ID Q5KPM6_CRYNJ Unreviewed; 407 AA.
AC Q5KPM6;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DUS-like FMN-binding domain-containing protein {ECO:0000259|Pfam:PF01207};
GN OrderedLocusNames=CNA02240 {ECO:0000313|EMBL:AAW40793.1};
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW40793.1, ECO:0000313|Proteomes:UP000002149};
RN [1] {ECO:0000313|EMBL:AAW40793.1, ECO:0000313|Proteomes:UP000002149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149};
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00033653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00033638};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; AE017341; AAW40793.1; -; Genomic_DNA.
DR RefSeq; XP_566612.1; XM_566612.1.
DR AlphaFoldDB; Q5KPM6; -.
DR STRING; 214684.Q5KPM6; -.
DR PaxDb; 214684-Q5KPM6; -.
DR EnsemblFungi; AAW40793; AAW40793; CNA02240.
DR GeneID; 3253630; -.
DR KEGG; cne:CNA02240; -.
DR VEuPathDB; FungiDB:CNA02240; -.
DR eggNOG; KOG2335; Eukaryota.
DR HOGENOM; CLU_013299_4_2_1; -.
DR InParanoid; Q5KPM6; -.
DR OMA; KIVEPYC; -.
DR OrthoDB; 35861at2759; -.
DR Proteomes; UP000002149; Chromosome 1.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
DR GO; GO:0102266; F:tRNA-dihydrouridine20a synthase activity; IEA:EnsemblFungi.
DR GO; GO:0102267; F:tRNA-dihydrouridine20b synthase activity; IEA:EnsemblFungi.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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:SF31; TRNA-DIHYDROURIDINE(20A_20B) SYNTHASE [NAD(P)+]-LIKE; 1.
DR Pfam; PF01207; Dus; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002149};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 151..359
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 116..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 45564 MW; CE9D105933723473 CRC64;
MALDQDATDE QLYADLPSPL HLSPSELIET YHPNVLAPLV RCSKLPFRHL TSLYETHITH
TPMILAEEFS RAQIARTSDF STSSNERGVY WMAPNNGKCR GKGEYITRVG HPEDVRPAKE
PWKTYHSPPS TERLPPSPAP PNPQAQLVRG CLIAQFASPN AKSLADAAEL ISPYVDGIDL
NCGCPQRWAY NEGIGCALLR KPELVRDMVR GVKDRMGWGW PVSIKIRIDS EQEKTEQLIS
NALQAGISHL TIHGRTRHQP STDPVNLPGI KFAVDCVKGE VPCVANGDVW ELEDARQMRL
HTGVQGVMAA RGLLANPALF AGYDKTPEDC VSQFINLGLD YGFNFSLFHR HLAYMLESHL
SRVEKVWFNS LTSQASAIEW LNERAINFKE KRGTIWDARR GYNITDV
//
