Protein : Qrob_P0221430.2 Q. robur
Protein Identifier  ? Qrob_P0221430.2 Organism . Name  Quercus robur
Score  62.0 Score Type  egn
Protein Description  (M=1) PTHR10853 - PELOTA Gene Prediction Quality  validated
Protein length 

Sequence

Length: 153  
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0 Synonyms

3 GO Terms

Identifier Name Description
GO:0070481 nuclear-transcribed mRNA catabolic process, non-stop decay The chemical reactions and pathways resulting in the breakdown of the transcript body of a nuclear-transcribed mRNA that is lacking a stop codon.
GO:0070966 nuclear-transcribed mRNA catabolic process, no-go decay The chemical reactions and pathways resulting in the breakdown of the transcript body of a nuclear-transcribed mRNA with stalls in translation elongation.
GO:0071025 RNA surveillance The set of processes involved in identifying and degrading defective or aberrant RNAs.

25 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pper:PRUPE_ppa007181mg 1 87 + 87 Gaps:25 31.11 360 64.29 2e-37 hypothetical protein
blastp_kegg lcl|gmx:100800939 1 87 + 87 Gaps:44 34.56 379 58.02 4e-37 protein pelota-like
blastp_kegg lcl|pvu:PHAVU_007G119100g 1 87 + 87 Gaps:44 34.56 379 57.25 6e-36 hypothetical protein
blastp_kegg lcl|pxb:103938540 1 138 + 138 Gaps:51 48.81 379 45.41 1e-35 protein PELOTA 1-like
blastp_kegg lcl|cic:CICLE_v100136752m 1 138 + 138 Gaps:50 71.88 256 45.11 1e-35 hypothetical protein
blastp_kegg lcl|gmx:100793935 1 87 + 87 Gaps:44 34.56 379 55.73 2e-35 protein pelota-like
blastp_kegg lcl|pxb:103930379 1 138 + 138 Gaps:51 48.81 379 44.86 3e-35 protein PELOTA 1-like
blastp_kegg lcl|mdm:103451128 1 138 + 138 Gaps:51 48.56 381 44.32 7e-35 protein pelota
blastp_kegg lcl|cit:102617256 1 138 + 138 Gaps:50 48.68 378 45.11 9e-35 protein pelota-like
blastp_kegg lcl|pmum:103318765 1 87 + 87 Gaps:44 34.56 379 54.96 2e-34 protein pelota
blastp_pdb 3mca_B 1 92 + 92 Gaps:2 24.10 390 31.91 6e-12 mol:protein length:390 Protein dom34
blastp_uniprot_sprot sp|Q5U567|PELO_XENLA 1 78 + 78 none 20.37 383 39.74 1e-12 Protein pelota homolog OS Xenopus laevis GN pelo PE 2 SV 1
blastp_uniprot_sprot sp|Q5ZK01|PELO_CHICK 1 78 + 78 none 20.26 385 39.74 7e-12 Protein pelota homolog OS Gallus gallus GN PELO PE 2 SV 1
blastp_uniprot_sprot sp|Q58DV0|PELO_BOVIN 1 78 + 78 none 20.26 385 39.74 7e-12 Protein pelota homolog OS Bos taurus GN PELO PE 2 SV 2
blastp_uniprot_sprot sp|Q5XIP1|PELO_RAT 1 78 + 78 none 20.26 385 39.74 8e-12 Protein pelota homolog OS Rattus norvegicus GN Pelo PE 2 SV 1
blastp_uniprot_sprot sp|Q9USL5|DOM34_SCHPO 1 92 + 92 Gaps:2 24.10 390 31.91 2e-11 Protein dom34 OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN dom34 PE 1 SV 1
blastp_uniprot_sprot sp|Q9BRX2|PELO_HUMAN 1 78 + 78 none 20.26 385 38.46 2e-11 Protein pelota homolog OS Homo sapiens GN PELO PE 1 SV 2
blastp_uniprot_sprot sp|Q7ZWC4|PELO_DANRE 1 78 + 78 none 20.26 385 38.46 2e-11 Protein pelota homolog OS Danio rerio GN pelo PE 2 SV 1
blastp_uniprot_sprot sp|Q5RCE3|PELO_PONAB 1 78 + 78 none 20.26 385 38.46 3e-11 Protein pelota homolog OS Pongo abelii GN PELO PE 2 SV 1
blastp_uniprot_sprot sp|Q80X73|PELO_MOUSE 1 78 + 78 none 20.26 385 38.46 3e-11 Protein pelota homolog OS Mus musculus GN Pelo PE 2 SV 3
blastp_uniprot_sprot sp|P48612|PELO_DROME 1 78 + 78 none 19.75 395 38.46 8e-11 Protein pelota OS Drosophila melanogaster GN pelo PE 2 SV 2
rpsblast_cdd gnl|CDD|202649 1 71 + 71 Gaps:2 54.89 133 32.88 2e-13 pfam03463 eRF1_1 eRF1 domain 1. The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known. The overall shape and dimensions of eRF1 resemble a tRNA molecule with domains 1 2 and 3 of eRF1 corresponding to the anticodon loop aminoacyl acceptor stem and T stem of a tRNA molecule respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1 80 A from the GGQ motif is proposed to form the codon recognition site. This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.
rpsblast_cdd gnl|CDD|31726 1 71 + 71 Gaps:3 19.32 352 39.71 1e-12 COG1537 PelA Predicted RNA-binding proteins [General function prediction only].
rpsblast_cdd gnl|CDD|129217 1 70 + 70 Gaps:2 19.37 351 33.82 3e-07 TIGR00111 pelota mRNA surveillance protein pelota. This model describes the Drosophila protein Pelota the budding yeast protein DOM34 which it can replace and a set of closely related archaeal proteins. Members contain a proposed RNA binding motif. The meiotic defect in pelota mutants may be a complex result of a protein translation defect as suggested in yeast by ribosomal protein RPS30A being a multicopy suppressor and by an altered polyribosome profile in DOM34 mutants rescued by RPS30A. This family is homologous to a family of peptide chain release factors. Pelota is proposed to act in protein translation.
rpsblast_kog gnl|CDD|38080 1 83 + 83 Gaps:1 21.64 379 51.22 3e-21 KOG2869 KOG2869 KOG2869 Meiotic cell division protein Pelota/DOM34 [Translation ribosomal structure and biogenesis].

3 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Pfam 1 71 71 PF03463 none eRF1 domain 1 IPR005140
SUPERFAMILY 1 75 75 SSF159065 none none none
PANTHER 2 78 77 PTHR10853 none none IPR004405

0 Localization

2 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_rEpiBC_3P Qrob_Chr05 5 s_2GDU0O_517 s_1BT8O3_239 25,81 0 55,45 lod 2,2101 5,5

0 Targeting