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Conserved domains on  [gi|830867233|gb|AKL88568|]
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carbamoyl phosphate synthase large subunit, partial [Limosilactobacillus fermentum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carB super family cl35300
carbamoyl-phosphate synthase large subunit;
1-172 2.71e-110

carbamoyl-phosphate synthase large subunit;


The actual alignment was detected with superfamily member PRK05294:

Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 337.45  E-value: 2.71e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:PRK05294  284 VQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDLLSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRRG 160
Cdd:PRK05294  364 EKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRG 443

                         170
                  ....*....|..
gi 830867233  161 YSLADLHELTRI 172
Cdd:PRK05294  444 ASVEEIHELTKI 455
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-172 2.71e-110

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 337.45  E-value: 2.71e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:PRK05294  284 VQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDLLSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRRG 160
Cdd:PRK05294  364 EKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRG 443

                         170
                  ....*....|..
gi 830867233  161 YSLADLHELTRI 172
Cdd:PRK05294  444 ASVEEIHELTKI 455
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-172 8.19e-96

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: 298.84  E-value: 8.19e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233     1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:TIGR01369  282 VQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDF 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDLLSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRRG 160
Cdd:TIGR01369  362 DKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRG 441

                          170
                   ....*....|..
gi 830867233   161 YSLADLHELTRI 172
Cdd:TIGR01369  442 VSVDEIHELTKI 453
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-172 4.14e-74

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: 231.31  E-value: 4.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   1 VQLALDpnSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPvtkttyAEFEPALDYVVVKIPRWTF 80
Cdd:COG0458  269 IQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGND------TGFEPTLDYVVVKEPVFPF 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233  81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQ--KDLLSKEaaaASDRQLEDKLVHAQDDRLFYIAEAFR 158
Cdd:COG0458  341 EKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLpgTVLLSLV---ADDDKEEALLLARRLARLGFLIEATR 417

                        170
                 ....*....|....
gi 830867233 159 RGYSLADLHELTRI 172
Cdd:COG0458  418 GTAEVLEEAGITVI 431
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1-50 6.81e-20

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 82.35  E-value: 6.81e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 50
Cdd:pfam02786 160 VEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 138-172 7.74e-12

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 59.00  E-value: 7.74e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 830867233   138 LEDKLVHAQDDRLFYIAEAFRRGYSLADLHELTRI 172
Cdd:smart01096   1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKI 35
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-172 2.71e-110

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 337.45  E-value: 2.71e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:PRK05294  284 VQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAF 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDLLSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRRG 160
Cdd:PRK05294  364 EKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRG 443

                         170
                  ....*....|..
gi 830867233  161 YSLADLHELTRI 172
Cdd:PRK05294  444 ASVEEIHELTKI 455
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-172 8.19e-96

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: 298.84  E-value: 8.19e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233     1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:TIGR01369  282 VQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDF 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDLLSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRRG 160
Cdd:TIGR01369  362 DKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRG 441

                          170
                   ....*....|..
gi 830867233   161 YSLADLHELTRI 172
Cdd:TIGR01369  442 VSVDEIHELTKI 453
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 1-172 5.29e-86

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 272.61  E-value: 5.29e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:PRK12815  283 IQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPF 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQKDL-LSKEAAAASDRQLEDKLVHAQDDRLFYIAEAFRR 159
Cdd:PRK12815  363 DKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLsLPIELSGKSDEELLQDLRHPDDRRLFALLEALRR 442

                         170
                  ....*....|...
gi 830867233  160 GYSLADLHELTRI 172
Cdd:PRK12815  443 GITYEEIHELTKI 455
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-172 4.14e-74

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: 231.31  E-value: 4.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   1 VQLALDpnSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPvtkttyAEFEPALDYVVVKIPRWTF 80
Cdd:COG0458  269 IQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGND------TGFEPTLDYVVVKEPVFPF 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233  81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDQ--KDLLSKEaaaASDRQLEDKLVHAQDDRLFYIAEAFR 158
Cdd:COG0458  341 EKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLpgTVLLSLV---ADDDKEEALLLARRLARLGFLIEATR 417

                        170
                 ....*....|....
gi 830867233 159 RGYSLADLHELTRI 172
Cdd:COG0458  418 GTAEVLEEAGITVI 431
PLN02735 PLN02735
carbamoyl-phosphate synthase
 1-172 1.15e-53

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 182.67  E-value: 1.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPVTKTTYAEFEPALDYVVVKIPRWTF 80
Cdd:PLN02735  301 VQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAF 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVASLEIDqkdlLSKEAAAASDR------QLEDKLVHAQDDRLFYIA 154
Cdd:PLN02735  381 EKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG----FSGWGCAKVKEldwdweQLKYKLRVPNPDRIHAIY 456

                         170
                  ....*....|....*...
gi 830867233  155 EAFRRGYSLADLHELTRI 172
Cdd:PLN02735  457 AAMKKGMTVDEIHELTFI 474
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-114 4.45e-28

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 109.42  E-value: 4.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNS-YdynVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKnpvtkttyAEFEPALDYVVVKIPRWT 79
Cdd:PRK05294  823 VQFAVKDDEvY---VIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELG--------YTKGLIPPYVAVKEAVFP 891

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 830867233   80 FDKFTKADRRLGSQMKATGEVMAIGRTAEEALLKA 114
Cdd:PRK05294  892 FNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-117 3.72e-26

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: 103.93  E-value: 3.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233     1 VQLALDPNsyDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIknPVTKttyaefEPALDYVVVKIPRWTF 80
Cdd:TIGR01369  823 IQFAVKDG--EVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEEL--GVGK------EKEPKYVAVKEPVFSF 892

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 830867233    81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVAS 117
Cdd:TIGR01369  893 SKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLS 929
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 1-117 1.28e-23

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 96.58  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNsyDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKNPvtkttyAEFEPALDYVVVKIPRWTF 80
Cdd:PRK12815  821 IQFVLAND--EIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYP------NGLWPGSPFIHVKMPVFSY 892

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKAVAS 117
Cdd:PRK12815  893 LKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEA 929
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 1-50 6.81e-20

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 82.35  E-value: 6.81e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYNVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 50
Cdd:pfam02786 160 VEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
PLN02735 PLN02735
carbamoyl-phosphate synthase
 1-114 2.61e-17

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 78.28  E-value: 2.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 830867233    1 VQLALDPNSYDYnVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEIKnpVTKttyaefEPALDYVVVKIPRWTF 80
Cdd:PLN02735  857 CQYAITPSGEVY-IIEANPRASRTVPFVSKAIGHPLAKYASLVMSGKSLKDLG--FTE------EVIPAHVSVKEAVLPF 927

                          90       100       110
                  ....*....|....*....|....*....|....
gi 830867233   81 DKFTKADRRLGSQMKATGEVMAIGRTAEEALLKA 114
Cdd:PLN02735  928 DKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKA 961
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 140-172 5.26e-12

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 58.16  E-value: 5.26e-12
                          10        20        30
                  ....*....|....*....|....*....|...
gi 830867233  140 DKLVHAQDDRLFYIAEAFRRGYSLADLHELTRI 172
Cdd:pfam02787   1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKI 33
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 138-172 7.74e-12

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 59.00  E-value: 7.74e-12
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 830867233   138 LEDKLVHAQDDRLFYIAEAFRRGYSLADLHELTRI 172
Cdd:smart01096   1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKI 35
 
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.
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