Protein : Qrob_P0379590.2 Q. robur
Protein Identifier  ? Qrob_P0379590.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) K14566 - U3 small nucleolar RNA-associated protein 24 Gene Prediction Quality  validated
Protein length 

Sequence

Length: 131  
Kegg Orthology  K14566
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0032040 small-subunit processome A large ribonucleoprotein complex that is an early preribosomal complex. In S. cerevisiae, it has a size of 80S and consists of the 35S pre-rRNA, early-associating ribosomal proteins most of which are part of the small ribosomal subunit, the U3 snoRNA and associated proteins.

26 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|fve:101302294 1 120 + 120 none 60.61 198 86.67 2e-69 rRNA-processing protein FCF1 homolog
blastp_kegg lcl|tcc:TCM_005228 1 120 + 120 none 60.61 198 86.67 3e-69 PIN domain-like family protein
blastp_kegg lcl|csv:101220343 1 120 + 120 none 60.61 198 83.33 2e-67 rRNA-processing protein FCF1 homolog
blastp_kegg lcl|cmo:103486894 1 120 + 120 none 60.61 198 82.50 7e-67 rRNA-processing protein FCF1 homolog
blastp_kegg lcl|pxb:103965869 1 120 + 120 none 59.11 203 83.33 1e-66 rRNA-processing protein FCF1 homolog
blastp_kegg lcl|cam:101504471 1 120 + 120 none 60.61 198 83.33 1e-66 rRNA-processing protein FCF1 homolog
blastp_kegg lcl|dosa:Os06t0158600-01 1 120 + 120 Gaps:1 60.80 199 82.64 1e-66 Os06g0158600 Protein of unknown function DUF652 family protein.
blastp_kegg lcl|osa:4340192 1 120 + 120 Gaps:1 60.80 199 82.64 1e-66 Os06g0158600
blastp_kegg lcl|mtr:MTR_7g116720 1 120 + 120 none 60.61 198 83.33 2e-66 rRNA-processing protein FCF1-like protein
blastp_kegg lcl|pper:PRUPE_ppa011750mg 1 120 + 120 none 60.61 198 82.50 2e-66 hypothetical protein
blastp_uniprot_sprot sp|Q5RFQ0|FCF1_PONAB 1 120 + 120 Gaps:2 61.62 198 60.66 7e-41 rRNA-processing protein FCF1 homolog OS Pongo abelii GN FCF1 PE 2 SV 1
blastp_uniprot_sprot sp|Q9Y324|FCF1_HUMAN 1 120 + 120 Gaps:2 61.62 198 60.66 7e-41 rRNA-processing protein FCF1 homolog OS Homo sapiens GN FCF1 PE 2 SV 1
blastp_uniprot_sprot sp|Q32PD0|FCF1_BOVIN 1 120 + 120 Gaps:2 61.62 198 60.66 7e-41 rRNA-processing protein FCF1 homolog OS Bos taurus GN FCF1 PE 2 SV 1
blastp_uniprot_sprot sp|Q05498|FCF1_YEAST 1 120 + 120 Gaps:2 62.43 189 59.32 7e-41 rRNA-processing protein FCF1 OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN FCF1 PE 1 SV 1
blastp_uniprot_sprot sp|Q9CTH6|FCF1_MOUSE 1 120 + 120 Gaps:2 61.62 198 59.84 3e-40 rRNA-processing protein FCF1 homolog OS Mus musculus GN Fcf1 PE 2 SV 2
blastp_uniprot_sprot sp|O13610|FCF1_SCHPO 1 120 + 120 none 62.50 192 52.50 5e-37 rRNA-processing protein fcf1 OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN fcf1 PE 3 SV 1
blastp_uniprot_sprot sp|Q55GM5|FCF1_DICDI 7 120 + 114 Gaps:1 59.28 194 46.96 3e-30 rRNA-processing protein FCF1 homolog OS Dictyostelium discoideum GN fcf1 PE 3 SV 1
rpsblast_cdd gnl|CDD|189034 53 120 + 68 none 47.55 143 86.76 7e-37 cd09864 PIN_Fcf1 PIN domain of rRNA-processing protein Fcf1 (Utp24 YDR339C) and other eukaryotic homologs. Fcf1/Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) is an essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Component of the small subunit (SSU) processome Fcf1 is an essential nucleolar protein that is required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). The PIN (PilT N terminus) domain of this protein is a homolog of flap endonuclease-1 (FEN1)-like PIN domains but apparently lack the H3TH domain or extensive arch/clamp region seen in the latter. PIN domains typically contain three or four conserved acidic residues (putative metal-binding active site residues). The Fcf1 PIN domain subfamily has four of these putative active site residues and the Fcf1-Utp23 homolog PIN domain subfamily has three of them. Point mutation studies of the conserved acidic residues in the putative active site of Saccharomyces cerevisiae Fcf1 determined they were essential for pre-rRNA processing at sites A1 and A2 whereas the presence of the Fcf1 protein itself is also required for cleavage at site A0.
rpsblast_cdd gnl|CDD|189021 67 119 + 53 none 44.17 120 54.72 4e-17 cd08553 PIN_Fcf1-like PIN domain of rRNA-processing proteins Fcf1 (Utp24 YDR339C) Utp23 (YOR004W) and other eukaryotic homologs. Fcf1 (FAF1-copurifying factor 1 also known as Utp24) and Utp23 (U three-associated protein 23) are essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly. Components of the small subunit (SSU) processome Fcf1 and Utp23 are essential nucleolar proteins that are required for processing of the 18S pre-rRNA at sites A0-A2. The Fcf1 protein was reported to interact with Pmc1p (vacuolar Ca2+ ATPase) and Cor1p (core subunit of the ubiquinol-cytochrome c reductase complex). The PIN (PilT N terminus) domains of these proteins are homologs of flap endonuclease-1 (FEN1)-like PIN domains but apparently lack the H3TH domain or extensive arch/clamp region seen in the latter. PIN domains typically contain three or four conserved acidic residues (putative metal-binding active site residues). The Fcf1 PIN domain subfamily has four of these putative active site residues. Point mutation studies showed that the conserved acidic residues in the putative active site of Saccharomyces cerevisiae Fcf1 are essential for pre-rRNA processing at sites A1 and A2 whereas the presence of the Fcf1 protein itself is also required for cleavage at site A0. S. cerevisiae Utp23 lacks several of these key residues and mutation of the conserved acidic residues seen in Utp23 did not interfere with rRNA maturation and cell viability. The subfamily of Fcf1- and Utp23-like homologs found in eukaryotes (except fungi) posses three of the four conserved residues seen in S. cerevisiae Fcf1.
rpsblast_cdd gnl|CDD|31602 55 120 + 66 none 48.53 136 43.94 4e-16 COG1412 COG1412 Uncharacterized proteins of PilT N-term./Vapc superfamily [General function prediction only].
rpsblast_cdd gnl|CDD|189024 68 120 + 53 none 42.40 125 45.28 2e-11 cd09854 PIN_VapC-Smg6_family PIN domains of VapC and Smg6 ribonucleases ribosome assembly factor NOB1 rRNA-processing protein Fcf1 Archaeoglobus fulgidus AF0591 protein and homologs. PIN (PilT N terminus) domains of such ribonucleases as the toxins of prokaryotic toxin/antitoxin operons FitAB and VapBC as well as eukaryotic ribonucleases such as Smg6 ribosome assembly factor NOB1 exosome subunit Rrp44 endoribonuclease and rRNA-processing protein Fcf1 are included in this family. Also included are the PIN domains of the Pyrobaculum aerophilum Pea0151 and Archaeoglobus fulgidus AF0591 proteins and other similar archaeal homologs. These PIN domains are structural homologs of flap endonuclease-1 (FEN1)-like PIN domains but lack the extensive arch/clamp region and the H3TH (helix-3-turn-helix) domain an atypical helix-hairpin-helix-2-like region seen in FEN1-like PIN domains. PIN domains typically contain three or four highly conserved acidic residues (putative metal-binding active site residues) which cluster at the C-terminal end of the beta-sheet and form a negatively charged pocket near the center of the molecule.
rpsblast_cdd gnl|CDD|191123 89 120 + 32 none 31.68 101 65.62 1e-09 pfam04900 Fcf1 Fcf1. Fcf1 is a nucleolar protein involved in pre-rRNA processing. Depletion of yeast Fcf1 and Fcf2 leads to a decrease in synthesis of the 18S rRNA and results in a deficit in 40S ribosomal subunits.
rpsblast_cdd gnl|CDD|189036 54 125 + 72 Gaps:3 51.02 147 29.33 3e-09 cd09866 PIN_Fcf1-Utp23-H PIN domain of rRNA-processing protein Fcf1- and Utp23-like homologs found in eukaryotes except fungi. PIN domain homologs of Fcf1/Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) and Utp23 essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly are included in this subfamily. Fcf1 is a component of the small subunit (SSU) processome and an essential nucleolar protein required for processing of the 18S pre-rRNA at sites A0-A2. These PIN (PilT N terminus) domains are homologs of flap endonuclease-1 (FEN1)-like PIN domains but apparently lack the H3TH domain or extensive arch/clamp region seen in the latter. PIN domains typically contain three or four conserved acidic residues (putative metal-binding active site residues). The Fcf1-Utp23 homolog PIN domain subfamily has three of these conserved acidic residues rather than the four seen in the Fcf1 PIN domain subfamily.
rpsblast_cdd gnl|CDD|189022 68 122 + 55 Gaps:7 51.67 120 30.65 4e-08 cd09852 PIN_SF PIN (PilT N terminus) domain: Superfamily. PIN_SF The PIN (PilT N terminus) domain belongs to a large nuclease superfamily with representatives from eukaryota eubacteria and archaea. PIN domains were originally named for their sequence similarity to the N-terminal domain of an annotated pili biogenesis protein PilT a domain fusion between a PIN-domain and a PilT ATPase domain. The structural properties of the PIN domain indicate its putative active center consisting of invariant acidic amino acid residues (putative metal-binding residues) is geometrically similar in the active center of structure-specific 5' nucleases (also known as Flap endonuclease-1-like) PIN-domain ribonucleases of eukaryotic rRNA editing proteins and bacterial toxins of toxin-antitoxin (TA) operons. Seen here are two major divisions in the PIN domain superfamily. The first major division the structure-specific 5' nuclease family is represented by FEN1 the 5'-3' exonuclease of DNA polymerase I and T4 RNase H nuclease PIN domains. These 5' nucleases are involved in DNA replication repair and recombination. They are capable of both 5'-3' exonucleolytic activity and cleaving bifurcated DNA in an endonucleolytic structure-specific manner. Unique to FEN1-like nucleases the PIN domain has a helical arch/clamp region (I domain) of variable length (approximately 16 to 800 residues) and inserted within the C-terminal region of the PIN domain a H3TH (helix-3-turn-helix) domain an atypical helix-hairpin-helix-2-like region. Both the H3TH domain (not included here) and the helical arch/clamp region are involved in DNA binding. With the exception of Mkt1 these nucleases have a carboxylate rich active site that is involved in binding essential divalent metal ion cofactors (Mg2+ Mn2+ Zn2+ or Co2+). The second major division of the PIN domain superfamily the VapC-Smg6 family includes such eukaryotic ribonucleases as Smg6 an essential factor in nonsense-mediated mRNA decay Rrp44 the catalytic subunit of the exosome and Nob1 a ribosome assembly factor critical in pre-rRNA processing. A large percentage of members in this family are bacterial ribonuclease toxins of TA operons such as Mycobacterium tuberculosis VapC and Neisseria gonorrhoeae FitB as well as archaeal homologs Pyrobaculum aerophilum Pea0151 and P. aerophilum Pae2754. Also included are the eukaryotic Fcf1/ Utp24 (FAF1-copurifying factor 1/U three-associated protein 24) and Utp23-like proteins. Components of the small subunit processome Fcf1/Utp24 and Utp23 are essential proteins involved in pre-rRNA processing and 40S ribosomal subunit assembly.
rpsblast_kog gnl|CDD|38375 1 120 + 120 Gaps:1 61.03 195 69.75 1e-42 KOG3165 KOG3165 KOG3165 Predicted nucleic-acid-binding protein contains PIN domain [General function prediction only].
rpsblast_kog gnl|CDD|38374 53 112 + 60 none 25.42 236 38.33 6e-07 KOG3164 KOG3164 KOG3164 Uncharacterized proteins of PilT N-term./Vapc superfamily [General function prediction only].

4 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 2 120 119 PTHR12416 none none none
SUPERFAMILY 63 122 60 SSF88723 none none IPR029060
Pfam 89 120 32 PF04900 none Fcf1 IPR006984
Gene3D 64 121 58 G3DSA:3.40.50.1010 none none IPR029060

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