NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1220131398|gb|ASN78294|]
View 

CAD2, partial [Acanthinevania sp. 242]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CPSaseII_lrg super family cl36884
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 50-107 3.54e-32

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


The actual alignment was detected with superfamily member TIGR01369:

Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 118.18  E-value: 3.54e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220131398   50 KKPKKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMAD 61
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 50-107 3.54e-32

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 118.18  E-value: 3.54e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220131398   50 KKPKKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMAD 61
carB PRK05294
carbamoyl-phosphate synthase large subunit;
53-107 2.26e-27

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 104.41  E-value: 2.26e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:PRK05294     8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMAD 62
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 58-107 4.09e-21

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 86.47  E-value: 4.09e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1220131398  58 LGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTAD 50
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 50-107 3.54e-32

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 118.18  E-value: 3.54e-32
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220131398   50 KKPKKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:TIGR01369    4 TDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMAD 61
carB PRK05294
carbamoyl-phosphate synthase large subunit;
53-107 2.26e-27

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 104.41  E-value: 2.26e-27
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:PRK05294     8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMAD 62
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 58-107 4.09e-21

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 86.47  E-value: 4.09e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1220131398  58 LGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTAD 50
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 53-107 9.39e-21

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 85.41  E-value: 9.39e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:PRK12815     8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPAD 62
PLN02735 PLN02735
carbamoyl-phosphate synthase
 53-107 2.06e-17

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 75.97  E-value: 2.06e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:PLN02735    24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETAD 78
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 53-107 1.51e-13

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 64.99  E-value: 1.51e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:PRK12815   556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTAD 610
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 50-107 2.65e-13

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 64.25  E-value: 2.65e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1220131398   50 KKPKKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQTSKGMAD 107
Cdd:TIGR01369  552 TDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSD 609
carB PRK05294
carbamoyl-phosphate synthase large subunit;
53-101 2.90e-11

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 58.18  E-value: 2.90e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQT 101
Cdd:PRK05294   555 KKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVST 603
PLN02735 PLN02735
carbamoyl-phosphate synthase
 53-101 8.18e-08

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 48.62  E-value: 8.18e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1220131398   53 KKVLILGSGGLSIGQAGEFDYSGSQAIKALREESIQTLLINPNIATVQT 101
Cdd:PLN02735   575 KKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVST 623
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH