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Conserved domains on  [gi|164663810|ref|NP_775913|]
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N-acetylaspartylglutamate synthase A [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 ...
 5-298 1.37e-94

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: 284.24  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  165 FLARDKHHLSDICHLIRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCSLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164663810  241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDY 275
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-298 1.37e-94

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: 284.24  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  165 FLARDKHHLSDICHLIRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCSLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164663810  241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDY 275
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-298 2.01e-54

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: 181.29  E-value: 2.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   5 LWFLTDRRIRedYPQVQILRALRQRcseqdvRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFpDVVLVRVPTPSVQsdsd 84
Cdd:COG0189    4 IAILTDPPDK--DSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189   71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 165 FLARDKHHLSDICHLIR--HDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGK 242
Cdd:COG0189  148 FLVEDEDALESILEALTelGSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEER 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164663810 243 QLAIQVSNILGMDFCGIDlLIMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:COG0189  228 ELALRAAPALGLDFAGVD-LIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADY 282
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-298 3.58e-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: 122.61  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLIRHDVpyLFQ 189
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNEQI--LVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  190 KYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGsF 269
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158

                         170       180
                  ....*....|....*....|....*....
gi 164663810  270 VVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
87-293 1.54e-21

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 93.81  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  87 VLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEplGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG--GAPLVVKLVEGTQGIGVVL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 167 ARDKHHLSDICHLIRH-DVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLA 245
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164663810 246 IQVSNILGMDFCGIDLLIMDDGSFVVcEANANVGFLAFDQACNLDVGG 293
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPLVM-EVNASPGLEGIEKTTGIDIAG 280
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 5-298 1.37e-94

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: 284.24  E-value: 1.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810    5 LWFLTDRRiredypqVQILRALRQRCSEQDVRFRAVLMDQIAVTIVGGHLGLQlnqkalttFPDVVLVRVptpsVQSDSD 84
Cdd:TIGR00768   2 IAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPRALA--------ELDVVIVRI----VSMFRG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:TIGR00768  63 LAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRGV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  165 FLARDKHHLSDICHLIRHDVP----YLFQKYVKESHGKDIRVVVVGGQVIGSMLRCsTDGRMQSNCSLGGVGVKCPLTEQ 240
Cdd:TIGR00768 140 SLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164663810  241 GKQLAIQVSNILGMDFCGIDLLiMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:TIGR00768 219 IEELAIKAAKALGLDVAGVDLL-ESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDY 275
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 5-298 2.01e-54

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: 181.29  E-value: 2.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   5 LWFLTDRRIRedYPQVQILRALRQRcseqdvRFRAVLMDQIAVTIVGGHLGLQLNQKALTTFpDVVLVRVPTPSVQsdsd 84
Cdd:COG0189    4 IAILTDPPDK--DSTKALIEAAQRR------GHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG---- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  85 ITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAV 164
Cdd:COG0189   71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRGV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 165 FLARDKHHLSDICHLIR--HDVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGK 242
Cdd:COG0189  148 FLVEDEDALESILEALTelGSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEER 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164663810 243 QLAIQVSNILGMDFCGIDlLIMDDGSFVVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:COG0189  228 ELALRAAPALGLDFAGVD-LIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADY 282
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 110-298 3.58e-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: 122.61  E-value: 3.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  110 NKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHLIRHDVpyLFQ 189
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNEQI--LVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  190 KYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLAIQVSNILGMDFCGIDLLIMDDGsF 269
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158

                         170       180
                  ....*....|....*....|....*....
gi 164663810  270 VVCEANANVGFLAFDQACNLDVGGIIADY 298
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
87-293 1.54e-21

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 93.81  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  87 VLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEplGYPVVVKSTRGHRGKAVFL 166
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG--GAPLVVKLVEGTQGIGVVL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 167 ARDKHHLSDICHLIRH-DVPYLFQKYVKESHGKDIRVVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVKCPLTEQGKQLA 245
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 164663810 246 IQVSNILGMDFCGIDLLIMDDGSFVVcEANANVGFLAFDQACNLDVGG 293
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPLVM-EVNASPGLEGIEKTTGIDIAG 280
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 91-194 1.75e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 70.68  E-value: 1.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  91 LEKLGCR-LVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDEAEpLGYPVVVKSTRGHRGKAVFLARD 169
Cdd:PRK12767  91 FEEIGVKvLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVND 169

                         90       100
                 ....*....|....*....|....*
gi 164663810 170 KhhlSDICHLIRHDVPYLFQKYVKE 194
Cdd:PRK12767 170 K---EELEFLLEYVPNLIIQEFIEG 191
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 92-279 1.70e-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: 61.04  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  92 EKLGCRlVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDKH 171
Cdd:COG0439   37 EELGLP-GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA---LAFAEEIGYPVVVKPADGAGSRGVRVVRDEE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 172 HLSDICHLIR-------HDVPYLFQKYVKE---------SHGKDIrvvvvggqvigsmlRCSTDGRMQSNCSLGGVG--- 232
Cdd:COG0439  113 ELEAALAEARaeakagsPNGEVLVEEFLEGreysveglvRDGEVV--------------VCSITRKHQKPPYFVELGhea 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164663810 233 ---VKCPLTEQGKQLAIQVSNILGMDFCG--IDLLIMDDGSFVVCEANANVG 279
Cdd:COG0439  179 pspLPEELRAEIGELVARALRALGYRRGAfhTEFLLTPDGEPYLIEINARLG 230
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
58-192 3.76e-07

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 51.47  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  58 LNQKALTTFPDVVLvrvPTpsvqSDSDITVL-RHLEKLGCR-LVNRP--QSILNCINKfWTFQELAG-HGVPMPDTFSYG 132
Cdd:COG3919   68 LLELAERHGPDVLI---PT----GDEYVELLsRHRDELEEHyRLPYPdaDLLDRLLDK-ERFYELAEeLGVPVPKTVVLD 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164663810 133 GHEDFSKMideAEPLGYPVVVKSTRGHR--------GKAVFLARDKHHLSDICHLIR-HDVPYLFQKYV 192
Cdd:COG3919  140 SADDLDAL---AEDLGFPVVVKPADSVGydelsfpgKKKVFYVDDREELLALLRRIAaAGYELIVQEYI 205
PRK12458 PRK12458
glutathione synthetase; Provisional
 89-260 3.64e-05

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 45.40  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  89 RHLEKLGCRLVNRPQSILNCINKFWtFQElaghgvpMPDTFSYGGHedFSKMIDE-----AEPLGYPVVVKSTRGHRGKA 163
Cdd:PRK12458 108 RLAARDGVLVVNDPDGLRIANNKLY-FQS-------FPEEVRPTTH--ISRNKEYireflEESPGDKMILKPLQGSGGQG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 164 VFLARdKHHLSDICHLIRH--DVPYLF-QKYVKESHGKDIR------VVVVGGQVIGSMLRCSTDGRMQSNCSLGGVGVK 234
Cdd:PRK12458 178 VFLIE-KSAQSNLNQILEFysGDGYVIaQEYLPGAEEGDVRilllngEPLERDGHYAAMRRVPAGGDVRSNVHAGGSVVK 256

                        170       180
                 ....*....|....*....|....*....
gi 164663810 235 CPLTEQGKQLAIQVSNIL---GMDFCGID 260
Cdd:PRK12458 257 HTLTKEELELCEAIRPKLvrdGLFFVGLD 285
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 108-275 4.86e-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: 43.14  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  108 CINKFWTFQELAGHGVPMPDTFSygghedfskmIDEAEPLGYPVVVKSTRGHRGKAVFLARDKHHLSDICHlirhdvPYL 187
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQ----------AEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE------NVL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  188 FQKYVKESH--------GKDIRvvvvggqvIGSMLRCSTDGRMQSNCSLGGVgVKCPLTEQGK--QLAIQV----SNILG 253
Cdd:pfam02655  65 VQEFIEGEPlsvsllsdGEKAL--------PLSVNRQYIDNGGSGFVYAGNV-TPSRTELKEEiiELAEEVveclPGLRG 135

                         170       180
                  ....*....|....*....|..
gi 164663810  254 MDfcGIDLLIMDDGSFVVcEAN 275
Cdd:pfam02655 136 YV--GVDLVLKDNEPYVI-EVN 154
YheC COG5891
Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, ...
 66-286 1.56e-04

Spore coat protein YheC/YheD, ATP-grasp superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444593 [Multi-domain]  Cd Length: 400  Bit Score: 43.44  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  66 FPDVVLVRVPTPSVQSDSDI-TVLRHLEKL-GCRLVNRpqsilNCINK------FWTFQELAGHgvpMPDTFSYGGHEDF 137
Cdd:COG5891  107 LPDVIYNRIPSRKAERSEKVkELREKLKKRpGIPFFNP-----RFFNKwevyqlLSKDPRLRPY---LPETELLTSPEDL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 138 SKMIDEaeplgYP-VVVKSTRGHRGKAVF-LARDK------------------HHLSDICHLIR---HDVPYLFQKYV-- 192
Cdd:COG5891  179 LEFLKR-----YKsVYLKPVNGSLGRGIIrIEKKGdgyllryrrkkrnvrrrfSSLDELLAFLRrllRRKRYIIQQGIpl 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 193 KESHGK--DIRvvvvggqvigsML----------------RCSTDGRMQSNCSLGG--------------VGVKCPLTEQ 240
Cdd:COG5891  254 ATIDGRpfDFR-----------VLvqkngrgewvvtgivaRIAGPGSITTNLSGGGtalpleellrrafgDSKAEEILQK 322

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164663810 241 GKQLAIQVSNIL-----GMDFCGIDLLIMDDGSFVVCEANANVGFLAFDQA 286
Cdd:COG5891  323 LERIALEIARALeesygGLGELGIDLGIDRDGKIWLLEVNSKPGRSIFDEP 373
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 84-175 2.34e-04

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 43.12  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  84 DITVLRHLEKLGCRLVNRPQSILNCINKFWTFQELAGHGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTRGH---R 160
Cdd:PLN02948  95 DVDTLEALEKQGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE---FMEIDDLESAEKAGDLFGYPLMLKSRRLAydgR 171

                         90
                 ....*....|....*
gi 164663810 161 GKAVflARDKHHLSD 175
Cdd:PLN02948 172 GNAV--AKTEEDLSS 184
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 96-288 1.80e-03

Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.


Pssm-ID: 405145 [Multi-domain]  Cd Length: 278  Bit Score: 39.63  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810   96 CRLVNRPQSILNCINKFWTFQELAGHGVPMPDTFSYGGHEDFSKMIDE-AEPLGYPVVVKSTRGHRGK-AVFLARD---- 169
Cdd:pfam14397   7 IRKYNPRALYPLVDDKLKFKQLALRAGLPVPKLYGVISIGHDISRLDAfVRSLPPGFVIKPAKGSGGKgILVITRRgdqd 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  170 --------------KHHlsdICHLIRHDVPYLFQKYVkESHGK----------DIR----VVVVGGQVIGSMLRCSTDGR 221
Cdd:pfam14397  87 yfkssgcrilldelKRH---VSSLGGKPDVALVEERI-VQDPVfaklspesvnTIRvitfLLDNGVPVMPAMLRLGTGAS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810  222 MQSNCSLGGVGVK--------CPLTEQGKQ----------------------------LAIQVS-NILGMDFCGIDLLIM 264
Cdd:pfam14397 163 LVDNLHQGGVGVGidlatgvlFKPALQAVQygepiehhpdtgvkfrgfqipnwdqileLAAECAqTLPGLGYVGWDIVID 242

                         250       260
                  ....*....|....*....|....
gi 164663810  265 DDGSFVVCEANANVGfLAFDQACN 288
Cdd:pfam14397 243 ENGGPLLLELNARPG-LGIFQIAN 265
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 108-280 2.64e-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: 39.32  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 108 CINKFWTFQELAGHGVPMPD--TFSYGGHEDFSKMIDEaepLGYPVVVKSTRGHRGKAVFLARDKHHLSD-ICHLIRHDV 184
Cdd:COG1181   93 AMDKALTKRVLAAAGLPTPPyvVLRRGELADLEAIEEE---LGLPLFVKPAREGSSVGVSKVKNAEELAAaLEEAFKYDD 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164663810 185 PYLFQKYVKeshGKDIrvvvvggqvigsmlrcstdgrmqsNCS-LGGVGVK----------------------------C 235
Cdd:COG1181  170 KVLVEEFID---GREV------------------------TVGvLGNGGPRalppieivpengfydyeakytdggteyiC 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 164663810 236 P------LTEQGKQLAIQVSNILGM-DFCGIDLLIMDDGSFVVCEANANVGF 280
Cdd:COG1181  223 ParlpeeLEERIQELALKAFRALGCrGYARVDFRLDEDGEPYLLEVNTLPGM 274
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 121-175 2.81e-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: 2.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164663810  121 HGVPMPDtfsYGGHEDFSKMIDEAEPLGYPVVVKSTR-GHRGKAVFLARDKHHLSD 175
Cdd:pfam02222   3 LGLPTPR---FMAAESLEELIEAGQELGYPCVVKARRgGYDGKGQYVVRSEADLPQ 55
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 110-166 7.31e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 38.60  E-value: 7.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 164663810 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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