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Protein

tRNA-dihydrouridine(20) synthase [NAD(P)+]

Gene

SMM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U20 in cytoplasmic tRNAs.2 Publications

Catalytic activityi

5,6-dihydrouracil(20) in tRNA + NAD(P)+ = uracil(20) in tRNA + NAD(P)H.

Cofactori

FADBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. tRNA dihydrouridine synthase activity Source: SGD

GO - Biological processi

  1. tRNA dihydrouridine synthesis Source: GOC
  2. tRNA modification Source: SGD
  3. tRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16677.
YEAST:G3O-33331-MONOMER.
BRENDAi1.3.1.91. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-dihydrouridine(20) synthase [NAD(P)+] (EC:1.3.1.91)
Alternative name(s):
Protein SMM1
tRNA-dihydrouridine synthase 2
Gene namesi
Name:SMM1
Synonyms:DUS2
Ordered Locus Names:YNR015W
ORF Names:N2065
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNR015w.
EuPathDBiFungiDB:YNR015W.
SGDiS000005298. SMM1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384tRNA-dihydrouridine(20) synthase [NAD(P)+]PRO_0000162154Add
BLAST

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP53720.
PaxDbiP53720.
PeptideAtlasiP53720.

Expressioni

Gene expression databases

GenevestigatoriP53720.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi35840. 46 interactions.
DIPiDIP-4102N.
MINTiMINT-551094.
STRINGi4932.YNR015W.

Structurei

3D structure databases

ProteinModelPortaliP53720.
SMRiP53720. Positions 7-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Dus family. Dus2 subfamily.Curated

Phylogenomic databases

eggNOGiCOG0042.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
InParanoidiP53720.
KOiK05543.
OMAiYGVDGAM.
OrthoDBiEOG7J9W16.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTYAGKLVL APMVRAGELP TRLMALAHGA DLVWSPEIID KKLIQCVRKE
60 70 80 90 100
NTALQTVDYV VPSKVQTRPE TLVFRTYPKL ESSKLIFQIG SASPALATQA
110 120 130 140 150
ALKVINDVSG IDINAGCPKH FSIHSGMGSA LLRTPDTLCL ILKELVKNVG
160 170 180 190 200
NPHSKPISVK IRLLDTKQDT LQLVKRLCAT GITNLTVHCR KTEMRNREQP
210 220 230 240 250
ITDYIAEIYE ICQANNVSLI VNGAIRDRSH FHDLQANHWK NTNIGGMIAE
260 270 280 290 300
CAERDPTVFD HTSKPSEDGP SWVVACREFI QWATKFDNHI GNTKYMLSRI
310 320 330 340 350
VPGKSVFFQY FARCKSPEEV SFVLKQLNDD GSAQTDPSEY LENCRAQEKA
360 370 380
LKNANAIAKQ KRKQTDHIGS DTKKQKVVPL PTDI
Length:384
Mass (Da):42,816
Last modified:October 1, 1996 - v1
Checksum:i637EEC05DD4F9D6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91816 Genomic DNA. Translation: CAA62924.1.
Z71630 Genomic DNA. Translation: CAA96293.1.
Z71631 Genomic DNA. Translation: CAA96295.1.
BK006947 Genomic DNA. Translation: DAA10556.1.
PIRiS63345.
RefSeqiNP_014412.1. NM_001183192.1.

Genome annotation databases

EnsemblFungiiYNR015W; YNR015W; YNR015W.
GeneIDi855749.
KEGGisce:YNR015W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91816 Genomic DNA. Translation: CAA62924.1.
Z71630 Genomic DNA. Translation: CAA96293.1.
Z71631 Genomic DNA. Translation: CAA96295.1.
BK006947 Genomic DNA. Translation: DAA10556.1.
PIRiS63345.
RefSeqiNP_014412.1. NM_001183192.1.

3D structure databases

ProteinModelPortaliP53720.
SMRiP53720. Positions 7-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35840. 46 interactions.
DIPiDIP-4102N.
MINTiMINT-551094.
STRINGi4932.YNR015W.

Proteomic databases

MaxQBiP53720.
PaxDbiP53720.
PeptideAtlasiP53720.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR015W; YNR015W; YNR015W.
GeneIDi855749.
KEGGisce:YNR015W.

Organism-specific databases

CYGDiYNR015w.
EuPathDBiFungiDB:YNR015W.
SGDiS000005298. SMM1.

Phylogenomic databases

eggNOGiCOG0042.
GeneTreeiENSGT00550000075019.
HOGENOMiHOG000195580.
InParanoidiP53720.
KOiK05543.
OMAiYGVDGAM.
OrthoDBiEOG7J9W16.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16677.
YEAST:G3O-33331-MONOMER.
BRENDAi1.3.1.91. 984.

Miscellaneous databases

NextBioi980160.
PROiP53720.

Gene expression databases

GenevestigatoriP53720.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001269. tRNA_hU_synthase.
IPR018517. tRNA_hU_synthase_CS.
[Graphical view]
PANTHERiPTHR11082. PTHR11082. 1 hit.
PfamiPF01207. Dus. 1 hit.
[Graphical view]
PIRSFiPIRSF006621. Dus. 1 hit.
PROSITEiPS01136. UPF0034. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. 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].

Entry informationi

Entry nameiDUS2_YEAST
AccessioniPrimary (citable) accession number: P53720
Secondary accession number(s): D6W1J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2650 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.