vanin-like [Drosophila melanogaster]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
33-304 | 3.40e-132 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. : Pssm-ID: 143591 Cd Length: 299 Bit Score: 386.98 E-value: 3.40e-132
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Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
328-512 | 2.50e-55 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. : Pssm-ID: 465946 Cd Length: 165 Bit Score: 183.72 E-value: 2.50e-55
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Name | Accession | Description | Interval | E-value | |||||
biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
33-304 | 3.40e-132 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143591 Cd Length: 299 Bit Score: 386.98 E-value: 3.40e-132
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Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
328-512 | 2.50e-55 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. Pssm-ID: 465946 Cd Length: 165 Bit Score: 183.72 E-value: 2.50e-55
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Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
34-276 | 7.37e-14 | |||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 71.82 E-value: 7.37e-14
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CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
68-208 | 4.57e-08 | |||||
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins. Pssm-ID: 425873 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 4.57e-08
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PLN02747 | PLN02747 | N-carbamolyputrescine amidase |
153-297 | 6.73e-04 | |||||
N-carbamolyputrescine amidase Pssm-ID: 215398 Cd Length: 296 Bit Score: 42.06 E-value: 6.73e-04
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Name | Accession | Description | Interval | E-value | |||||
biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
33-304 | 3.40e-132 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143591 Cd Length: 299 Bit Score: 386.98 E-value: 3.40e-132
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Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
328-512 | 2.50e-55 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. Pssm-ID: 465946 Cd Length: 165 Bit Score: 183.72 E-value: 2.50e-55
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nitrilase | cd07197 | Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
54-299 | 3.42e-17 | |||||
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy. Pssm-ID: 143587 [Multi-domain] Cd Length: 253 Bit Score: 81.60 E-value: 3.42e-17
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Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
34-276 | 7.37e-14 | |||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 71.82 E-value: 7.37e-14
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nitrilase_5 | cd07583 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
58-230 | 1.64e-13 | |||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143607 Cd Length: 253 Bit Score: 70.64 E-value: 1.64e-13
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nitrilase_3 | cd07581 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
70-232 | 4.07e-13 | |||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143605 Cd Length: 255 Bit Score: 69.53 E-value: 4.07e-13
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nit | cd07572 | Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
70-228 | 5.46e-12 | |||||
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 10. Pssm-ID: 143596 Cd Length: 265 Bit Score: 66.30 E-value: 5.46e-12
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nitrilase_6 | cd07584 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
58-230 | 7.63e-12 | |||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143608 Cd Length: 258 Bit Score: 65.85 E-value: 7.63e-12
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R-amidase_like | cd07576 | Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
66-208 | 6.45e-11 | |||||
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer. Pssm-ID: 143600 Cd Length: 254 Bit Score: 62.98 E-value: 6.45e-11
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CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
68-208 | 4.57e-08 | |||||
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins. Pssm-ID: 425873 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 4.57e-08
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DCase | cd07569 | N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ... |
70-205 | 3.50e-05 | |||||
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers. Pssm-ID: 143593 Cd Length: 302 Bit Score: 45.76 E-value: 3.50e-05
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ALP_N-acyl_transferase | cd07571 | Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
54-208 | 1.68e-04 | |||||
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9. Pssm-ID: 143595 Cd Length: 270 Bit Score: 43.74 E-value: 1.68e-04
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Lnt | COG0815 | Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-208 | 2.73e-04 | |||||
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 43.68 E-value: 2.73e-04
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nitrilases_CHs | cd07564 | Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ... |
70-195 | 5.96e-04 | |||||
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 1. Pssm-ID: 143588 Cd Length: 297 Bit Score: 42.09 E-value: 5.96e-04
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PLN02747 | PLN02747 | N-carbamolyputrescine amidase |
153-297 | 6.73e-04 | |||||
N-carbamolyputrescine amidase Pssm-ID: 215398 Cd Length: 296 Bit Score: 42.06 E-value: 6.73e-04
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ScNTA1_like | cd07566 | Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); ... |
59-206 | 8.33e-04 | |||||
Saccharomyces cerevisiae N-terminal amidase NTA1, and related proteins (class 3 nitrilases); Saccharomyces cerevisiae NTA1 functions in the N-end rule protein degradation pathway. It specifically deaminates the N-terminal asparagine and glutamine residues of substrates of this pathway, to aspartate and glutamate respectively, these latter are the destabilizing residues. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 3. Pssm-ID: 143590 Cd Length: 295 Bit Score: 41.56 E-value: 8.33e-04
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nitrilase_7 | cd07585 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
151-205 | 2.11e-03 | |||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143609 Cd Length: 261 Bit Score: 39.99 E-value: 2.11e-03
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PLN02798 | PLN02798 | nitrilase |
152-220 | 4.90e-03 | |||||
nitrilase Pssm-ID: 215428 Cd Length: 286 Bit Score: 38.96 E-value: 4.90e-03
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Blast search parameters | ||||
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