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Conserved domains on  [gi|166977476|sp|A7ZYF5|]
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RecName: Full=Ribosomal protein bS6--L-glutamate ligase; AltName: Full=Poly-alpha-glutamate synthase; AltName: Full=Ribosomal protein bS6 modification protein

Protein Classification

RimK family alpha-L-glutamate ligase( domain architecture ID 11484731)

RimK family alpha-L-glutamate ligase, similar to Escherichia coli RimK which can catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected Glu residues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
1-300 0e+00

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


:

Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 601.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
 
Name Accession Description Interval E-value
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
1-300 0e+00

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 601.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-286 4.80e-122

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: 350.49  E-value: 4.80e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476    2 KIAILSRDGTLySCKRLREAAIQRGHLVEILDPLSCYMNINPaassihyKGRKLPHFDAVIPRIgtAITFYGTAALRQFE 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   82 MLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768  71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  162 SVIDAFRGLNA---HILVQEYIKEAQGCDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGAASVASITPQEREIAIKAAR 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 166977476  239 TMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-290 2.57e-112

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: 326.13  E-value: 2.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASsiHYKGRKLPHFDAVIPRIGTaiTFYGTAALRQF 80
Cdd:COG0189    2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189   78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 161 ESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:COG0189  157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 166977476 240 MALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHA 290
Cdd:COG0189  237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARA 287
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 97-286 8.04e-104

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: 300.96  E-value: 8.04e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   97 ARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  176 VQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRG 255
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 166977476  256 PLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
2-287 2.60e-49

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 165.49  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   2 KIAILSRDGTLYSCKRLREAAIQRGhlveiLDPLscYMNINPAASSIH------YKGRKLPHFDAVIPRIGTAITFYGTA 75
Cdd:NF040720   1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  76 ----ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720  74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQ 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 166977476 229 EREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
 
Name Accession Description Interval E-value
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
1-300 0e+00

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 601.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-286 4.80e-122

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: 350.49  E-value: 4.80e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476    2 KIAILSRDGTLySCKRLREAAIQRGHLVEILDPLSCYMNINPaassihyKGRKLPHFDAVIPRIgtAITFYGTAALRQFE 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRI--VSMFRGLAVLRYLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   82 MLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768  71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  162 SVIDAFRGLNA---HILVQEYIKEAQGCDIRCLVVGDEVVAAIERRaKEGDFRSNLHRGGAASVASITPQEREIAIKAAR 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 166977476  239 TMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-290 2.57e-112

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: 326.13  E-value: 2.57e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASsiHYKGRKLPHFDAVIPRIGTaiTFYGTAALRQF 80
Cdd:COG0189    2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189   78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 161 ESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:COG0189  157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 166977476 240 MALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHA 290
Cdd:COG0189  237 LGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEARA 287
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 97-286 8.04e-104

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: 300.96  E-value: 8.04e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   97 ARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  176 VQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRG 255
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 166977476  256 PLVMEVNASPGLEGIEKTTGIDIAGKMIRWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
Rimk_N pfam18030
RimK PreATP-grasp domain; This is the N-terminal domain found in Escherichia coli RimK ...
 1-94 4.29e-57

RimK PreATP-grasp domain; This is the N-terminal domain found in Escherichia coli RimK proteins (Ribosomal protein S6-L-glutamate ligase). This domain precedes the ATP-grasp domain pfam08443.


Pssm-ID: 465621 [Multi-domain]  Cd Length: 94  Bit Score: 178.82  E-value: 4.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476    1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80
Cdd:pfam18030   1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80

                          90
                  ....*....|....
gi 166977476   81 EMLGSYPLNESVAI 94
Cdd:pfam18030  81 EMMGVFSLNSSQAI 94
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
2-287 2.60e-49

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 165.49  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   2 KIAILSRDGTLYSCKRLREAAIQRGhlveiLDPLscYMNINPAASSIH------YKGRKLPHFDAVIPRIGTAITFYGTA 75
Cdd:NF040720   1 KIGIIVTDRNDWTANALIRACEKKD-----IDPV--LIDLSKIEVSIGsdikfkYGKINLLDLDAIFVRDIGAGSNEGVS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  76 ----ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVVKLVEGTQGIGV 151
Cdd:NF040720  74 frfdVLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 152 VL---AETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQ 228
Cdd:NF040720 152 VRiknGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEE 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 166977476 229 EREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIE 287
Cdd:NF040720 232 QEELAIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKIIDYII 290
PRK12458 PRK12458
glutathione synthetase; Provisional
 88-288 3.07e-21

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 92.01  E-value: 3.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  88 LNESVAIARARDKLRSMQLlarQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAET--RQAAESVID 165
Cdd:PRK12458 118 VNDPDGLRIANNKLYFQSF---PEEVRPTTHISRNKEYIREFLEESPGDKMILKPLQGSGGQGVFLIEKsaQSNLNQILE 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 166 AFRGLNaHILVQEYIKEAQGCDIRCLVV------GDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAART 239
Cdd:PRK12458 195 FYSGDG-YVIAQEYLPGAEEGDVRILLLngepleRDGHYAAMRRVPAGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPK 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 166977476 240 MALD---VAGVDILranrGPLVMEVNA-SP-GLEGIEKTTGIDIAGKMIRWIER 288
Cdd:PRK12458 274 LVRDglfFVGLDIV----GDKLVEVNVfSPgGLTRINKLNKIDFVEDIIEALER 323
PRK05246 PRK05246
glutathione synthetase; Provisional
 174-288 1.27e-17

glutathione synthetase; Provisional


Pssm-ID: 235371 [Multi-domain]  Cd Length: 316  Bit Score: 81.30  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 174 ILVQEYIKEAQGCDIRCLVVGDEVV-AAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMA---LDVAGVDI 249
Cdd:PRK05246 195 VMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLAAGGRGEATPLTERDREICAAIGPELKergLIFVGIDV 274

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 166977476 250 LranrGPLVMEVN-ASP-GLEGIEKTTGIDIAGKMIRWIER 288
Cdd:PRK05246 275 I----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEA 311
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 91-267 4.26e-17

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 81.36  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  91 SVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 170 LNAHILVQEYIKeaqGCDIRCLVVGDEVVAAIERRAKE--GDFRS----------------------------------- 212
Cdd:PRK14016 285 ESSDVIVERYIP---GKDHRLLVVGGKLVAAARREPPHviGDGKHtirelieivnqdprrgeghekpltkiklddialle 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 213 ------------------------NLHRGGAAS--VASITPQEREIAIKAARTMALDVAGVDI--------LRANRGpLV 258
Cdd:PRK14016 362 lakqgytldsvppkgekvylrrnaNLSTGGTAIdvTDEVHPENAAIAERAAKIIGLDIAGVDVvcediskpLEEQGG-AI 440


                 ....*....
gi 166977476 259 MEVNASPGL 267
Cdd:PRK14016 441 VEVNAAPGL 449
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 58-284 6.12e-14

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: 70.29  E-value: 6.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  58 FDAVIPriGTAITFYGTAALRqfEMLGsYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaP 137
Cdd:COG0439   18 IDAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-P 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 138 LVVKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYIkEAQGCDIRCLVVGDEVV-AAIERRAKEGDF 210
Cdd:COG0439   92 VVVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFL-EGREYSVEGLVRDGEVVvCSITRKHQKPPY 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 211 RsnLHRGGAASvASITPQEREIAIKAARTmALDVAGVD--------ILRANRGPLVMEVNASPGLEGI----EKTTGIDI 278
Cdd:COG0439  171 F--VELGHEAP-SPLPEELRAEIGELVAR-ALRALGYRrgafhtefLLTPDGEPYLIEINARLGGEHIppltELATGVDL 246


                 ....*.
gi 166977476 279 AGKMIR 284
Cdd:COG0439  247 VREQIR 252
GSH-S_ATP pfam02955
Prokaryotic glutathione synthetase, ATP-grasp domain;
139-275 1.74e-12

Prokaryotic glutathione synthetase, ATP-grasp domain;


Pssm-ID: 427078 [Multi-domain]  Cd Length: 175  Bit Score: 64.50  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  139 VVKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYIKEAQGCDIRCLVVGDEVV-AAIERRAKEGDFRSNLH 215
Cdd:pfam02955  35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166977476  216 RGGAASVASITPQEREIAIKAARTMA---LDVAGVDILranrGPLVMEVN-ASP-GLEGIEKTTG 275
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLKergLFFVGLDVI----GDYLTEINvTSPtGIREIERLTG 175
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 80-267 5.62e-12

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: 65.13  E-value: 5.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  80 FEML-----GSYPLnesvAIARARDKLRSMQLLARQGIDLPvTGIAHSPDDTSDLIDMVG--GAPLVVKLV-EGTqGIGV 151
Cdd:COG1181   75 LELLgipytGSGVL----ASALAMDKALTKRVLAAAGLPTP-PYVVLRRGELADLEAIEEelGLPLFVKPArEGS-SVGV 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 152 VLAETRQAAESVIDAFRGLNAHILVQEYIKeaqGCDIRCLVVGDEVVAA---IERRAKEG--DFRSNLHRGGAASV--AS 224
Cdd:COG1181  149 SKVKNAEELAAALEEAFKYDDKVLVEEFID---GREVTVGVLGNGGPRAlppIEIVPENGfyDYEAKYTDGGTEYIcpAR 225

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 166977476 225 ITPQE----REIAIKAARtmALDVAG---VD-ILRANRGPLVMEVNASPGL 267
Cdd:COG1181  226 LPEELeeriQELALKAFR--ALGCRGyarVDfRLDEDGEPYLLEVNTLPGM 274
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 99-267 2.37e-09

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 57.04  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  99 DKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILVQ 177
Cdd:PRK01372  98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLG-LPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLVE 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 178 EYIKeaqGCDIRCLVVGDEVVAAIERRAKEG--DFRSNLHRGGAASV------ASITPQEREIAIKAARtmALDVAG--- 246
Cdd:PRK01372 176 KYIK---GRELTVAVLGGKALPVIEIVPAGEfyDYEAKYLAGGTQYIcpaglpAEIEAELQELALKAYR--ALGCRGwgr 250

                        170       180
                 ....*....|....*....|..
gi 166977476 247 VD-ILRANRGPLVMEVNASPGL 267
Cdd:PRK01372 251 VDfMLDEDGKPYLLEVNTQPGM 272
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 93-284 6.19e-09

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 56.78  E-value: 6.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDmvGGA-PLVVKLVEGTQGIGVVLAETRQAA-ESVIDAFRGL 170
Cdd:PRK02186 101 AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALD--GLTyPVVVKPRMGSGSVGVRLCASVAEAaAHCAALRRAG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 171 NAHILVQEYIKEAQ-GCDIRCLVVGDEVVAAIERR-AKEGDFRSNLHRGGAASVAsitPQEREIAIKAARtmALDVAG-- 246
Cdd:PRK02186 179 TRAALVQAYVEGDEySVETLTVARGHQVLGITRKHlGPPPHFVEIGHDFPAPLSA---PQRERIVRTVLR--ALDAVGya 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 166977476 247 -----VDILRANRGPLVMEVNasPGLEG------IEKTTGIDIAGKMIR 284
Cdd:PRK02186 254 fgpahTELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVID 300
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 57-263 5.77e-08

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 53.35  E-value: 5.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  57 HFDAVIPRIGTAITFYgtAALRQ-FEMLGSYPLNESVA-IARARDKLRSMQLLARQGIDLPVTGIAHSPDDTS-DLIDMV 133
Cdd:PRK12767  69 KIDLLIPLIDPELPLL--AQNRDrFEEIGVKVLVSSKEvIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKaALAKGE 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 134 GGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrgLNAHILVQEYIKEAQ-GCDIRCLVVGdEVVAAIERRakegdfRS 212
Cdd:PRK12767 147 LQFPLFVKPRDGSASIGVFKVNDKEELEFLLE----YVPNLIIQEFIEGQEyTVDVLCDLNG-EVISIVPRK------RI 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 166977476 213 NLhRGGAASVASITPQER--EIAIKAARtmALDVAG---VDILRANRGPLVMEVNA 263
Cdd:PRK12767 216 EV-RAGETSKGVTVKDPElfKLAERLAE--ALGARGplnIQCFVTDGEPYLFEINP 268
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 97-266 9.95e-08

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: 50.46  E-value: 9.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   97 ARDKLRSMQLLARQGIDLPVTGIAHSPDdtsdlidmVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQAEELL--------REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  177 QEYIKE--------AQGCDIRCLVVGDEVvaaIERRAKEGDFRSNLhrggaasVASITPqEREIAIKAARTMALDV---- 244
Cdd:pfam02655  66 QEFIEGeplsvsllSDGEKALPLSVNRQY---IDNGGSGFVYAGNV-------TPSRTE-LKEEIIELAEEVVECLpglr 134

                         170       180
                  ....*....|....*....|....
gi 166977476  245 --AGVDILRANRGPLVMEVNASPG 266
Cdd:pfam02655 135 gyVGVDLVLKDNEPYVIEVNPRIT 158
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
 124-266 7.18e-07

YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the modification/biosynthesis of spore-wall and capsular proteins.


Pssm-ID: 405146 [Multi-domain]  Cd Length: 256  Bit Score: 49.48  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  124 DDTSDLIDMVGGAPLV-VKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYIK 181
Cdd:pfam14398  36 QSPEDLERMLEKYGSVyLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGID 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  182 --EAQGC--DIRCLVVGDE-----VVAAIERRAKEGDFRSNLHRGGAASVAS-----ITPQEREIAIKA-ARTMALDVA- 245
Cdd:pfam14398 116 laTIDGRpfDFRVLVQKNGkgkwvVTGIAARIAGPGSITTNLSGGGTAIPLEealrrAFGEERAEKILEkLEELALELAr 195

                         170       180       190
                  ....*....|....*....|....*....|....
gi 166977476  246 ------------GVDILRANRGPLVM-EVNASPG 266
Cdd:pfam14398 196 aleesfgglgelGLDLGIDKNGRVWLlEVNSKPG 229
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 135-266 7.76e-07

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: 48.85  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  135 GAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKeaqGCDIRCLVVGDE---VVAAIERRAKEG--D 209
Cdd:pfam07478  36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIE---GREIECAVLGNEdpeVSPVGEIVPSGGfyD 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166977476  210 FRSNLHRGGAASV--ASITPQE----REIAIKAARtmALDVAG---VDI-LRANRGPLVMEVNASPG 266
Cdd:pfam07478 113 YEAKYIDDSAQIVvpADLEEEQeeqiQELALKAYK--ALGCRGlarVDFfLTEDGEIVLNEVNTIPG 177
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
93-266 1.24e-06

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 49.16  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVVK--------LVEGTQGIGVVLAETRQAAESVI 164
Cdd:COG3919  111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKpadsvgydELSFPGKKKVFYVDDREELLALL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 165 DAFRGLNAHILVQEYIKEAQGcDIRCLVV-----GDEVVAAIERRAKEgdfrsnLHRGGAASVASITPQEREIaIKAART 239
Cdd:COG3919  190 RRIAAAGYELIVQEYIPGDDG-EMRGLTAyvdrdGEVVATFTGRKLRH------YPPAGGNSAARESVDDPEL-EEAARR 261

                        170       180       190
                 ....*....|....*....|....*....|....
gi 166977476 240 M--ALD---VAGVDILRANRG--PLVMEVNASPG 266
Cdd:COG3919  262 LleALGyhgFANVEFKRDPRDgeYKLIEINPRFW 295
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 78-278 6.23e-05

Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];


Pssm-ID: 441833 [Multi-domain]  Cd Length: 370  Bit Score: 44.14  E-value: 6.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  78 RQFEMLGsyplNESVAIARARDKLRSMQLLARQGIDLPVTgIAHSPDDTSdlidmvggaPLVVKLVEGTQGIGVVLAETR 157
Cdd:COG2232   95 RRLPLLG----NPPEVVRRVKDPLRFFALLDELGIPHPET-RFEPPPDPG---------PWLVKPIGGAGGWHIRPADSE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 158 QAAEsvidafrglnAHILVQEYIkeaQGCDIRCLVVGD----EVVAAIE---RRAKEGDFRSnlhrGGAASVASITPQER 230
Cdd:COG2232  161 APPA----------PGRYFQRYV---EGTPASVLFLADgsdaRVLGFNRqliGPAGERPFRY----GGNIGPLALPPALA 223

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 166977476 231 EIAIKAARTMALD-----VAGVDILRANRGPLVMEVNASPG--LEGIEKTTGIDI 278
Cdd:COG2232  224 EEMRAIAEALVAAlglvgLNGVDFILDGDGPYVLEVNPRPQasLDLYEDATGGNL 278
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 93-284 4.66e-04

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: 41.91  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476    93 AIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVgGAPLVVK--LVEGTQGIGVVLAEtRQAAESVIDAFRGL 170
Cdd:TIGR01369  663 SIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEI-GYPVLVRpsYVLGGRAMEIVYNE-EELRRYLEEAVAVS 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476   171 NAH-ILVQEYIKEAQGCDIRCLVVGDEVVAA-----IErrakegdfRSNLHRGGAASV--ASITPQEREIAIKA-ARTMA 241
Cdd:TIGR01369  741 PEHpVLIDKYLEDAVEVDVDAVSDGEEVLIPgimehIE--------EAGVHSGDSTCVlpPQTLSAEIVDRIKDiVRKIA 812

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 166977476   242 --LDVAG---VDILRANRGPLVMEVN--ASPGLEGIEKTTGIDIAGKMIR 284
Cdd:TIGR01369  813 keLNVKGlmnIQFAVKDGEVYVIEVNprASRTVPFVSKATGVPLAKLAVR 862
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 92-269 1.01e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 40.27  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  92 VAIARARDKLRSMQLLARQGI------DLPVTGIAHSPDDTsdLIDMVG-GAPLVVKLVEGTQGIGVVLAETRQAAESVI 164
Cdd:PRK14572 123 LASALAMDKTRANQIFLQSGQkvapffELEKLKYLNSPRKT--LLKLESlGFPQFLKPVEGGSSVSTYKITNAEQLMTLL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 165 DAFRGLNAHILVQEyikeaqgcdircLVVGDEVVAAIERRAKEG-------------------DFRSNLHRGGAASV--A 223
Cdd:PRK14572 201 ALIFESDSKVMSQS------------FLSGTEVSCGVLERYRGGkrnpialpateivpggeffDFESKYKQGGSEEItpA 268

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 166977476 224 SITPQE----REIAIKAARTMALD-VAGVDILRANRGPLVMEVNASPGLEG 269
Cdd:PRK14572 269 RISDQEmkrvQELAIRAHESLGCKgYSRTDFIIVDGEPHILETNTLPGMTE 319
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 93-247 7.15e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 37.44  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476  93 AIARARDKLRSMQLLARQGIdlPVTG--IAHSPDDTSDLIDMVGGaPLVVKLV-EGTQGIGVVLAETRQAAESVIDAFRG 169
Cdd:PRK06019  94 ALAIAQDRLTEKQFLDKLGI--PVAPfaVVDSAEDLEAALADLGL-PAVLKTRrGGYDGKGQWVIRSAEDLEAAWALLGS 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166977476 170 LNAhiLVQEYI---KEAQgcdirclvvgdeVVAAierRAKEGDFRS-----NLHRGG--AASV--ASITPQEREIAIKAA 237
Cdd:PRK06019 171 VPC--ILEEFVpfeREVS------------VIVA---RGRDGEVVFyplveNVHRNGilRTSIapARISAELQAQAEEIA 233

                        170
                 ....*....|..
gi 166977476 238 RTMA--LDVAGV 247
Cdd:PRK06019 234 SRIAeeLDYVGV 245
 
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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