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Database: UniProt
Entry: Q57V78_TRYB2
LinkDB: Q57V78_TRYB2
Original site: Q57V78_TRYB2 
ID   Q57V78_TRYB2            Unreviewed;       520 AA.
AC   Q57V78; D6XME0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 104.
DE   RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] {ECO:0000256|ARBA:ARBA00038890};
DE            EC=1.3.1.88 {ECO:0000256|ARBA:ARBA00038890};
GN   Name=Tb08.30P3.90 {ECO:0000313|EMBL:AAZ13520.1};
GN   ORFNames=Tb927.8.7570 {ECO:0000313|EMBL:AAX70483.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:AAX70483.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:AAZ13520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13520.1};
RX   PubMed=16020724; DOI=10.1126/science.1112181;
RA   El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA   Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA   Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA   Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA   Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA   Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA   Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA   Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA   Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT   "Comparative genomics of trypanosomatid parasitic protozoa.";
RL   Science 309:404-409(2005).
RN   [2] {ECO:0000313|EMBL:AAZ13520.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13520.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [3] {ECO:0000313|EMBL:AAX70483.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX70483.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   ".";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AAZ13520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ13520.1};
RA   Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA   Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA   Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA   Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA   Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT   "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT   through 8.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC         Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00035900};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC         Evidence={ECO:0000256|ARBA:ARBA00035900};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC         Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00036049};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC         Evidence={ECO:0000256|ARBA:ARBA00036049};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC         uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC         Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00035864};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC         Evidence={ECO:0000256|ARBA:ARBA00035864};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC         uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC         Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC         Evidence={ECO:0000256|ARBA:ARBA00035813};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC         Evidence={ECO:0000256|ARBA:ARBA00035813};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038313}.
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DR   EMBL; AC159445; AAX70483.1; -; Genomic_DNA.
DR   EMBL; CP000071; AAZ13520.1; -; Genomic_DNA.
DR   RefSeq; XP_847586.1; XM_842493.1.
DR   AlphaFoldDB; Q57V78; -.
DR   STRING; 185431.Q57V78; -.
DR   PaxDb; 5691-AAZ13520; -.
DR   GeneID; 3659765; -.
DR   KEGG; tbr:Tb927.8.7570; -.
DR   VEuPathDB; TriTrypDB:Tb927.8.7570; -.
DR   eggNOG; KOG2335; Eukaryota.
DR   InParanoid; Q57V78; -.
DR   OMA; FLMEDWE; -.
DR   OrthoDB; 5487726at2759; -.
DR   Proteomes; UP000008524; Chromosome 8.
DR   GO; GO:0097014; C:ciliary plasm; IDA:GeneDB.
DR   GO; GO:0005929; C:cilium; IDA:GeneDB.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0031981; C:nuclear lumen; IDA:GeneDB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISM:GeneDB.
DR   GO; GO:0017150; F:tRNA dihydrouridine synthase activity; ISM:GeneDB.
DR   GO; GO:0006400; P:tRNA modification; ISM:GeneDB.
DR   CDD; cd02801; DUS_like_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035587; DUS-like_FMN-bd.
DR   InterPro; IPR018517; tRNA_hU_synthase_CS.
DR   PANTHER; PTHR11082; TRNA-DIHYDROURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR11082:SF5; TRNA-DIHYDROURIDINE(16/17) SYNTHASE [NAD(P)(+)]-LIKE; 1.
DR   Pfam; PF01207; Dus; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS01136; UPF0034; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          77..340
FT                   /note="DUS-like FMN-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01207"
FT   REGION          471..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  58146 MW;  91C15B598BA952DA CRC64;
     MTYNEAALSK YRGLLDSGEP FRSRTCRYCS SGNTAVKHIN SKKKPNSPWD FWNGIACSPT
     ASHARAEGRK RTPMYVVGPM VDQSELPFRL LCRRYGATLA YTPMFHAKSF AQSAHYRQRY
     FSTTTFPPHS AMESGGNVAA NDSTSNDGAL DNDHPLFAQF CGNDPETVLA AARHVEDYCE
     AVDFNIGCPQ GIARRGHYGS FLMEDWELLH NILHALAVEL RVPVTAKMRI FDDEALTLKY
     AEMLRDTGIY VLCVHGRTRE NKGQQQQPAD LRMIRRVHEH LRGSIPIIAN GNVLTFEDVP
     RNLAITGCEG YMCAEPLLWD PKLFAPLASS STAEFAPNIT DSTLSTSPAP STVRSGRLFA
     ESRPTRLKAL ATASEYLELV RRFPVDIGFV KAHFFKMLYH SYEMHPAHQQ WLANFSINGS
     NVGNDVVENC ATSHCGEQRE TTVVGRDIFT AALDALTDHL HSLQKAELSL EHDGPQPKRQ
     RELKVGEEGK ERQQLKNGRR VDALTDTFAD DETLGIDFLM
//
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