allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called ...
1-229
8.84e-117
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called allantoate amidinohydrolase. This enzyme hydrolyzes allantoate to (S)-ureidoglycolate and urea; it can also degrade (R)-ureidoglycolate to glyoxylate and urea. Allantoinase (EC 3.5.2.5) hydrolyzes (S)-allantoin (a xanthine metabolite, via urate) to allantoate. Allantoate can then be degraded either by this enzyme, allantoicase, or by allantoate deiminase (EC 3.5.3.9). Members of the seed alignment for this model were taken from BRENDA. Proteins in this family contain two copies of the allantoicase repeat (pfam03561). A different but similarly named enzyme, allantoate amidohydrolase (EC 3.5.3.9), simultaneously breaks down the urea to ammonia and carbon dioxide. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
The actual alignment was detected with superfamily member TIGR02961:
Pssm-ID: 274363 [Multi-domain] Cd Length: 322 Bit Score: 336.98 E-value: 8.84e-117
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called ...
1-229
8.84e-117
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called allantoate amidinohydrolase. This enzyme hydrolyzes allantoate to (S)-ureidoglycolate and urea; it can also degrade (R)-ureidoglycolate to glyoxylate and urea. Allantoinase (EC 3.5.2.5) hydrolyzes (S)-allantoin (a xanthine metabolite, via urate) to allantoate. Allantoate can then be degraded either by this enzyme, allantoicase, or by allantoate deiminase (EC 3.5.3.9). Members of the seed alignment for this model were taken from BRENDA. Proteins in this family contain two copies of the allantoicase repeat (pfam03561). A different but similarly named enzyme, allantoate amidohydrolase (EC 3.5.3.9), simultaneously breaks down the urea to ammonia and carbon dioxide. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 274363 [Multi-domain] Cd Length: 322 Bit Score: 336.98 E-value: 8.84e-117
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of ...
67-231
6.96e-58
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of the protein. These proteins allow the use of purines as secondary nitrogen sources in nitrogen-limiting conditions through the reaction: allantoate + H(2)0 = (-)-ureidoglycolate + urea.
Pssm-ID: 460972 [Multi-domain] Cd Length: 150 Bit Score: 181.13 E-value: 6.96e-58
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called ...
1-229
8.84e-117
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called allantoate amidinohydrolase. This enzyme hydrolyzes allantoate to (S)-ureidoglycolate and urea; it can also degrade (R)-ureidoglycolate to glyoxylate and urea. Allantoinase (EC 3.5.2.5) hydrolyzes (S)-allantoin (a xanthine metabolite, via urate) to allantoate. Allantoate can then be degraded either by this enzyme, allantoicase, or by allantoate deiminase (EC 3.5.3.9). Members of the seed alignment for this model were taken from BRENDA. Proteins in this family contain two copies of the allantoicase repeat (pfam03561). A different but similarly named enzyme, allantoate amidohydrolase (EC 3.5.3.9), simultaneously breaks down the urea to ammonia and carbon dioxide. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 274363 [Multi-domain] Cd Length: 322 Bit Score: 336.98 E-value: 8.84e-117
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of ...
67-231
6.96e-58
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of the protein. These proteins allow the use of purines as secondary nitrogen sources in nitrogen-limiting conditions through the reaction: allantoate + H(2)0 = (-)-ureidoglycolate + urea.
Pssm-ID: 460972 [Multi-domain] Cd Length: 150 Bit Score: 181.13 E-value: 6.96e-58
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called ...
59-230
7.43e-31
allantoicase; Members of this family are the enzyme allantoicase (EC 3.5.3.4), also called allantoate amidinohydrolase. This enzyme hydrolyzes allantoate to (S)-ureidoglycolate and urea; it can also degrade (R)-ureidoglycolate to glyoxylate and urea. Allantoinase (EC 3.5.2.5) hydrolyzes (S)-allantoin (a xanthine metabolite, via urate) to allantoate. Allantoate can then be degraded either by this enzyme, allantoicase, or by allantoate deiminase (EC 3.5.3.9). Members of the seed alignment for this model were taken from BRENDA. Proteins in this family contain two copies of the allantoicase repeat (pfam03561). A different but similarly named enzyme, allantoate amidohydrolase (EC 3.5.3.9), simultaneously breaks down the urea to ammonia and carbon dioxide. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 274363 [Multi-domain] Cd Length: 322 Bit Score: 116.26 E-value: 7.43e-31
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of ...
1-47
5.77e-18
Allantoicase repeat; This family is found in pairs in Allantoicases, forming the majority of the protein. These proteins allow the use of purines as secondary nitrogen sources in nitrogen-limiting conditions through the reaction: allantoate + H(2)0 = (-)-ureidoglycolate + urea.
Pssm-ID: 460972 [Multi-domain] Cd Length: 150 Bit Score: 77.90 E-value: 5.77e-18
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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