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Q9D7B1 (DUS2L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

EC=1.3.1.-
Alternative name(s):
tRNA-dihydrouridine synthase 2-like
Gene names
Name:Dus2l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dihydrouridine synthase. Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs By similarity.

Cofactor

FAD By similarity.

Subunit structure

Interacts with EPRS By similarity.

Subcellular location

Cytoplasm By similarity. Endoplasmic reticulum By similarity. Note: Mainly at the endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the dus family. Dus2 subfamily.

Contains 1 DRBM (double-stranded RNA-binding) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
PRO_0000162158

Regions

Domain369 – 43668DRBM

Secondary structure

..................... 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D7B1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B66BDCB06B096299

FASTA49355,325
        10         20         30         40         50         60 
MIVNSLSLCY HNKLILAPMV RVGTLPMRLL ALDYGADIVY CEELIDLKML QCKRVVNEVL 

        70         80         90        100        110        120 
STVDFVAPDD RVVFRTCERE QSRVVFQMGT SDAERALAVA RLVENDVAGI DVNMGCPKEY 

       130        140        150        160        170        180 
STKGGMGAAL LSDPDKIEKI LSTLVKGTHR PVTCKIRILP SLEDTLNLVK RIERTGISAI 

       190        200        210        220        230        240 
AVHGRNRDER PQHPVSCEVI RAIAETLSIP VIANGGSHDH IQQHVDIEDF RQATAASSVM 

       250        260        270        280        290        300 
VARAAMWNPS IFLKDGLRPL EEVMQKYIRY AVQYDNHYTN TKYCLCQMLR EQLESPQGRL 

       310        320        330        340        350        360 
LHAAQSSQEI CEAFGLGAFY EETIRELDAR RADLLAKTPE AVEEPAEDTS GIIKMAIRFD 

       370        380        390        400        410        420 
RRAYPPQITP KMCLLEWCRR EKLPQPVYET VQRTIDRMFC SVVTVAEQKY QSTLWDKSKK 

       430        440        450        460        470        480 
LAEQTAAIVC LRSQGLPEGR LGEESPSLNK RKREAPDQDP GGPRVQEPAL PGEICKKPFV 

       490 
TLDSSEENLL EGC 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-493.
Strain: C57BL/6.
Tissue: Brain.
[3]"Solution structure of the DSRBD from hypothetical protein BAB26260."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 350-464.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK009391 mRNA. Translation: BAB26260.1.
BC058431 mRNA. Translation: AAH58431.1.
IPIIPI00110119.
RefSeqNP_079794.1. NM_025518.3.
UniGeneMm.287500.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WHNNMR-A350-464[»]
ProteinModelPortalQ9D7B1.
SMRQ9D7B1. Positions 88-253, 352-464.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D7B1.

PTM databases

PhosphoSiteQ9D7B1.

Proteomic databases

PRIDEQ9D7B1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034375; ENSMUSP00000034375; ENSMUSG00000031901.
GeneID66369.
KEGGmmu:66369.

Organism-specific databases

CTD54920.
MGIMGI:1913619. Dus2l.

Phylogenomic databases

GeneTreeENSGT00550000075019.
HOGENOMHBG396464.
HOVERGENHBG079551.
InParanoidQ9D7B1.
OMAYHNKLIL.
OrthoDBEOG4MW85W.
PhylomeDBQ9D7B1.

Gene expression databases

ArrayExpressQ9D7B1.
BgeeQ9D7B1.
GenevestigatorQ9D7B1.
GermOnlineENSMUSG00000031901. Mus musculus.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
KOK05543.
PANTHERPTHR11082. Du_synth. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF01207. Dus. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
[Graphical view]
PROSITEPS50137. DS_RBD. False negative.
PS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio321469.
SOURCESearch...

Entry information

Entry nameDUS2L_MOUSE
AccessionPrimary (citable) accession number: Q9D7B1
Secondary accession number(s): Q6PDX2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families