ID A0A2K5XVD0_MANLE Unreviewed; 464 AA.
AC A0A2K5XVD0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Dihydrouridine synthase 2 {ECO:0000313|Ensembl:ENSMLEP00000007272.1};
GN Name=DUS2 {ECO:0000313|Ensembl:ENSMLEP00000007272.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000007272.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000007272.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR AlphaFoldDB; A0A2K5XVD0; -.
DR STRING; 9568.ENSMLEP00000007272; -.
DR Ensembl; ENSMLET00000030574.1; ENSMLEP00000007272.1; ENSMLEG00000027642.1.
DR GeneTree; ENSGT00550000075019; -.
DR OMA; GPIRTNS; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:Ensembl.
DR GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:Ensembl.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR CDD; cd19871; DSRM_DUS2L; 1.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR044463; DUS2_DSRM.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR PANTHER; PTHR45936; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR PANTHER; PTHR45936:SF1; TRNA-DIHYDROURIDINE(20) SYNTHASE [NAD(P)+]-LIKE; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF01207; Dus; 1.
DR SMART; SM00358; DSRM; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 341..406
FT /note="DRBM"
FT /evidence="ECO:0000259|SMART:SM00358"
FT REGION 409..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 52025 MW; A4F01E2402CCCC71 CRC64;
MFRTDKRPLI PLQELIDLKM IQCKRVVNEV LSTVDFVAPD DRVVFRTCER EQNRVVFQMG
TSDAERALAV ARLVENDVAG IDVNMGCPKE YSTKGGMGAA LLSDPDKIEK ILSTLVKGIR
RPVTCKIRIL PSLEDTLSLV KRIERTGIAA IAVHGRKREE RPQHPVSCEV IKAIADTLSI
PVIANGGSHD HIQRYSDIED FRQATAASSV MVARAAMWNP SIFLKEGLRP LEEVMQKYIR
YAVQYDNHYT NTKYCLCQML REQLESPQGR LLHAAQSSRE ICEAFGLGAF YEETTQELDA
QRAKLSARTS EETGEPAEDT SGVIKMAVKF DRRAYPAQIT PKMCLLEWCR REKLAQPVYE
TVQRPLDRLF SSIVTVAEQK YQSTLWDKSK KLAEQAAAIV CLRSQGLPEG RLGEESPSLH
KRKREAPDQD PGGPRAQELA QPGELCKKPF VALGSGEESP LEGW
//
