ID A0A2K5HSY2_COLAP Unreviewed; 317 AA.
AC A0A2K5HSY2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=tRNA-dihydrouridine synthase {ECO:0000256|PIRNR:PIRNR006621};
DE EC=1.3.1.- {ECO:0000256|PIRNR:PIRNR006621};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000007445.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000007445.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. {ECO:0000256|ARBA:ARBA00002468,
CC ECO:0000256|PIRNR:PIRNR006621}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|PIRNR:PIRNR006621};
CC -!- SIMILARITY: Belongs to the dus family. {ECO:0000256|PIRNR:PIRNR006621}.
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DR RefSeq; XP_011803605.1; XM_011948215.1.
DR AlphaFoldDB; A0A2K5HSY2; -.
DR STRING; 336983.ENSCANP00000007445; -.
DR Ensembl; ENSCANT00000027599.1; ENSCANP00000007445.1; ENSCANG00000024456.1.
DR GeneID; 105516128; -.
DR KEGG; cang:105516128; -.
DR CTD; 11062; -.
DR OMA; LIYPYVD; -.
DR OrthoDB; 35861at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IEA:InterPro.
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; IPR001269; DUS_fam.
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 PIRSF; PIRSF006621; 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 ECO:0000256|PIRNR:PIRNR006621};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR006621};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006621};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|PIRNR:PIRNR006621}.
FT DOMAIN 31..292
FT /note="DUS-like FMN-binding"
FT /evidence="ECO:0000259|Pfam:PF01207"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006621-1"
SQ SEQUENCE 317 AA; 35866 MW; 7B3B5CCFBB346654 CRC64;
MKSDCMQTII CQERKKDPIE MFHSGQLVKV CAPMVRYSKL AFRTLVRKYS CDLCYTPMIV
AADFVKSIKA RDSEFTTNQG DCPLIVQFAA NDARLLSDAA RIVCPYANGI DINCGCPQRW
AMAEGYGACL INKPELVRDM VKQVRNQVET PGFSVSIKIR IHDDLKRTVD LCRKAEATGV
SWITVHGRTA EERHQPVHYD SIKIIKENMS IPVIANGDIR SLKEAENVWH ITGTDGVMVA
RGLLANPAMF AGYEETPLKC IWDWVDIALE LGTPYMCFHQ HLMYMMEKIT SRQEKRVFNA
LSSTSAIIDY LTDHYGI
//
