ID A0A0N8H6U3_9HYPO Unreviewed; 1065 AA.
AC A0A0N8H6U3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 02-APR-2025, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPM39932.1};
GN ORFNames=AK830_g6607 {ECO:0000313|EMBL:KPM39932.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM39932.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM39932.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM39932.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. Specifically modifies U47 in
CC cytoplasmic tRNAs. Catalyzes the synthesis of dihydrouridine in some
CC mRNAs, thereby affecting their translation.
CC {ECO:0000256|ARBA:ARBA00045934}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC NADH + H(+); 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:ARBA00048342};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000256|ARBA:ARBA00048342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC NADPH + H(+); 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:ARBA00049447};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000256|ARBA:ARBA00049447};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM39932.1}.
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DR EMBL; LKCW01000094; KPM39932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8H6U3; -.
DR STRING; 78410.A0A0N8H6U3; -.
DR OrthoDB; 9977870at2759; -.
DR Proteomes; UP000050424; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0102265; F:tRNA-dihydrouridine47 synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd20335; BRcat_RBR; 1.
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; IPR002867; IBR_dom.
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 Pfam; PF01485; IBR; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 314..361
FT /note="IBR"
FT /evidence="ECO:0000259|Pfam:PF01485"
FT DOMAIN 734..918
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..524
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 121374 MW; 571D2555624101C3 CRC64;
MAVLALGQKL QLMPGSFSPE DYIDFYENPF DDLENLQTAW RDRDTLVPWS TNNLSNVDVT
DVDWYQYNPP AALRKATHIT SQVLLDIIWS SIENVKTQAA EQQRQKREKK EQSKLAEDAA
KKLDKGKEPY LPINIPQDKP KPYIDDKTPR HSIISLSGST STITATDIPS KPEKRRKFAL
RKFFQRGHGK GESSSTGSTL EALRKTYESR QVSSRNSTSD ATTVSRTGSL GELVECVSCL
DGFSVKDVIK VPCHSYCRVC FVRLVSAAVQ NEQQWPPKCC LNQIPVQTIV RYIPSNLKKT
FQERSSEWDI PVGDRIYCSH QGCNLIIKPQ SIDKKKRQGT CDNRHATCTI CRDAGHKGRE
CERDPDMDLT NILAEEEGWK SQRWRTCECT MQQLYDLKAA ADTKREQRQF REQTDAEELR
QILLQIEEFE REETLKAEML RQEQERLEEE RRQHELEERV RQESMRRRDI EIKFRGLRVT
LDELHELQQV LVEVNQEEMG EEIIAEIKTA KEELAKKQEA ERSELDSLMM TKLADKEYSL
NRDFQIRAAG EHDIEEAYHE KLQDYWKGKR DGEKEIEASM LALRKRMDQR QHTWQKWKTE
AMRVHEANLK EDWSLREELI YSTKHRLDAA CEEKERELIR RKAAEKKWLE MVILERERLM
NETEAQEVEG DADSLFTPDL DNGRNDGAVR SSRPALKEVL PKMSICGEGQ SAHPLKIFDV
TRKQDRFLYA LAPMVRNESS PIQDFTVSTN PDQPATIVQF GANVPLEMAR AAALVAPRAN
GVDLNCGCPQ SWACAEKLGA ALMGHRELVR DMVVETRQRL QRDGWHVGLE RDIESPKGRS
VSVKIRIHDD LRKTMDFLDT VIGEPQNRLV DWVTIHPRTK STPSTTPIRT EALEILIAKY
AGTLPILLSG DIFDIKSLPV QPTINTNNDA PHASLATLTL NSSSIVATPY SKPAASPSNT
NLSGFMSARG LLANPALFAG HSACPWEAVE TFMCNVTRCP LPFKLALHHL QEMCGPGMGA
DKSSLLSKKE RAEMTGLANM CGLIDYLDDM IEEKNGRVGG LRRDL
//
