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Conserved domains on  [gi|578798968|ref|XP_006710648|]
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N-acetylaspartylglutamate synthase A isoform X2 [Homo sapiens]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 106900)

ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CPSase_L_D2 super family cl17255
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 5-191 1.13e-50

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.


The actual alignment was detected with superfamily member TIGR00768:

Pssm-ID: 473076 [Multi-domain]  Cd Length: 276  Bit Score: 165.60  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578798968  165 FLARDKHHLSDICHLIRHDVP----YLFQKW 191
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEY 170
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-191 1.13e-50

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: 165.60  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578798968  165 FLARDKHHLSDICHLIRHDVP----YLFQKW 191
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEY 170
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-191 4.79e-26

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 101.94  E-value: 4.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968   5 LWFLTDRRIRedYPQVQILRALRQRcseqdvRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFpDVVLVRVPTPSVQsdsd 84
Cdd:COG0189    4 IAILTDPPDK--DSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189   71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                        170       180
                 ....*....|....*....|....*....
gi 578798968 165 FLARDKHHLSDICHLIR--HDVPYLFQKW 191
Cdd:COG0189  148 FLVEDEDALESILEALTelGSEPVLVQEF 176
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 91-190 6.18e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 66.45  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  91 LEKLGCR-LVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARD 169
Cdd:PRK12767  91 FEEIGVKvLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVND 169

                         90       100
                 ....*....|....*....|.
gi 578798968 170 KhhlSDICHLIRHDVPYLFQK 190
Cdd:PRK12767 170 K---EELEFLLEYVPNLIIQE 187
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-176 1.09e-07

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 50.19  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798968  110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDI 176
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQT 68
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-191 1.13e-50

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: 165.60  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 578798968  165 FLARDKHHLSDICHLIRHDVP----YLFQKW 191
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEY 170
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-191 4.79e-26

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 101.94  E-value: 4.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968   5 LWFLTDRRIRedYPQVQILRALRQRcseqdvRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFpDVVLVRVPTPSVQsdsd 84
Cdd:COG0189    4 IAILTDPPDK--DSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189   71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                        170       180
                 ....*....|....*....|....*....
gi 578798968 165 FLARDKHHLSDICHLIR--HDVPYLFQKW 191
Cdd:COG0189  148 FLVEDEDALESILEALTelGSEPVLVQEF 176
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 91-190 6.18e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 66.45  E-value: 6.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  91 LEKLGCR-LVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARD 169
Cdd:PRK12767  91 FEEIGVKvLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVND 169

                         90       100
                 ....*....|....*....|.
gi 578798968 170 KhhlSDICHLIRHDVPYLFQK 190
Cdd:PRK12767 170 K---EELEFLLEYVPNLIIQE 187
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 92-199 3.14e-10

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: 58.35  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  92 EKLGCRlVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDKH 171
Cdd:COG0439   37 EELGLP-GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA---LAFAEEIGYPVVVKPADGAGSRGVRVVRDEE 112

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 578798968 172 HLSDICHLIR-------HDVPYLFQKW-RGRQVSAD 199
Cdd:COG0439  113 ELEAALAEARaeakagsPNGEVLVEEFlEGREYSVE 148
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-176 1.09e-07

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 50.19  E-value: 1.09e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578798968  110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDI 176
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQT 68
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
58-191 1.20e-05

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 45.30  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  58 LNQKALTTFPDVVLvrvPTpsvqSDSDITVL-RHLEKLGCR-LVNRP--QSILNCINKfWTFQELAG-HGVPMPDTFSYG 132
Cdd:COG3919   68 LLELAERHGPDVLI---PT----GDEYVELLsRHRDELEEHyRLPYPdaDLLDRLLDK-ERFYELAEeLGVPVPKTVVLD 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578798968 133 GHEDFSKMideAEPLGYPVVVKSTRGHR--------GKAVFLARDKHHLSDICHLIR-HDVPYLFQKW 191
Cdd:COG3919  140 SADDLDAL---AEDLGFPVVVKPADSVGydelsfpgKKKVFYVDDREELLALLRRIAaAGYELIVQEY 204
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 84-175 6.62e-05

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 43.12  E-value: 6.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  84 DITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTRGH---R 160
Cdd:PLN02948  95 DVDTLEALEKQGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE---FMEIDDLESAEKAGDLFGYPLMLKSRRLAydgR 171

                         90
                 ....*....|....*
gi 578798968 161 GKAVflARDKHHLSD 175
Cdd:PLN02948 172 GNAV--AKTEEDLSS 184
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 108-199 2.36e-04

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 40.06  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  108 CINKFWTFQELAGHGVPMPDTFSygghedfskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHlirhdvPYL 187
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQ----------AEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE------NVL 64

                          90
                  ....*....|...
gi 578798968  188 FQKW-RGRQVSAD 199
Cdd:pfam02655  65 VQEFiEGEPLSVS 77
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
87-171 1.12e-03

30S ribosomal protein S6--L-glutamate ligase;


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 39.11  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578798968  87 VLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEplGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG--GAPLVVKLVEGTQGIGVVL 153


                 ....*
gi 578798968 167 ARDKH 171
Cdd:PRK10446 154 AETRQ 158
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 108-170 1.20e-03

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 38.93  E-value: 1.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578798968 108 CINKFWTFQELAGHGVPMPD--TFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAVFLARDK 170
Cdd:COG1181   93 AMDKALTKRVLAAAGLPTPPyvVLRRGELADLEAIEEE---LGLPLFVKPAREGSSVGVSKVKNA 154
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 121-175 1.20e-03

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: 38.39  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578798968  121 HGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTR-GHRGKAVFLARDKHHLSD 175
Cdd:pfam02222   3 LGLPTPR---FMAAESLEELIEAGQELGYPCVVKARRgGYDGKGQYVVRSEADLPQ 55
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 110-166 2.50e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 38.60  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578798968 110 NKFWTFQELAGHGVPMPDtfsygGH--EDFSKMIDEAEPLGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPE-----GRvvTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTV 267
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 108-158 6.57e-03

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 36.63  E-value: 6.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578798968 108 CINKFWTFQELAGHGVPMPDTFSYGGHEDFskmIDEAEPLGYPVVVKSTRG 158
Cdd:PRK01372  96 AMDKLRTKLVWQAAGLPTPPWIVLTREEDL---LAAIDKLGLPLVVKPARE 143
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
 122-177 8.47e-03

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: 36.13  E-value: 8.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578798968  122 GVPMPDTFSyGGHEDFSKMIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDIC 177
Cdd:pfam02786  13 GVPTVPGTA-GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELF 67
 
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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