P53720 (DUS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+]
EC=1.3.1.91

Alternative name(s):
Protein SMM1
tRNA-dihydrouridine synthase 2

Gene names

Name:	SMM1
Synonyms:	DUS2
Ordered Locus Names:	YNR015W
ORF Names:	N2065

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U20 in cytoplasmic tRNAs. Ref.4 Ref.7
Catalytic activity	5,6-dihydrouracil20 in tRNA + NAD(P)+ = uracil20 in tRNA + NAD(P)H.
Cofactor	FAD By similarity.
Subunit structure	Monomer.
Subcellular location	Cytoplasm. Nucleus Ref.5.
Post-translational modification	N-glycosylated.
Miscellaneous	Present with 2650 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the dus family. Dus2 subfamily.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Cytoplasm Nucleus
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: SGD nucleus Inferred from direct assay Ref.5. Source: SGD
Molecular_function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro tRNA dihydrouridine synthase activity Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	tRNA-dihydrouridine(20) synthase [NAD(P)+]		PRO_0000162154

Sequences

	Sequence		Length	Mass (Da)
	P53720 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 637EEC05DD4F9D6D	FASTA	384	42,816
	10 20 30 40 50 60 MVTYAGKLVL APMVRAGELP TRLMALAHGA DLVWSPEIID KKLIQCVRKE NTALQTVDYV 70 80 90 100 110 120 VPSKVQTRPE TLVFRTYPKL ESSKLIFQIG SASPALATQA ALKVINDVSG IDINAGCPKH 130 140 150 160 170 180 FSIHSGMGSA LLRTPDTLCL ILKELVKNVG NPHSKPISVK IRLLDTKQDT LQLVKRLCAT 190 200 210 220 230 240 GITNLTVHCR KTEMRNREQP ITDYIAEIYE ICQANNVSLI VNGAIRDRSH FHDLQANHWK 250 260 270 280 290 300 NTNIGGMIAE CAERDPTVFD HTSKPSEDGP SWVVACREFI QWATKFDNHI GNTKYMLSRI 310 320 330 340 350 360 VPGKSVFFQY FARCKSPEEV SFVLKQLNDD GSAQTDPSEY LENCRAQEKA LKNANAIAKQ 370 380 KRKQTDHIGS DTKKQKVVPL PTDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of three nuclear genes which in high copy number suppress a mitochondrial mutation in the tRNA(Asp) gene in Saccharomyces cerevisiae." Rinaldi T., Lande R., Bolotin-Fukuhara M., Frontali L. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R100.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA." Xing F., Martzen M.R., Phizicky E.M. RNA 8:370-381(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"The specificities of four yeast dihydrouridine synthases for cytoplasmic tRNAs." Xing F., Hiley S.L., Hughes T.R., Phizicky E.M. J. Biol. Chem. 279:17850-17860(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes." Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H. Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91816 Genomic DNA. Translation: CAA62924.1. Z71630 Genomic DNA. Translation: CAA96293.1. Z71631 Genomic DNA. Translation: CAA96295.1. BK006947 Genomic DNA. Translation: DAA10556.1.
PIR	S63345.
RefSeq	NP_014412.1. NM_001183192.1.
3D structure databases
ProteinModelPortal	P53720.
SMR	P53720. Positions 7-190.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4102N.
MINT	MINT-551094.
STRING	4932.YNR015W.
Proteomic databases
PaxDb	P53720.
PeptideAtlas	P53720.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNR015W; YNR015W; YNR015W.
GeneID	855749.
KEGG	sce:YNR015W.
Organism-specific databases
CYGD	YNR015w.
SGD	S000005298. SMM1.
Phylogenomic databases
eggNOG	COG0042.
GeneTree	ENSGT00550000075019.
HOGENOM	HOG000195580.
KO	K05543.
OMA	VEESMFY.
OrthoDB	EOG4PG98M.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16677.
Gene expression databases
Genevestigator	P53720.
GermOnline	YNR015W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR001269. tRNA_hU_synthase. IPR018517. tRNA_hU_synthase_CS. [Graphical view]
PANTHER	PTHR11082. PTHR11082. 1 hit.
Pfam	PF01207. Dus. 1 hit. [Graphical view]
PIRSF	PIRSF006621. Dus. 1 hit.
PROSITE	PS01136. UPF0034. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980160.

Entry information

Entry name

DUS2_YEAST

Accession

Primary (citable) accession number: P53720
Secondary accession number(s): D6W1J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program