PELO_ARCFU
ID PELO_ARCFU Reviewed; 344 AA.
AC O29421;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=AF_0837;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000782; AAB90402.1; -; Genomic_DNA.
DR PIR; E69354; E69354.
DR RefSeq; WP_010878340.1; NC_000917.1.
DR PDB; 3OBY; X-ray; 2.90 A; A/B=1-344.
DR PDBsum; 3OBY; -.
DR AlphaFoldDB; O29421; -.
DR SMR; O29421; -.
DR STRING; 224325.AF_0837; -.
DR PRIDE; O29421; -.
DR DNASU; 1484056; -.
DR EnsemblBacteria; AAB90402; AAB90402; AF_0837.
DR GeneID; 1484056; -.
DR KEGG; afu:AF_0837; -.
DR eggNOG; arCOG01741; Archaea.
DR HOGENOM; CLU_023334_0_0_2; -.
DR OMA; DDLWHLK; -.
DR OrthoDB; 90096at2157; -.
DR PhylomeDB; O29421; -.
DR Proteomes; UP000002199; 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; IPR005141; eRF1_2.
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; PF03464; eRF1_2; 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_0000361780"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 22..31
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 236..262
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:3OBY"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:3OBY"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3OBY"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:3OBY"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:3OBY"
SQ SEQUENCE 344 AA; 39145 MW; 68E794B889E372BB CRC64;
MQIVEENLRD NEGEIKLIPE TLDDLWHLRF IIEKGDVVFA TTKRASQSSD KLRSDKEMVT
VRLGIEVEKV EFHRFANRLR VSGKIVAGIE ESGYHTLNIT VGKELSIIKK WKPEQLERLR
RAVEDSNRPE IVMLTIEEGY AVAGVLRQWG VEEIFEERMG YGKGMGDSRK EFFGEVAAKL
ESFDFKYLIV AGPGFAKNDF LDFLKERYPE MAKNAVVVDV SSVGSRGFIE ILKRRVVDKI
VGEVRLAEEA EYIDRLLEGI AKGERVAYGL DEVREAHNYR AIEVLLVADE FLLEEREKWD
VDGLLREVEE SGGKVVIMST EFEPGKRLMS LGGIAALLRF NVKG
