Protein : Qrob_P0515700.2 Q. robur
Protein Identifier  ? Qrob_P0515700.2 Organism . Name  Quercus robur
Score  76.5 Score Type  egn
Protein Description  (M=2) 1.3.1.91 - tRNA-dihydrouridine(20) synthase (NAD(P)(+)). Code Enzyme  EC:1.3.1.91
Gene Prediction Quality  validated Protein length 

Sequence

Length: 106  
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0 Synonyms

5 GO Terms

Identifier Name Description
GO:0055114 oxidation-reduction process A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons.
GO:0003824 catalytic activity Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0050660 flavin adenine dinucleotide binding Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
GO:0008033 tRNA processing The process in which a pre-tRNA molecule is converted to a mature tRNA, ready for addition of an aminoacyl group.
GO:0017150 tRNA dihydrouridine synthase activity Catalysis of the reaction: tRNA-uracil + acceptor = tRNA-dihydrouridine + reduced acceptor.

27 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cmo:103484905 12 103 + 92 none 28.31 325 82.61 2e-43 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|csv:101220446 12 103 + 92 none 28.31 325 82.61 2e-43 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|csv:101225227 12 103 + 92 none 28.31 325 82.61 2e-43 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|mdm:103436768 11 101 + 91 Gaps:7 30.82 318 76.53 1e-42 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|tcc:TCM_000905 12 101 + 90 Gaps:7 29.75 326 77.32 2e-42 TRNA-dihydrouridine synthase
blastp_kegg lcl|rcu:RCOM_0188130 12 101 + 90 Gaps:7 29.39 330 76.29 2e-42 tRNA-dihydrouridine synthase putative
blastp_kegg lcl|gmx:100791745 12 101 + 90 Gaps:7 27.79 349 77.32 2e-42 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|pper:PRUPE_ppa008825mg 12 101 + 90 Gaps:7 30.50 318 77.32 3e-42 hypothetical protein
blastp_kegg lcl|mdm:103409433 12 101 + 90 Gaps:7 35.40 274 76.29 3e-42 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_kegg lcl|pmum:103336703 12 101 + 90 Gaps:7 30.50 318 77.32 3e-42 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
blastp_uniprot_sprot sp|Q9NX74|DUS2L_HUMAN 12 101 + 90 Gaps:11 20.49 493 41.58 3e-14 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like OS Homo sapiens GN DUS2 PE 1 SV 1
blastp_uniprot_sprot sp|Q9D7B1|DUS2L_MOUSE 12 101 + 90 Gaps:11 20.49 493 40.59 2e-12 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like OS Mus musculus GN Dus2 PE 1 SV 1
blastp_uniprot_sprot sp|O68273|DUSC_CUPNH 19 69 + 51 none 15.84 322 43.14 1e-07 tRNA-dihydrouridine synthase C OS Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) GN dusC PE 3 SV 2
blastp_uniprot_sprot sp|Q54CU9|DUS3L_DICDI 12 76 + 65 none 9.69 671 41.54 1e-07 tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like OS Dictyostelium discoideum GN dus3l PE 3 SV 1
blastp_uniprot_sprot sp|Q9JZL5|DUSC_NEIMB 12 69 + 58 none 17.42 333 41.38 4e-07 tRNA-dihydrouridine synthase C OS Neisseria meningitidis serogroup B (strain MC58) GN dusC PE 3 SV 1
blastp_uniprot_sprot sp|Q55724|DUS1_SYNY3 22 69 + 48 none 13.52 355 52.08 5e-07 Probable tRNA-dihydrouridine synthase 1 OS Synechocystis sp. (strain PCC 6803 / Kazusa) GN dus1 PE 3 SV 1
blastp_uniprot_sprot sp|Q9JUP6|DUSC_NEIMA 12 69 + 58 none 17.42 333 41.38 7e-07 tRNA-dihydrouridine synthase C OS Neisseria meningitidis serogroup A / serotype 4A (strain Z2491) GN dusC PE 3 SV 1
blastp_uniprot_sprot sp|P44606|DUSC_HAEIN 12 69 + 58 Gaps:1 19.03 310 47.46 8e-07 tRNA-dihydrouridine synthase C OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN dusC PE 3 SV 1
blastp_uniprot_sprot sp|Q8EFG7|DUSC_SHEON 11 69 + 59 none 18.73 315 42.37 1e-06 tRNA-dihydrouridine synthase C OS Shewanella oneidensis (strain MR-1) GN dusC PE 3 SV 1
blastp_uniprot_sprot sp|O95620|DUS4L_HUMAN 13 76 + 64 none 20.19 317 39.06 1e-06 tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like OS Homo sapiens GN DUS4L PE 2 SV 2
rpsblast_cdd gnl|CDD|73368 11 80 + 70 none 30.30 231 42.86 4e-17 cd02801 DUS_like_FMN Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5 6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities which may overlap. 1VHN a putative flavin oxidoreductase has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present..
rpsblast_cdd gnl|CDD|144707 11 94 + 84 Gaps:5 28.80 309 38.20 3e-12 pfam01207 Dus Dihydrouridine synthase (Dus). Members of this family catalyze the reduction of the 5 6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit requiring NADPH or NADH and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
rpsblast_cdd gnl|CDD|129820 21 76 + 56 none 17.55 319 46.43 1e-11 TIGR00737 nifR3_yhdG putative TIM-barrel protein nifR3 family. This model represents one branch of COG0042 (Predicted TIM-barrel enzymes possibly dehydrogenases nifR3 family). This branch includes NifR3 itself from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803 HI0634 from Haemophilus influenzae and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3 a member of this family is unknown but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase.
rpsblast_cdd gnl|CDD|30391 11 75 + 65 Gaps:1 20.43 323 42.42 3e-10 COG0042 COG0042 tRNA-dihydrouridine synthase [Translation ribosomal structure and biogenesis].
rpsblast_cdd gnl|CDD|182540 24 69 + 46 none 14.74 312 43.48 1e-07 PRK10550 PRK10550 tRNA-dihydrouridine synthase C Provisional.
rpsblast_kog gnl|CDD|37545 11 96 + 86 Gaps:8 35.01 477 38.32 4e-19 KOG2334 KOG2334 KOG2334 tRNA-dihydrouridine synthase [Translation ribosomal structure and biogenesis].
rpsblast_kog gnl|CDD|37546 20 92 + 73 Gaps:2 20.95 358 36.00 1e-10 KOG2335 KOG2335 KOG2335 tRNA-dihydrouridine synthase [Translation ribosomal structure and biogenesis].

5 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
Gene3D 11 77 67 G3DSA:3.20.20.70 none none IPR013785
SUPERFAMILY 11 94 84 SSF51395 none none none
PANTHER 11 92 82 PTHR11082 none none IPR001269
Pfam 12 83 72 PF01207 none Dihydrouridine synthase (Dus) IPR001269
PANTHER 11 92 82 PTHR11082:SF4 none none none

0 Localization

7 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_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_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

0 Targeting