1456607; -.
DR KEGG; tac:Ta1098; -.
DR eggNOG; arCOG01741; Archaea.
DR HOGENOM; CLU_023334_0_0_2; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 90096at2157; -.
DR EvolutionaryTrace; Q9HJ74; -.
DR Proteomes; UP000001024; 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.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Protein pelota homolog"
FT /id="PRO_0000359869"
FT MUTAGEN 18
FT /note="E->A: Strongly reduced ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:17889667"
FT MUTAGEN 21
FT /note="D->A: No effect. Strongly reduced ribonuclease
FT activity; when associated with A-22."
FT /evidence="ECO:0000269|PubMed:17889667"
FT MUTAGEN 22
FT /note="D->A: No effect. Strongly reduced ribonuclease
FT activity; when associated with A-21."
FT /evidence="ECO:0000269|PubMed:17889667"
FT MUTAGEN 231
FT /note="E->A: Slightly reduced ribonuclease activity."
FT /evidence="ECO:0000269|PubMed:17889667"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2QI2"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 246..262
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:2QI2"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:2QI2"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:2QI2"
SQ SEQUENCE 339 AA; 38407 MW; 2FF6C17C668006CA CRC64;
MRILEEDLKN STYRIRIESL DDLWYLRNIL SEGDEVSAIT FRRVEESADV QRSRERERIP
ITIRLKVEKI EFQDFDNRLR ILGTVIEGPE DTKGKHQSIT VTVDSEISIT KEWDDQHIDL
LKEATDEKYV TVYTAVAMDE DEAQIFLIHP YGIQQVGTVY SGRSGKYAEG NYSEASYFDQ
IVNALKNYSN SIIILGPGFA RDRFARYCAQ RGVNVIGSFP ANRTDSGAVY EFITSADGAK
LLSNERIARD KEIVDEFLVA VKKDMGVYGR DQTESALQMG ALSDLIITDE MFRTEDGRRS
LSIAQTVGTR IHIVSVSNDP GQIVKKFGGF AGILRYRVQ
