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Conserved domains on  [gi|40254319|ref|NP_808240|]
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N-acetylaspartylglutamate synthase A [Mus musculus]

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 ...
 5-299 2.11e-90

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: 273.07  E-value: 2.11e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319     5 VWLLTDRlIRedypqvQILRALRQRCSEQDVGFRAVFLDQIAVTvvgghLGLQLSQKPlttFPDVVVVRVstpsVQSDSE 84
Cdd:TIGR00768   2 IAILYDR-IR------LDEKMLKEAAEELGIDYKVVTPPAINLT-----FNEGPRALA---ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319    85 ITILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   165 FLARDKHHLSDICHLVRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCFLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40254319   241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFTVCEANANVGFLAFDQACNLDVGAIIADYA 299
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-299 2.11e-90

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: 273.07  E-value: 2.11e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319     5 VWLLTDRlIRedypqvQILRALRQRCSEQDVGFRAVFLDQIAVTvvgghLGLQLSQKPlttFPDVVVVRVstpsVQSDSE 84
Cdd:TIGR00768   2 IAILYDR-IR------LDEKMLKEAAEELGIDYKVVTPPAINLT-----FNEGPRALA---ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319    85 ITILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   165 FLARDKHHLSDICHLVRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCFLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40254319   241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFTVCEANANVGFLAFDQACNLDVGAIIADYA 299
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-304 3.08e-55

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: 183.22  E-value: 3.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   5 VWLLTDRliREDYPQVQILRALRQRcseqdvGFRAVFLDQIAVTVVGGHLGLQLSQKPLTTFpDVVVVRVSTPSVQsdse 84
Cdd:COG0189   4 IAILTDP--PDKDSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  85 ITILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189  71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319 165 FLARDKHHLSDICHLVR--HDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGK 242
Cdd:COG0189 148 FLVEDEDALESILEALTelGSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEER 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40254319 243 QLAIQVSNILGMDFCGIDlLIMDDGSFTVCEANANVGFLAFDQACNLDVGAIIADYAMSLLP 304
Cdd:COG0189 228 ELALRAAPALGLDFAGVD-LIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAA 288
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-298 5.53e-33

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: 121.84  E-value: 5.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLVRHDVpyLFQ 189
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNEQI--LVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   190 KYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGsF 269
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158

                         170       180
                  ....*....|....*....|....*....
gi 40254319   270 TVCEANANVGFLAFDQACNLDVGAIIADY 298
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
87-291 3.46e-20

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 89.96  E-value: 3.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   87 ILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEplGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG--GAPLVVKLVEGTQGIGVVL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  167 ARDKHHLSDICHLVRH-DVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGKQLA 245
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 40254319  246 IQVSNILGMDFCGIDLLIMDDGSFtVCEANANVGFLAFDQACNLDV 291
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPL-VMEVNASPGLEGIEKTTGIDI 278
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-299 2.11e-90

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: 273.07  E-value: 2.11e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319     5 VWLLTDRlIRedypqvQILRALRQRCSEQDVGFRAVFLDQIAVTvvgghLGLQLSQKPlttFPDVVVVRVstpsVQSDSE 84
Cdd:TIGR00768   2 IAILYDR-IR------LDEKMLKEAAEELGIDYKVVTPPAINLT-----FNEGPRALA---ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319    85 ITILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   165 FLARDKHHLSDICHLVRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCFLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 40254319   241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFTVCEANANVGFLAFDQACNLDVGAIIADYA 299
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-304 3.08e-55

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: 183.22  E-value: 3.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   5 VWLLTDRliREDYPQVQILRALRQRcseqdvGFRAVFLDQIAVTVVGGHLGLQLSQKPLTTFpDVVVVRVSTPSVQsdse 84
Cdd:COG0189   4 IAILTDP--PDKDSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  85 ITILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189  71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319 165 FLARDKHHLSDICHLVR--HDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGK 242
Cdd:COG0189 148 FLVEDEDALESILEALTelGSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEER 227

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40254319 243 QLAIQVSNILGMDFCGIDlLIMDDGSFTVCEANANVGFLAFDQACNLDVGAIIADYAMSLLP 304
Cdd:COG0189 228 ELALRAAPALGLDFAGVD-LIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAA 288
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-298 5.53e-33

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: 121.84  E-value: 5.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLVRHDVpyLFQ 189
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNEQI--LVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   190 KYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGsF 269
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158

                         170       180
                  ....*....|....*....|....*....
gi 40254319   270 TVCEANANVGFLAFDQACNLDVGAIIADY 298
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
87-291 3.46e-20

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 89.96  E-value: 3.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   87 ILRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEplGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG--GAPLVVKLVEGTQGIGVVL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  167 ARDKHHLSDICHLVRH-DVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGKQLA 245
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 40254319  246 IQVSNILGMDFCGIDLLIMDDGSFtVCEANANVGFLAFDQACNLDV 291
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPL-VMEVNASPGLEGIEKTTGIDI 278
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 81-194 8.96e-14

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 71.45  E-value: 8.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   81 SDSEITIL-RH---LEKLGCR-LVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKS 155
Cdd:PRK12767  77 IDPELPLLaQNrdrFEEIGVKvLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGE-LQFPLFVKP 155

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 40254319  156 TRGHRGKAVFLARDKhhlSDICHLVRHDVPYLFQKYVKE 194
Cdd:PRK12767 156 RDGSASIGVFKVNDK---EELEFLLEYVPNLIIQEFIEG 191
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 92-279 4.08e-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: 59.89  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  92 EKLGCRlVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDK- 170
Cdd:COG0439  37 EELGLP-GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA---LAFAEEIGYPVVVKPADGAGSRGVRVVRDEe 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319 171 ---HHLSDIC---HLVRHDVPYLFQKYVKE---------SHGKDIrvvvvggqvigsmlRCSTDGRMQSNCFLGGVG--- 232
Cdd:COG0439 113 eleAALAEARaeaKAGSPNGEVLVEEFLEGreysveglvRDGEVV--------------VCSITRKHQKPPYFVELGhea 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 40254319 233 ---VKCPLTEQGKQLAIQVSNILGMDFCG--IDLLIMDDGSFTVCEANANVG 279
Cdd:COG0439 179 pspLPEELRAEIGELVARALRALGYRRGAfhTEFLLTPDGEPYLIEINARLG 230
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
110-192 6.70e-06

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 47.62  E-value: 6.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319 110 NKfWTFQELAG-HGVPMPDTFSYGGHEDFSKMideAEPLGYPVVVKSTRGHR--------GKAVFLARDKHHLSDICH-L 179
Cdd:COG3919 117 DK-ERFYELAEeLGVPVPKTVVLDSADDLDAL---AEDLGFPVVVKPADSVGydelsfpgKKKVFYVDDREELLALLRrI 192

                        90
                ....*....|...
gi 40254319 180 VRHDVPYLFQKYV 192
Cdd:COG3919 193 AAAGYELIVQEYI 205
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 108-267 3.88e-05

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: 43.53  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   108 CINKFWTFQELAGHGVPMPDTFSygghedfskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHlvrhdvPYL 187
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQ----------AEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE------NVL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   188 FQKYVKESH--------GKDIRvvvvggqvIGSMLRCSTDGRMQSNCFLGGVgVKCPLTEQGK--QLAIQV----SNILG 253
Cdd:pfam02655  65 VQEFIEGEPlsvsllsdGEKAL--------PLSVNRQYIDNGGSGFVYAGNV-TPSRTELKEEiiELAEEVveclPGLRG 135

                         170
                  ....*....|....
gi 40254319   254 MDfcGIDLLIMDDG 267
Cdd:pfam02655 136 YV--GVDLVLKDNE 147
PRK12458 PRK12458
glutathione synthetase; Provisional
 62-260 1.01e-04

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 43.86  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   62 PLTTFpDVVVVRvSTPSVQSDS-------EITILRHLEKLGCRLVNRPQSILNCINKFWtFQElaghgvpMPDTFSYGGH 134
Cdd:PRK12458  76 PLAGF-DVIFLR-ANPPLDPLArnwadsvGIAFGRLAARDGVLVVNDPDGLRIANNKLY-FQS-------FPEEVRPTTH 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  135 edFSKMIDE-----AEPLGYPVVVKSTRGHRGKAVFLARdKHHLSDICHLVRH--DVPYLF-QKYVKESHGKDIR----- 201
Cdd:PRK12458 146 --ISRNKEYireflEESPGDKMILKPLQGSGGQGVFLIE-KSAQSNLNQILEFysGDGYVIaQEYLPGAEEGDVRillln 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40254319  202 -VVVVGGQVIGSMLRCSTDGRMQSNCFLGGVGVKCPLTEQGKQLAIQVSNIL---GMDFCGID 260
Cdd:PRK12458 223 gEPLERDGHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLD 285
PRK05246 PRK05246
glutathione synthetase; Provisional
 62-298 4.45e-04

glutathione synthetase; Provisional


Pssm-ID: 235371 [Multi-domain]  Cd Length: 316  Bit Score: 41.62  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   62 PLTTFpDVVVVRVSTPSvqsDSE-IT---ILRHLEKLGCRLVNRPQSILNCINKFWT--FQELaghgvpMPDT------- 128
Cdd:PRK05246  76 PLADF-DVILMRKDPPF---DMEyIYatyLLERAERPGTLVVNKPQSLRDANEKLFTlwFPEL------MPPTlvtrdka 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  129 ----FsYGGHEDfskmideaeplgypVVVKSTRGHRGKAVF-LARDKHHLSDICHLVRHD--VPYLFQKYVKE-SHGkDI 200
Cdd:PRK05246 146 eiraF-RAEHGD--------------IILKPLDGMGGAGIFrVKADDPNLGSILETLTEHgrEPVMAQRYLPEiKEG-DK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319  201 RVVvvggqvigsML----------RCSTDGRMQSNCFLGGVGVKCPLTEQGKQLAIQVSNIL---GMDFCGIDLLimdDG 267
Cdd:PRK05246 210 RIL---------LVdgepvgyalaRIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELkerGLIFVGIDVI---GD 277

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 40254319  268 SFTvcEanANV----GFLAFDQACNLDVGAIIADY 298
Cdd:PRK05246 278 YLT--E--INVtsptGIREIERLTGVDIAGMLWDA 308
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 88-175 6.20e-04

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 41.58  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40254319   88 LRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTRGH---RGKAV 164
Cdd:PLN02948  99 LEALEKQGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE---FMEIDDLESAEKAGDLFGYPLMLKSRRLAydgRGNAV 175

                         90
                 ....*....|.
gi 40254319  165 flARDKHHLSD 175
Cdd:PLN02948 176 --AKTEEDLSS 184
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 121-175 2.71e-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: 2.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 40254319   121 HGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTR-GHRGKAVFLARDKHHLSD 175
Cdd:pfam02222   3 LGLPTPR---FMAAESLEELIEAGQELGYPCVVKARRgGYDGKGQYVVRSEADLPQ 55
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 108-170 3.30e-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: 3.30e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40254319 108 CINKFWTFQELAGHGVPMPD--TFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAVFLARDK 170
Cdd:COG1181  93 AMDKALTKRVLAAAGLPTPPyvVLRRGELADLEAIEEE---LGLPLFVKPAREGSSVGVSKVKNA 154
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 110-166 7.17e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 38.60  E-value: 7.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 40254319  110 NKFWTFQELAGHGVPMPDtfsygGH--EDFSKMIDEAEPLGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK14016 214 DKELTKRLLAAAGVPVPE-----GRvvTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTV 267
 
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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