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Conserved domains on  [gi|425870583|gb|AFY05269|]
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putative CAD trifunctional protein, partial [Curtonotum helvum]

Protein Classification

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 ...
 1-187 4.82e-101

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: 313.47  E-value: 4.82e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583     1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:TIGR01369  604 DYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIP 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDAVA 160
Cdd:TIGR01369  684 QPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVS 763

                          170       180
                   ....*....|....*....|....*..
gi 425870583   161 ADGEILCMAVSEHVENAGVHSGDATLV 187
Cdd:TIGR01369  764 DGEEVLIPGIMEHIEEAGVHSGDSTCV 790
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-187 4.82e-101

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: 313.47  E-value: 4.82e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583     1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:TIGR01369  604 DYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIP 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDAVA 160
Cdd:TIGR01369  684 QPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVS 763

                          170       180
                   ....*....|....*....|....*..
gi 425870583   161 ADGEILCMAVSEHVENAGVHSGDATLV 187
Cdd:TIGR01369  764 DGEEVLIPGIMEHIEEAGVHSGDSTCV 790
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-187 1.40e-82

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: 253.65  E-value: 1.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQA----KVLGTSPESIDSAENRFKFSRMLDR 76
Cdd:COG0458   45 DYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGGQTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  77 KGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDV 156
Cdd:COG0458  125 LGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEV 204

                        170       180       190
                 ....*....|....*....|....*....|..
gi 425870583 157 DAVA-ADGEILCMAVSEHVENAGVHSGDATLV 187
Cdd:COG0458  205 DVVRdGEDNVIIVGIMEHIEPAGVHSGDSICV 236
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-187 9.02e-81

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 258.87  E-value: 9.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:PRK05294  604 DYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIP 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDAVa 160
Cdd:PRK05294  684 QPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI- 762

                         170       180
                  ....*....|....*....|....*...
gi 425870583  161 ADGE-ILCMAVSEHVENAGVHSGDATLV 187
Cdd:PRK05294  763 CDGEdVLIGGIMEHIEEAGVHSGDSACS 790
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 89-160 2.58e-07

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: 48.84  E-value: 2.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 425870583   89 NLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYP----VVISKFLTEAKEIDVDAVA 160
Cdd:pfam02786  26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
 
Name Accession Description Interval E-value
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-187 4.82e-101

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: 313.47  E-value: 4.82e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583     1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:TIGR01369  604 DYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIP 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDAVA 160
Cdd:TIGR01369  684 QPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVS 763

                          170       180
                   ....*....|....*....|....*..
gi 425870583   161 ADGEILCMAVSEHVENAGVHSGDATLV 187
Cdd:TIGR01369  764 DGEEVLIPGIMEHIEEAGVHSGDSTCV 790
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 1-187 1.40e-82

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: 253.65  E-value: 1.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQA----KVLGTSPESIDSAENRFKFSRMLDR 76
Cdd:COG0458   45 DYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGGQTALNLAVELEEAGIlegvKILGTSPDAIDLAEDRELFKELLDK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  77 KGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDV 156
Cdd:COG0458  125 LGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEV 204

                        170       180       190
                 ....*....|....*....|....*....|..
gi 425870583 157 DAVA-ADGEILCMAVSEHVENAGVHSGDATLV 187
Cdd:COG0458  205 DVVRdGEDNVIIVGIMEHIEPAGVHSGDSICV 236
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-187 9.02e-81

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 258.87  E-value: 9.02e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:PRK05294  604 DYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIP 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDAVa 160
Cdd:PRK05294  684 QPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIVYDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI- 762

                         170       180
                  ....*....|....*....|....*...
gi 425870583  161 ADGE-ILCMAVSEHVENAGVHSGDATLV 187
Cdd:PRK05294  763 CDGEdVLIGGIMEHIEEAGVHSGDSACS 790
PLN02735 PLN02735
carbamoyl-phosphate synthase
 1-184 3.32e-55

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 187.68  E-value: 3.32e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQ-------------QAKVLGTSPESIDSAENR 67
Cdd:PLN02735  624 DYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDR 703

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   68 FKFSRMLDRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKF 147
Cdd:PLN02735  704 ERFNAILNELKIEQPKGGIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKY 783

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 425870583  148 LTEAKEIDVDAVA-ADGEILCMAVSEHVENAGVHSGDA 184
Cdd:PLN02735  784 LSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSGDS 821
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 1-187 9.50e-53

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 180.55  E-value: 9.50e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQAKVLGTSPESIDSAENRFKFSRMLDRKGIL 80
Cdd:PRK12815  605 DYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLP 684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   81 QPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEYPVVISKFLtEAKEIDVDAVa 160
Cdd:PRK12815  685 HVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEPALEAYLAEN--ASQLYPILIDQFI-DGKEYEVDAI- 760

                         170       180
                  ....*....|....*....|....*...
gi 425870583  161 ADGE-ILCMAVSEHVENAGVHSGDATLV 187
Cdd:PRK12815  761 SDGEdVTIPGIIEHIEQAGVHSGDSIAV 788
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 1-187 6.66e-29

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: 112.40  E-value: 6.66e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583     1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQ------QAKVLGTSPESIDSAENRFKFSRML 74
Cdd:TIGR01369   56 DPEMADKVYIEPLTPEAVEKIIEKERPDAILPTFGGQTALNLAVELEESgvlekyGVEVLGTPVEAIKKAEDRELFREAM 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    75 DRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEI 154
Cdd:TIGR01369  136 KEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEI 215

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 425870583   155 DVDAV--AADGEIL--CMavsEHVENAGVHSGDATLV 187
Cdd:TIGR01369  216 EYEVMrdSNDNCITvcNM---ENFDPMGVHTGDSIVV 249
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 6-187 1.58e-27

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 108.13  E-value: 1.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    6 DRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQA------KVLGTSPESIDSAENRFKFSRMLDRKGI 79
Cdd:PRK12815   62 DTVYFEPLTVEFVKRIIAREKPDALLATLGGQTALNLAVKLHEDGIleqygvELLGTNIEAIQKGEDRERFRALMKELGE 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   80 LQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKEIDVDaV 159
Cdd:PRK12815  142 PVPESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYE-V 220

                         170       180       190
                  ....*....|....*....|....*....|
gi 425870583  160 AADGEILCMAVS--EHVENAGVHSGDATLV 187
Cdd:PRK12815  221 MRDRNGNCITVCnmENIDPVGIHTGDSIVV 250
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-187 2.14e-27

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 107.88  E-value: 2.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMDLHRQQA------KVLGTSPESIDSAENRFKFSRML 74
Cdd:PRK05294   57 DPEMADATYIEPITPEFVEKIIEKERPDAILPTMGGQTALNLAVELAESGVlekygvELIGAKLEAIDKAEDRELFKEAM 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   75 DRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLN---AASLVSKeypVVISKFLTEA 151
Cdd:PRK05294  137 KKIGLPVPRSGIAHSMEEALEVAEEIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVErglDLSPVTE---VLIEESLLGW 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 425870583  152 KEIDVDAV--AADGeilCMAVS--EHVENAGVHSGDATLV 187
Cdd:PRK05294  214 KEYEYEVMrdKNDN---CIIVCsiENIDPMGVHTGDSITV 250
PLN02735 PLN02735
carbamoyl-phosphate synthase
 1-187 9.70e-18

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 80.21  E-value: 9.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583    1 DYDMCDRLYFEEISFETVMDVYEMEHCDGIILSMGGQLPNNIAMD------LHRQQAKVLGTSPESIDSAENRFKFSRML 74
Cdd:PLN02735   73 DPETADRTYIAPMTPELVEQVIAKERPDALLPTMGGQTALNLAVAlaesgiLEKYGVELIGAKLDAIKKAEDRELFKQAM 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   75 DRKGILQPRWKELTNLQSAINFCEEVG-YPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYPVVISKFLTEAKE 153
Cdd:PLN02735  153 EKIGLKTPPSGIATTLDECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKE 232

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 425870583  154 IDVDAVA--ADGEILCMAVsEHVENAGVHSGDATLV 187
Cdd:PLN02735  233 YELEVMRdlADNVVIICSI-ENIDPMGVHTGDSITV 267
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 55-172 2.85e-12

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 63.35  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  55 GTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAS 134
Cdd:COG0439   43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 425870583 135 ----LVSKEYPVVISKFLtEAKEIDVDAVAADGEILCMAVSE 172
Cdd:COG0439  123 aeakAGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITR 163
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 89-160 2.58e-07

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: 48.84  E-value: 2.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 425870583   89 NLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLVSKEYP----VVISKFLTEAKEIDVDAVA 160
Cdd:pfam02786  26 TEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFgnpqVLVEKSLKGPKHIEYQVLR 101
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 52-167 3.08e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 46.03  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  52 KVLGTSPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQS--AINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 129
Cdd:PRK12767  97 KVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL 176

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 425870583 130 LNAASlvskeyPVVISKFLtEAKEIDVDA-VAADGEILC 167
Cdd:PRK12767 177 LEYVP------NLIIQEFI-EGQEYTVDVlCDLNGEVIS 208
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 57-166 8.27e-06

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 45.03  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   57 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAASLV 136
Cdd:TIGR00768  79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFEQL 158

                          90       100       110
                  ....*....|....*....|....*....|.
gi 425870583  137 SKEYPV-VISKFLTEAKEIDVDAVAADGEIL 166
Cdd:TIGR00768 159 NGPQNLfLVQEYIKKPGGRDIRVFVVGDEVV 189
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
52-160 1.32e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 44.59  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  52 KVLGTSPESIDSAENRFKFSRMLDRKG--ILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETY 129
Cdd:PRK08654 101 VFIGPSSDVIEAMGSKINAKKLMKKAGvpVLPGTEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDA 180

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 425870583 130 LNAASLVSKEY----PVVISKFLTEAKEIDVDAVA 160
Cdd:PRK08654 181 IESTQSIAQSAfgdsTVFIEKYLEKPRHIEIQILA 215
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 78-179 2.06e-05

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 43.01  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   78 GILQPRWKELTNLQSAINFCEEVGYPCLV---RPSYvlSGAAMNVAYSNQDLETYLNAAslvsKEYPVVISKFLTEAKEI 154
Cdd:pfam02222   4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77

                          90       100
                  ....*....|....*....|....*.
gi 425870583  155 DVDAV-AADGEILCMAVSEHVENAGV 179
Cdd:pfam02222  78 SVLVVrSVDGETAFYPVVETIQEDGI 103
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 69-162 4.03e-04

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 40.20  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583  69 KFSRMLDRKGILQprwkeltnlqsaiNFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEYPVVISKFL 148
Cdd:PRK14570 152 KYDYFLDKEGIKK-------------DIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEA--FKYDLTVVIEKFI 216

                         90
                 ....*....|....
gi 425870583 149 tEAKEIDVDAVAAD 162
Cdd:PRK14570 217 -EAREIECSVIGNE 229
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 77-156 4.48e-04

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 39.22  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870583   77 KGILQPRWKELTNLQSAiNFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYLNAAslVSKEYPVVISKFLtEAKEIDV 156
Cdd:pfam07478  13 VTFTRADWKLNPKEWCA-QVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEA--FQYDEKVLVEEGI-EGREIEC 88
LysX_arch TIGR02144
Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the ...
 57-130 3.76e-03

Lysine biosynthesis enzyme LysX; The family of proteins found in this equivalog include the characterized LysX from Thermus thermophilus, which is part of a well-organized lysine biosynthesis gene cluster. LysX is believed to carry out an ATP-dependent acylation of the amino group of alpha-aminoadipate in the prokaryotic version of the fungal AAA lysine biosynthesis pathway. No species having a sequence in this equivalog contains the elements of the more common diaminopimelate lysine biosythesis pathway, and none has been shown to be a lysine auxotroph. These sequences have mainly recieved the name of the related enzyme, "ribosomal protein S6 modification protein RimK". RimK has been characterized in E. coli, and acts by ATP-dependent condensation of S6 with glutamate residues.


Pssm-ID: 273994 [Multi-domain]  Cd Length: 280  Bit Score: 36.99  E-value: 3.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 425870583   57 SPESIDSAENRFKFSRMLDRKGILQPRWKELTNLQSAINFCEEVGYPCLVRPSYVLSGAAMNVAYSNQDLETYL 130
Cdd:TIGR02144  78 SSHAIEACGDKIFTYLKLAKAGVPTPRTYLAFDREAALKAAEALGYPVVLKPVIGSWGRLVAKVRDRDEAEALL 151
 
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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