PELO_SACS2
ID PELO_SACS2 Reviewed; 344 AA.
AC P96026; P95977;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 121.
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=SSO0083;
GN ORFNames=C04039;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8900058; DOI=10.1111/j.1574-6968.1996.tb08522.x;
RA Ragan M.A., Logsdon J.M. Jr., Sensen C.W., Charlebois R.L., Doolittle W.F.;
RT "An archaebacterial homolog of pelota, a meiotic cell division protein in
RT eukaryotes.";
RL FEMS Microbiol. Lett. 144:151-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA Ragan M.A., Charlebois R.L.;
RT "Organizational characteristics and information content of an archaeal
RT genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL Mol. Microbiol. 22:175-191(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 -!- 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; U67942; AAB49285.1; -; Genomic_DNA.
DR EMBL; Y08257; CAA69568.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40443.1; -; Genomic_DNA.
DR PIR; S75405; S75405.
DR RefSeq; WP_009988896.1; NC_002754.1.
DR PDB; 3OBW; X-ray; 2.60 A; A=1-344.
DR PDBsum; 3OBW; -.
DR AlphaFoldDB; P96026; -.
DR SMR; P96026; -.
DR STRING; 273057.SSO0083; -.
DR EnsemblBacteria; AAK40443; AAK40443; SSO0083.
DR GeneID; 44129044; -.
DR KEGG; sso:SSO0083; -.
DR PATRIC; fig|273057.12.peg.82; -.
DR eggNOG; arCOG01741; Archaea.
DR HOGENOM; CLU_023334_0_0_2; -.
DR InParanoid; P96026; -.
DR OMA; DDLWHLK; -.
DR PhylomeDB; P96026; -.
DR EvolutionaryTrace; P96026; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IBA:GO_Central.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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..344
FT /note="Protein pelota homolog"
FT /id="PRO_0000361823"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 52..67
FT /evidence="ECO:0007829|PDB:3OBW"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 165..184
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:3OBW"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 235..259
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:3OBW"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3OBW"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:3OBW"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3OBW"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:3OBW"
SQ SEQUENCE 344 AA; 39630 MW; C5A390FDF2271695 CRC64;
MRILEFDEKR QAVKLHIESE DDLWLLHLIL EKDDKVVAKT TRDVGLGKES RRIPMTIILK
VDYTEFQEFT NRLRIHGIIE DAPERFGIKG AHHTINLDIG DEIIIIKQQW NKYVLDRLKR
QANKRSRIII ALVDFDEYLI AIPFEQGIKI LSEKSLRPLN EEEGIIEQNA LEIATELAEY
VKQYDPDAIL LAGPGFFKEE VSKKVNAILK NKKIYIDSVS SATRAGLHEV LKRDIIDKIM
TDYEIAIGAK KMEKAMELLA KQPELVTYGL EQVKNAIEMG AVETVLVIED LLSSDEQERL
TIERMLEDIE NKRGEVILVP KESPIYFELK NLTGILAILR FRIN
