ID   PEL2_ARATH              Reviewed;         395 AA.
AC   Q9M2H7;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Protein PELOTA 2;
DE            Short=AtPelota2;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN   Name=PEL2; OrderedLocusNames=At3g58390; ORFNames=F9D24.300;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   AGRICOLA=IND22059670; DOI=10.1007/s004970050200;
RA   Caryl A.P., Lacroix I., Jones G.H., Franklin F.C.H.;
RT   "An Arabidopsis homologue of the Drosophila meiotic gene Pelota.";
RL   Sex. Plant Reprod. 12:310-313(2000).
CC   -!- FUNCTION: Required for normal chromosome segregation during cell
CC       division and genomic stability (By similarity). May function in
CC       recognizing stalled ribosomes and triggering endonucleolytic cleavage
CC       of the mRNA, a mechanism to release non-functional ribosomes and
CC       degrade damaged mRNAs. May have ribonuclease activity (Potential).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P33309};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC       the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL137081; CAB68177.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79776.1; -; Genomic_DNA.
DR   PIR; T45999; T45999.
DR   RefSeq; NP_191398.1; NM_115701.2.
DR   AlphaFoldDB; Q9M2H7; -.
DR   SMR; Q9M2H7; -.
DR   STRING; 3702.AT3G58390.1; -.
DR   iPTMnet; Q9M2H7; -.
DR   PaxDb; Q9M2H7; -.
DR   PRIDE; Q9M2H7; -.
DR   ProteomicsDB; 236680; -.
DR   EnsemblPlants; AT3G58390.1; AT3G58390.1; AT3G58390.
DR   GeneID; 825008; -.
DR   Gramene; AT3G58390.1; AT3G58390.1; AT3G58390.
DR   KEGG; ath:AT3G58390; -.
DR   Araport; AT3G58390; -.
DR   TAIR; locus:2085465; AT3G58390.
DR   eggNOG; KOG2869; Eukaryota.
DR   HOGENOM; CLU_023334_3_1_1; -.
DR   InParanoid; Q9M2H7; -.
DR   OMA; ACYGPKQ; -.
DR   OrthoDB; 953123at2759; -.
DR   PhylomeDB; Q9M2H7; -.
DR   PRO; PR:Q9M2H7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M2H7; baseline and differential.
DR   Genevisible; Q9M2H7; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR   GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEP:TAIR.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEP:TAIR.
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   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; 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   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..395
FT                   /note="Protein PELOTA 2"
FT                   /id="PRO_0000429931"
SQ   SEQUENCE   395 AA;  44721 MW;  F54433750E746423 CRC64;
     MKIIRKDFVR NGPGSVKMMA EDSDDLWYTY NLIGPEDSVM AITFRKVGGE GRDSTPSLSR
     IESKYLGKKR SFTRTERVKL KLEVQVEEVD YDKDGDVMRI RGKNIMENEH VRIGAFHTLE
     IELKRPFLLR KENWDSLALD TLKQASDLAA SADLAVVLMQ EGLAQIFLAG KSVKSCGARI
     KTSIPWKHGA GTAGYESVLK KFFENVVQAF LKHVDFSVVR CAVIASPGFT KDQFHRHLLL
     EAERRQLRPI LENKSRFILV HTNSGYKHSL SEVLHDPNVM NMIKDTKAAK EVKALNDFFT
     MFSNDPNRAC YGPKHVEVAH ERMAIQTLLI IDGLFRNSDV KTRKKYVDFV ESVKDSGGEV
     FIFSSMHASG EQLAQHTGIA AILRFPLPDL EDIEM