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Conserved domains on  [gi|307640723|gb|ADN81178|]
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CAD, partial [Salassa sp. NW-2010]

Protein Classification

carbamoyl-phosphate synthase large subunit family protein( domain architecture ID 1002141)

carbamoyl-phosphate synthase (CPSase) large subunit family protein; CPSase catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis

CATH:  3.30.470.20|1.10.1030.10|3.30.1490.20|3.40.50.1380
Gene Ontology:  GO:0005951
PubMed:  9914247|11212301
SCOP:  4001126|4002053|4003761|4003858

Graphical summary

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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 ...
 1-263 1.42e-134

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: 405.15  E-value: 1.42e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723     1 STKIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDPNIKNVNENE-----LREPTDKRMFVLAAALKQGYSVEKL 75
Cdd:TIGR01369  368 DRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEI 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    76 YELTKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTV 155
Cdd:TIGR01369  448 HELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTC 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   156 AAEWPASTNYLYLTYNGSTHDLEFP-GEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDM 234
Cdd:TIGR01369  528 AAEFEAQTPYLYSTYEGERDDVPFTdKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDT 607

                          250       260
                   ....*....|....*....|....*....
gi 307640723   235 SDRLYFEEISFEVVMDIYNIEHPEGVILS 263
Cdd:TIGR01369  608 SDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-263 1.42e-134

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: 405.15  E-value: 1.42e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723     1 STKIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDPNIKNVNENE-----LREPTDKRMFVLAAALKQGYSVEKL 75
Cdd:TIGR01369  368 DRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEI 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    76 YELTKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTV 155
Cdd:TIGR01369  448 HELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTC 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   156 AAEWPASTNYLYLTYNGSTHDLEFP-GEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDM 234
Cdd:TIGR01369  528 AAEFEAQTPYLYSTYEGERDDVPFTdKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDT 607

                          250       260
                   ....*....|....*....|....*....
gi 307640723   235 SDRLYFEEISFEVVMDIYNIEHPEGVILS 263
Cdd:TIGR01369  608 SDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
carB PRK05294
carbamoyl-phosphate synthase large subunit;
3-262 1.02e-120

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 369.04  E-value: 1.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    3 KIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDP-NIKNVNENELRE----PTDKRMFVLAAALKQGYSVEKLYE 77
Cdd:PRK05294  372 RLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEdLFEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHE 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   78 LTKIDIWFLEKFKNIIDYYKTLEALDSPsVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTVAA 157
Cdd:PRK05294  452 LTKIDPWFLEQIEEIVELEEELKENGLP-LDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAA 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723  158 EWPASTNYLYLTYNGSTHDLEFPGEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDR 237
Cdd:PRK05294  531 EFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDR 610

                         250       260
                  ....*....|....*....|....*
gi 307640723  238 LYFEEISFEVVMDIYNIEHPEGVIL 262
Cdd:PRK05294  611 LYFEPLTLEDVLEIIEKEKPKGVIV 635
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 48-170 2.32e-60

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: 186.89  E-value: 2.32e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    48 ENELREPTDKRMFVLAAALKQGYSVEKLYELTKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAA 127
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 307640723   128 AIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTY 170
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 187-263 3.52e-36

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: 134.62  E-value: 3.52e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307640723 187 LGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVILS 263
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 50-127 2.18e-35

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: 121.33  E-value: 2.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307640723   50 ELREPTDKRMFVLAAALKQGYSVEKLYELTKIDIWFLEKFKNIIDYYKTLEALDSPsVNFNVLKRAKKIGFSDKQIAA 127
Cdd:pfam02787   2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAK 78
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-263 1.42e-134

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: 405.15  E-value: 1.42e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723     1 STKIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDPNIKNVNENE-----LREPTDKRMFVLAAALKQGYSVEKL 75
Cdd:TIGR01369  368 DRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATGFDLPDREVEPDEdlwraLKKPTDRRIFAIAEALRRGVSVDEI 447

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    76 YELTKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTV 155
Cdd:TIGR01369  448 HELTKIDRWFLHKIKNIVDLEEELEEVKLTDLDPELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTC 527

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   156 AAEWPASTNYLYLTYNGSTHDLEFP-GEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDM 234
Cdd:TIGR01369  528 AAEFEAQTPYLYSTYEGERDDVPFTdKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDT 607

                          250       260
                   ....*....|....*....|....*....
gi 307640723   235 SDRLYFEEISFEVVMDIYNIEHPEGVILS 263
Cdd:TIGR01369  608 SDRLYFEPLTFEDVMNIIELEKPEGVIVQ 636
carB PRK05294
carbamoyl-phosphate synthase large subunit;
3-262 1.02e-120

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 369.04  E-value: 1.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    3 KIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDP-NIKNVNENELRE----PTDKRMFVLAAALKQGYSVEKLYE 77
Cdd:PRK05294  372 RLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTGLDEdLFEEESLEELREelkePTPERLFYIAEAFRRGASVEEIHE 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   78 LTKIDIWFLEKFKNIIDYYKTLEALDSPsVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTVAA 157
Cdd:PRK05294  452 LTKIDPWFLEQIEEIVELEEELKENGLP-LDAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAA 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723  158 EWPASTNYLYLTYNGSTHDLEFPGEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDR 237
Cdd:PRK05294  531 EFEADTPYYYSTYEEECESNPSDRKKVLVLGSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDR 610

                         250       260
                  ....*....|....*....|....*
gi 307640723  238 LYFEEISFEVVMDIYNIEHPEGVIL 262
Cdd:PRK05294  611 LYFEPLTLEDVLEIIEKEKPKGVIV 635
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 3-262 6.74e-82

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 265.29  E-value: 6.74e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    3 KIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDPNIKNVNENE------LREPTDKRMFVLAAALKQGYSVEKLY 76
Cdd:PRK12815  371 TLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGLSLPIELSGKSDeellqdLRHPDDRRLFALLEALRRGITYEEIH 450

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   77 ELTKIDIWFLEKFKNIIDYYKTLEAlDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTVA 156
Cdd:PRK12815  451 ELTKIDPFFLQKFEHIVALEKKLAE-DGLDLSADLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCA 529

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723  157 AEWPASTNYLYLTYNGSThDLEFPGE--YVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDM 234
Cdd:PRK12815  530 AEFEAKTPYYYSTYFGES-EAEPSSEkkKVLILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDT 608

                         250       260
                  ....*....|....*....|....*...
gi 307640723  235 SDRLYFEEISFEVVMDIYNIEHPEGVIL 262
Cdd:PRK12815  609 ADRLYFEPLTLEDVLNVAEAENIKGVIV 636
PLN02735 PLN02735
carbamoyl-phosphate synthase
 8-262 2.49e-71

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 236.60  E-value: 2.49e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    8 MKSVG*VMSIGRSFEEAFQKALRMVDENVNGFDPniKNVNENE---------LREPTDKRMFVLAAALKQGYSVEKLYEL 78
Cdd:PLN02735  394 MKSVGEAMALGRTFQESFQKALRSLETGFSGWGC--AKVKELDwdweqlkykLRVPNPDRIHAIYAAMKKGMTVDEIHEL 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   79 TKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTVAAE 158
Cdd:PLN02735  472 TFIDPWFLTQLKELVDVEQFLKSRSLSELSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAE 551

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723  159 WPASTNYLYLTYNGSTHDLEFPGEYVMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRL 238
Cdd:PLN02735  552 FEANTPYMYSSYDGECESAPTNKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRL 631

                         250       260
                  ....*....|....*....|....
gi 307640723  239 YFEEISFEVVMDIYNIEHPEGVIL 262
Cdd:PLN02735  632 YFEPLTVEDVLNVIDLERPDGIIV 655
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
 48-170 2.32e-60

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: 186.89  E-value: 2.32e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723    48 ENELREPTDKRMFVLAAALKQGYSVEKLYELTKIDIWFLEKFKNIIDYYKTLEALDSPSVNFNVLKRAKKIGFSDKQIAA 127
Cdd:smart01096   2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDELDADLLRKAKRLGFSDRQIAK 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 307640723   128 AIKSTEVAVRKLREEFKITPFVKQIDTVAAEWPASTNYLYLTY 170
Cdd:smart01096  82 LLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 187-263 3.52e-36

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: 134.62  E-value: 3.52e-36
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 307640723 187 LGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVILS 263
Cdd:COG0458    1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQ 77
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
 50-127 2.18e-35

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: 121.33  E-value: 2.18e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307640723   50 ELREPTDKRMFVLAAALKQGYSVEKLYELTKIDIWFLEKFKNIIDYYKTLEALDSPsVNFNVLKRAKKIGFSDKQIAA 127
Cdd:pfam02787   2 ELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLD-LDAELLREAKRLGFSDRQIAK 78
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-189 1.71e-29

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: 116.13  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723   1 STKIGSSMKSVG*VMSIGRSFEEAFQKALRMVDENVNG--FDPNIKNVNENELRE--PTDKRMFVLAAALKQGYSVEKLY 76
Cdd:COG0458  347 DPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSLVADDDKEEALLlaRRLARLGFLIEATRGTAEVLEEA 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 307640723  77 ELTKIDIWFLEKFKNIIdyyKTLEALDSPSVNFNVLKRAKKIGFSDKQIAAAIKSTEVAVRKLREEFKITPFVKQIDTVA 156
Cdd:COG0458  427 GITVIDVFKLSEGRPII---VDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEA 503

                        170       180       190
                 ....*....|....*....|....*....|...
gi 307640723 157 AEWPASTNYLYLTYNGSTHDLEFPGEYVMVLGS 189
Cdd:COG0458  504 GEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 184-262 2.19e-15

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: 75.42  E-value: 2.19e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307640723   184 VMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVIL 262
Cdd:TIGR01369    9 ILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAILP 87
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 184-261 2.54e-11

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 63.45  E-value: 2.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307640723  184 VMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVI 261
Cdd:PRK12815   10 ILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
carB PRK05294
carbamoyl-phosphate synthase large subunit;
184-261 5.70e-11

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 62.42  E-value: 5.70e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307640723  184 VMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVI 261
Cdd:PRK05294   10 ILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
PLN02735 PLN02735
carbamoyl-phosphate synthase
 184-261 4.91e-10

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 59.79  E-value: 4.91e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 307640723  184 VMVLGSGVYRIGSSVEFDWCAVGCLRELRNQGKKTIMVNYNPETVSTDYDMSDRLYFEEISFEVVMDIYNIEHPEGVI 261
Cdd:PLN02735   26 IMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
carB PRK05294
carbamoyl-phosphate synthase large subunit;
8-28 4.99e-04

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 41.24  E-value: 4.99e-04
                          10        20
                  ....*....|....*....|.
gi 307640723    8 MKSVG*VMSIGRSFEEAFQKA 28
Cdd:PRK05294  906 MKSTGEVMGIDRTFGEAFAKA 926
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 5-72 2.36e-03

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: 39.21  E-value: 2.36e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 307640723     5 GSSMKSVG*VMSIGRSFEEAFQKALRMVdenvnGFDPNIKNVNENELREPTDKRMFVLAAALKQ-GYSV 72
Cdd:TIGR01369  903 GPEMKSTGEVMGIGRDLAEAFLKAQLSS-----GNRIPKKGSVLLSVRDKDKEELLDLARKLAEkGYKL 966
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 2-28 5.55e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 38.03  E-value: 5.55e-03
                          10        20
                  ....*....|....*....|....*..
gi 307640723    2 TKIGSSMKSVG*VMSIGRSFEEAFQKA 28
Cdd:PRK12815  900 NTLGPEMKSTGEVMGIDKDLEEALYKG 926
 
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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