Protein : Qrob_P0359930.2 Q. robur
Protein Identifier  ? Qrob_P0359930.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=2) K02897 - large subunit ribosomal protein L25 Gene Prediction Quality  validated
Protein length 

Sequence

Length: 251  
Kegg Orthology  K02897
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0 Synonyms

4 GO Terms

Identifier Name Description
GO:0003735 structural constituent of ribosome The action of a molecule that contributes to the structural integrity of the ribosome.
GO:0005840 ribosome An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins.
GO:0006412 translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA. Translation ends with the release of a polypeptide chain from the ribosome.
GO:0008097 5S rRNA binding Interacting selectively and non-covalently with 5S ribosomal RNA, the smallest RNA constituent of a ribosome.

23 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103323524 1 250 + 250 Gaps:3 96.17 261 75.30 4e-134 uncharacterized LOC103323524
blastp_kegg lcl|pmum:103319136 5 250 + 246 Gaps:2 95.69 255 77.87 2e-133 uncharacterized LOC103319136
blastp_kegg lcl|pper:PRUPE_ppa009539mg 29 250 + 222 none 77.35 287 82.43 2e-131 hypothetical protein
blastp_kegg lcl|pper:PRUPE_ppa016528mg 31 250 + 220 Gaps:2 100.00 218 82.57 3e-129 hypothetical protein
blastp_kegg lcl|vvi:100242725 32 250 + 219 Gaps:2 84.11 258 81.11 3e-125 50S ribosomal protein L25-like
blastp_kegg lcl|vvi:100255348 32 250 + 219 Gaps:2 84.11 258 80.65 8e-125 50S ribosomal protein L25-like
blastp_kegg lcl|csv:101225381 32 248 + 217 Gaps:2 82.69 260 82.33 3e-124 50S ribosomal protein L25-like
blastp_kegg lcl|csv:101205251 32 248 + 217 Gaps:2 82.69 260 82.33 3e-124 50S ribosomal protein L25-like
blastp_kegg lcl|mdm:103453901 1 246 + 246 Gaps:1 92.80 264 72.65 4e-124 uncharacterized LOC103453901
blastp_kegg lcl|gmx:100809143 10 250 + 241 Gaps:3 94.16 257 74.38 6e-124 uncharacterized LOC100809143
blastp_uniprot_sprot sp|Q2G6G9|RL25_NOVAD 49 226 + 178 Gaps:18 78.43 204 30.63 3e-21 50S ribosomal protein L25 OS Novosphingobium aromaticivorans (strain DSM 12444) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|A5CF34|RL25_ORITB 43 250 + 208 Gaps:21 92.27 207 32.46 1e-20 50S ribosomal protein L25 OS Orientia tsutsugamushi (strain Boryong) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|Q1GSP2|RL25_SPHAL 43 214 + 172 Gaps:18 72.64 212 30.52 4e-20 50S ribosomal protein L25 OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|B3CTF9|RL25_ORITI 43 250 + 208 Gaps:21 92.27 207 32.46 7e-20 50S ribosomal protein L25 OS Orientia tsutsugamushi (strain Ikeda) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|A7HVD8|RL25_PARL1 42 221 + 180 Gaps:24 75.00 216 32.72 8e-20 50S ribosomal protein L25 OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|B0T899|RL25_CAUSK 49 226 + 178 Gaps:26 82.41 199 35.37 1e-19 50S ribosomal protein L25 OS Caulobacter sp. (strain K31) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|Q2NAN1|RL25_ERYLH 43 214 + 172 Gaps:18 67.25 229 30.52 4e-19 50S ribosomal protein L25 OS Erythrobacter litoralis (strain HTCC2594) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|A5FZ47|RL25_ACICJ 42 220 + 179 Gaps:18 74.19 217 33.54 4e-19 50S ribosomal protein L25 OS Acidiphilium cryptum (strain JF-5) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|B8IFN5|RL25_METNO 46 239 + 194 Gaps:19 83.89 211 32.20 9e-19 50S ribosomal protein L25 OS Methylobacterium nodulans (strain ORS2060 / LMG 21967) GN rplY PE 3 SV 1
blastp_uniprot_sprot sp|Q3SPM6|RL25_NITWN 46 239 + 194 Gaps:24 77.19 228 35.23 2e-18 50S ribosomal protein L25 OS Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391) GN rplY PE 3 SV 1
rpsblast_cdd gnl|CDD|180166 43 243 + 201 Gaps:22 92.89 197 32.79 1e-29 PRK05618 PRK05618 50S ribosomal protein L25/general stress protein Ctc Reviewed.
rpsblast_cdd gnl|CDD|162013 49 240 + 192 Gaps:21 97.16 176 26.32 3e-14 TIGR00731 ctc_TL5 ribosomal protein L25 Ctc-form. This model models a family of proteins with full-length homology to the general stress protein Ctc of Bacillus subtilis a mesophile and ribosomal protein TL5 of Thermus thermophilus a thermophile. Ribosomal protein L25 of Escherichia coli and H. influenzae appear to be orthologous but consist only of the N-terminal half of Ctc and TL5. Both short (L25-like) and full-length (CTC-like) members of this family bind the E-loop of bacterial 5S rRNA. This protein appears to be restricted to bacteria and organelles and consists of at most one copy per prokaryotic genome.Ctc of Bacillus subtilis has now been localized to ribosomes and can be viewed as the long form or Ctc form of L25. The C-terminal domain of sll1824 an apparent L25 of Synechocystis PCC6803 matches the N-terminal domain of this family. Examples of L25 and Ctc are not separated by a UPGMA tree built on the region of shared homology.
rpsblast_cdd gnl|CDD|198379 43 151 + 109 Gaps:19 100.00 90 31.11 1e-09 cd00495 Ribosomal_L25_TL5_CTC Ribosomal L25/TL5/CTC N-terminal 5S rRNA binding domain. L25 is a single-domain protein homologous to the N-terminal domain of TL5 and CTC. CTC is a known stress protein and proteins of this family are believed to have two functions acting as both ribosomal and stress proteins. In Escherichia coli cells deleted for L25 were found to be viable however these cells grew slowly and had impaired protein synthesis capability. In Bacillus subtilis CTC is induced under stress conditions and located in the ribosome it has been proposed that CTC may be necessary for accurate translation under stress conditions. Ribosomal_L25_TL5_CTC is mostly found in bacteria with a few exceptions such as plants or stramenopiles. Due to its limited taxonomic diversity and the viability of cells deleted for L25 this protein is not believed to be necessary for ribosomal assembly. Eukaryotes contain a protein called L25 which is not homologous to bacterial L25 but rather to bacterial L23.

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 43 151 109 G3DSA:2.40.240.10 "Reactome:REACT_71" none IPR020056
ProDom 49 151 103 PD012503 none RIBOSOMAL L25 50S RRNA-BINDING RNA-BINDING RIBONUCLEOPROTEIN STRESS GENERAL CTC RRNA IPR029751
Pfam 158 243 86 PF14693 none Ribosomal protein TL5, C-terminal domain IPR020057
Gene3D 158 247 90 G3DSA:2.170.120.20 none none IPR020057
SUPERFAMILY 48 240 193 SSF50715 "Reactome:REACT_71" none IPR011035
Pfam 45 149 105 PF01386 none Ribosomal L25p family IPR029751

0 Localization

16 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5
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_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2002_QTL11_peak_Bud_burst_A4 Qrob_Chr06 6 s_1C41PA_791 s_1AM1AV_1141 19,17 0 34,57 lod 2,3 2,9
Bourran2_2014_aSeqBC_3P Qrob_Chr06 6 v_506_189 v_686_77 30,72 13,58 43,48 lod 2,2746 6,3
Bourran2_2014_aSeqBC*_A4 Qrob_Chr06 6 s_2F5MK3_712 v_444_355 27,13 14,86 39,46 lod 3,7847 9,8
Bourran2_2014_nEpis*_3P Qrob_Chr08 8 s_1DA4QW_688 s_1DNI7D_820 17,96 0 37,75 lod 2,9745 7,5
Bourran2_2014_nEpis*_A4 Qrob_Chr07 7 v_12400_446 s_1BPEBU_1211 6,93 0 15,13 lod 4,7411 11
Bourran2_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran2_2014_nLBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,41 9,8 50,1 lod 1,9524 4,1
Bourran2_2014_nPriBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,51 3,36 51,86 lod 1,6747 3,9
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_vEpiBC_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,55 14,41 50,01 lod 1,7882 4,8
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9
Champenoux_2015_nP_3P Qrob_Chr06 6 s_1A386O_228 s_1AYZFS_603 27,03 26,47 27,34 lod 2.8 7.2

0 Targeting