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0DPYL3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameDPYSL3
DescriptionDihydropyrimidinase-related protein 3 (drp-3) (unc-33-like phosphoprotein) (ulip protein) (collapsin response mediator protein 4) (crmp-4).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0004157 dihydropyrimidinase activity (TAS)
0007399 neurogenesis (TAS)
0006139 nucleobase, nucleoside, nucleotide and nucl... (TAS)
0007165 signal transduction (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This group of enzymes represents a large metal dependent hydrolase superfamily . The family includes adenine deaminase () that hydrolyses adenine to form hypoxanthine and ammonia. The adenine deaminase reaction is important for adenine utilization as a purine and also as a nitrogen source . This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases (). These enzymes catalyse the reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetateThis family includes dihydroorotase and urease which belong to MEROPS peptidase family M38 (beta-aspartyl dipeptidase.lan MJ).here they are classified as non-peptidase homologs.
  IPR006680:Amidohydrolase 1
Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ).here it is classified as a non-peptidase homologue. DHOase catalyses the third step in the de novo biosynthesis of pyrimidine.he conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. Dihydroorotase binds a zinc ion which is required for its catalytic activity .Dihydroorotase () (DHOase) catalyzes the third step in the de novo biosynthesis of pyrimidine.he conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate.In bacteria DHOase is a dimer of identical chains of about 400 amino-acid residues (gene pyrC). In higher eukaryotes DHOase is part of a large multi-functional protein known as rudimentary in Drosophila and CAD in mammals and which catalyzes the first three steps of pyrimidine biosynthesis . The DHOase domain is located in the central part of this polyprotein. In yeast.HOase is encoded by a monofunctional protein (gene URA4). However. defective DHOase domain is found in a multifunctional protein (gene URA2) that catalyzes the first two steps of pyrimidine biosynthesis.
  IPR005847:Dihydroorotase region
The composite domain of metal-dependent hydrolases has a pseudo-barrel fold that is interrupted by the catalytic beta/alpha barrel domain. This domain is found in a variety of bacterial and fungal enzymes.ncluding: cytosine deaminase.n enzyme that is important in the pyrimidine salvage pathway ; the alpha-subunit of urease. virulence factor of gastric pathogens such as Helicobacter pylori ; D- and L-hydantoinases (dihydropyrimidinase).hich catalyse the production of D- and L-amino acids.espectively ; isoaspartyl dipeptidase from Escherichia coli.hich functions in protein degradation ; N-acetylglucosamine-6-phosphate deacetylase.hich is an enzyme from the biosynthetic pathway to amino-sugar-nucleotides ; and N-acyl-D-amino acid amidohydrolase (D-aminoacylase).nvolved in the synthesis of D-amino acids .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011059:Metal-dependent hydrolase, composite
This entry represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5.-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme .
  IPR011778:D-hydantoinase
IPR006680:Amidohydro_1 
Evalue:-45.7695503234863 
Location:64-413
SequencesProtein: DPYL3_HUMAN (570 aa)
mRNA: NM_001387
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 1105 residues, 146750565-146753879Exon2: 56 residues, 146755314-146755477Exon3: 62 residues, 146757421-146757601Exon4: 59 residues, 146758837-146759008Exon5: 49 residues, 146760447-146760589Exon6: 54 residues, 146761295-146761452Exon7: 42 residues, 146765365-146765486Exon8: 25 residues, 146768483-146768552Exon9: 29 residues, 146772363-146772444Exon10: 22 residues, 146773351-146773413Exon11: 57 residues, 146775464-146775629Exon12: 63 residues, 146778202-146778387Exon13: 31 residues, 146784630-146784719Exon14: 51 residues, 146813304-146813453Exon15: 2 residues, -Jump to DPYL3_HUMAN  
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