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Conserved domains on  [gi|647318756|ref|WP_025756080|]
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MULTISPECIES: 30S ribosomal protein S6--L-glutamate ligase [Enterobacter]

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: 602.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASSIHYKGRKLPHFDAVIPRIGSQITYYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  81 EMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVIKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 161 ESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 241 GLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWIERHATPGYCLKTGG 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: 602.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASSIHYKGRKLPHFDAVIPRIGSQITYYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  81 EMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVIKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 161 ESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 241 GLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWIERHATPGYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-286 1.42e-115

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: 333.93  E-value: 1.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756    2 KIAILSRDGTLySCKRLREAAAKRGHQVEILDPMSCYMNIDPaassihyKGRKLPHFDAVIPRIGSQitYYGTAALRQFE 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRIVSM--FRGLAVLRYLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   82 MLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVIKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768  71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  162 SVIDAFRGLNA---HILVQEYIEEAKGRDIRCFVVGNEVVAAIERQaKEGDFRSNLHRGGIARVATISDREREIAVKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 647318756  239 TLGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-290 1.33e-114

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: 331.91  E-value: 1.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASsiHYKGRKLPHFDAVIPRIGSqiTYYGTAALRQF 80
Cdd:COG0189    2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  81 EMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVIKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189   78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 161 ESVIDAFRGL-NAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQT 239
Cdd:COG0189  157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647318756 240 LGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWIERHA 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 4.22e-98

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: 286.32  E-value: 4.22e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   97 ARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVIKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  176 VQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQTLGLDVAGVDLLRATRG 255
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 647318756  256 PLVMEVNASPGLEGVEKTTGVDIAGKMIAWI 286
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
2-283 1.05e-51

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 171.65  E-value: 1.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   2 KIAILSRDGTLYSCKRLREAAAKRGHQVEILDP--MSCYMNIDpaaSSIHYKGRKLPHFDAVIPR-IGSQIT---YYGTA 75
Cdd:NF040720   1 KIGIIVTDRNDWTANALIRACEKKDIDPVLIDLskIEVSIGSD---IKFKYGKINLLDLDAIFVRdIGAGSNegvSFRFD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  76 ALRQFEMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVIKLVEGTQGIGVVL-- 153
Cdd:NF040720  78 VLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGIVRik 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 154 -AETRQAAESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREI 232
Cdd:NF040720 156 nGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQEEL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647318756 233 AVKAAQTLGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMI 283
Cdd:NF040720 236 AIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKII 286
 
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: 602.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASSIHYKGRKLPHFDAVIPRIGSQITYYGTAALRQF 80
Cdd:PRK10446   1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  81 EMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVIKLVEGTQGIGVVLAETRQAA 160
Cdd:PRK10446  81 EMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 161 ESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQTL 240
Cdd:PRK10446 161 ESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTM 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 241 GLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWIERHATPGYCLKTGG 300
Cdd:PRK10446 241 ALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG 300
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-286 1.42e-115

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: 333.93  E-value: 1.42e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756    2 KIAILSRDGTLySCKRLREAAAKRGHQVEILDPMSCYMNIDPaassihyKGRKLPHFDAVIPRIGSQitYYGTAALRQFE 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE-------GPRALAELDVVIVRIVSM--FRGLAVLRYLE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   82 MLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVIKLVEGTQGIGVVLAETRQAAE 161
Cdd:TIGR00768  71 SLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIG-FPVVLKPVFGSWGRGVSLARDRQAAE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  162 SVIDAFRGLNA---HILVQEYIEEAKGRDIRCFVVGNEVVAAIERQaKEGDFRSNLHRGGIARVATISDREREIAVKAAQ 238
Cdd:TIGR00768 150 SLLEHFEQLNGpqnLFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAK 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 647318756  239 TLGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWI 286
Cdd:TIGR00768 229 ALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-290 1.33e-114

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: 331.91  E-value: 1.33e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASsiHYKGRKLPHFDAVIPRIGSqiTYYGTAALRQF 80
Cdd:COG0189    2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPE--LYRGEDLSEFDAVLPRIDP--PFYGLALLRQL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  81 EMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVIKLVEGTQGIGVVLAETRQAA 160
Cdd:COG0189   78 EAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGG-PVVLKPLDGSGGRGVFLVEDEDAL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 161 ESVIDAFRGL-NAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQT 239
Cdd:COG0189  157 ESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELALRAAPA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647318756 240 LGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMIAWIERHA 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 4.22e-98

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: 286.32  E-value: 4.22e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   97 ARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVG-GAPLVIKLVEGTQGIGVVLAETRQAAESVIDAfrgLNAHIL 175
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSA---TNEQIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  176 VQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREIAVKAAQTLGLDVAGVDLLRATRG 255
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 647318756  256 PLVMEVNASPGLEGVEKTTGVDIAGKMIAWI 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 3.61e-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: 3.61e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756    1 MKIAILSRDGTLYSCKRLREAAAKRGHQVEILDPMSCYMNIDPAASSIHYKGRKLPHFDAVIPRIGSQITYYGTAALRQF 80
Cdd:pfam18030   1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPEIHYKGEPLPDFDAVIPRIGASITFYGTAVLRQF 80

                          90
                  ....*....|....
gi 647318756   81 EMLGSYPLNESVAI 94
Cdd:pfam18030  81 EMMGVFSLNSSQAI 94
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
2-283 1.05e-51

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 171.65  E-value: 1.05e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   2 KIAILSRDGTLYSCKRLREAAAKRGHQVEILDP--MSCYMNIDpaaSSIHYKGRKLPHFDAVIPR-IGSQIT---YYGTA 75
Cdd:NF040720   1 KIGIIVTDRNDWTANALIRACEKKDIDPVLIDLskIEVSIGSD---IKFKYGKINLLDLDAIFVRdIGAGSNegvSFRFD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  76 ALRQFEMLGSYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAplVIKLVEGTQGIGVVL-- 153
Cdd:NF040720  78 VLRYLEELGIPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKFEDA--VLKPVFGYKGKGIVRik 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 154 -AETRQAAESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQAKEGDFRSNLHRGGIARVATISDREREI 232
Cdd:NF040720 156 nGESIATKLELLNEFKEERGMLYIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQEEL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647318756 233 AVKAAQTLGLDVAGVDLLRATRGPLVMEVNASPGLEGVEKTTGVDIAGKMI 283
Cdd:NF040720 236 AIKAAEALGLVYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIAEKII 286
PRK12458 PRK12458
glutathione synthetase; Provisional
 13-288 1.90e-21

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 92.39  E-value: 1.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  13 YSCKRLREAAAKRGHQVEILDPMSCYMNIDPA----ASSIHYKGRKLPH--------------------FDAVIPR---- 64
Cdd:PRK12458  11 DTTLRLAHEAVNRGHEVAYTTPGDLTIRDDEAlafcAVTKKGKKYKKPEnflsflkkaefkkerlplagFDVIFLRanpp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  65 ---IGSQ-ITYYGTAALRQFEMLGSYPLNESVAISRARDKLrSLQLLARQGIdlPVTGIAHSPDDTSDLIDMVGGAPLVI 140
Cdd:PRK12458  91 ldpLARNwADSVGIAFGRLAARDGVLVVNDPDGLRIANNKL-YFQSFPEEVR--PTTHISRNKEYIREFLEESPGDKMIL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 141 KLVEGTQGIGVVLAET--RQAAESVIDAFRGLNaHILVQEYIEEAKGRDIRCFVVGNE------VVAAIERQAKEGDFRS 212
Cdd:PRK12458 168 KPLQGSGGQGVFLIEKsaQSNLNQILEFYSGDG-YVIAQEYLPGAEEGDVRILLLNGEplerdgHYAAMRRVPAGGDVRS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 213 NLHRGGIARVATISDREREIAVKAAQTL---GLDVAGVDLLratrGPLVMEVNA-SP-GLEGVEKTTGVDIAGKMIAWIE 287
Cdd:PRK12458 247 NVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIV----GDKLVEVNVfSPgGLTRINKLNKIDFVEDIIEALE 322


                 .
gi 647318756 288 R 288
Cdd:PRK12458 323 R 323
PRK05246 PRK05246
glutathione synthetase; Provisional
 134-288 4.83e-19

glutathione synthetase; Provisional


Pssm-ID: 235371 [Multi-domain]  Cd Length: 316  Bit Score: 85.53  E-value: 4.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 134 GGAPlVIKLVEGTQGIGVVLaE--TRQAAESVIdafrglnahilVQEYIEEAKGRDIRCFVVGNEVV-AAIERQAKEGDF 210
Cdd:PRK05246 166 GGAG-IFRVKADDPNLGSIL-EtlTEHGREPVM-----------AQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGET 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 211 RSNLHRGGIARVATISDREREIAVKAAQTL---GLDVAGVDLLratrGPLVMEVN-ASP-GLEGVEKTTGVDIAGKMIAW 285
Cdd:PRK05246 233 RGNLAAGGRGEATPLTERDREICAAIGPELkerGLIFVGIDVI----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDA 308


                 ...
gi 647318756 286 IER 288
Cdd:PRK05246 309 IEA 311
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 91-267 4.19e-18

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 84.44  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  91 SVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVIKLVEGTQGIGVVL-AETRQAAESVIDAFRG 169
Cdd:PRK14016 206 AIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGY-PVVVKPLDGNHGRGVTVnITTREEIEAAYAVASK 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 170 LNAHILVQEYIEeakGRDIRCFVVGNEVVAA------------------------------------------------- 200
Cdd:PRK14016 285 ESSDVIVERYIP---GKDHRLLVVGGKLVAAarrepphvigdgkhtirelieivnqdprrgeghekpltkiklddialle 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 201 IERQAKEGD----------FRS--NLHRGGIARVAT--ISDREREIAVKAAQTLGLDVAGVDL--------LRATRGpLV 258
Cdd:PRK14016 362 LAKQGYTLDsvppkgekvyLRRnaNLSTGGTAIDVTdeVHPENAAIAERAAKIIGLDIAGVDVvcediskpLEEQGG-AI 440


                 ....*....
gi 647318756 259 MEVNASPGL 267
Cdd:PRK14016 441 VEVNAAPGL 449
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 1-267 1.36e-15

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: 75.53  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   1 MKIAILS------RDGTLYSCKRLREAAAKRGHQVEILDpmscymnIDPAASSihyKGRKLPHFDAVIP----RIGSqit 70
Cdd:COG1181    1 MRVAVLFggrsaeREVSLKSGRAVAAALDKAGYDVVPIG-------IDVEDLP---AALKELKPDVVFPalhgRGGE--- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  71 yYGT-AALrqFEML-----GSYPLnesvAISRARDKLRSLQLLARQGIDLPvTGIAHSPDDTSDLIDMVG--GAPLVIKL 142
Cdd:COG1181   68 -DGTiQGL--LELLgipytGSGVL----ASALAMDKALTKRVLAAAGLPTP-PYVVLRRGELADLEAIEEelGLPLFVKP 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 143 V-EGTqGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIEeakGRDIRCFVVGNEVVAA---IERQAKEG--DFRSNLHR 216
Cdd:COG1181  140 ArEGS-SVGVSKVKNAEELAAALEEAFKYDDKVLVEEFID---GREVTVGVLGNGGPRAlppIEIVPENGfyDYEAKYTD 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 647318756 217 GGIARV--ATISDRE----REIAVKAAQTLGL-DVAGVDL-LRATRGPLVMEVNASPGL 267
Cdd:COG1181  216 GGTEYIcpARLPEELeeriQELALKAFRALGCrGYARVDFrLDEDGEPYLLEVNTLPGM 274
GSH-S_ATP pfam02955
Prokaryotic glutathione synthetase, ATP-grasp domain;
139-275 3.16e-14

Prokaryotic glutathione synthetase, ATP-grasp domain;


Pssm-ID: 427078 [Multi-domain]  Cd Length: 175  Bit Score: 69.13  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  139 VIKLVEGTQGIGVV-LAETRQAAESVIDAFRGL-NAHILVQEYIEEAKGRDIRCFVVGNEVV-AAIERQAKEGDFRSNLH 215
Cdd:pfam02955  35 ILKPLDGMGGAGIFrVKKGDPNLNVILETLTQYgTRPVMAQRYLPEIKEGDKRILLINGEPIgYALARIPAAGEFRGNLA 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647318756  216 RGGIARVATISDREREIAVKAAQTL---GLDVAGVDLLratrGPLVMEVN-ASP-GLEGVEKTTG 275
Cdd:pfam02955 115 AGGRGEATPLTERDREICETIGPKLkerGLFFVGLDVI----GDYLTEINvTSPtGIREIERLTG 175
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 58-278 4.80e-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: 70.67  E-value: 4.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  58 FDAVIPriGSQITYYGTAALRqfEMLGsYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaP 137
Cdd:COG0439   18 IDAVLS--ESEFAVETAAELA--EELG-LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGY-P 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 138 LVIKLVEGTQGIGVVLAETRQAAESVIDAFRG------LNAHILVQEYIEeakGRDIRC--FVVGNEVV--AAIERQAKE 207
Cdd:COG0439   92 VVVKPADGAGSRGVRVVRDEEELEAALAEARAeakagsPNGEVLVEEFLE---GREYSVegLVRDGEVVvcSITRKHQKP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 208 GDFrsnLHRGGIARvATISDRER----EIAVKAAQTLGLD--VAGVDLLRATRG-PLVMEVNASPGLEG----VEKTTGV 276
Cdd:COG0439  169 PYF---VELGHEAP-SPLPEELRaeigELVARALRALGYRrgAFHTEFLLTPDGePYLIEINARLGGEHipplTELATGV 244


                 ..
gi 647318756 277 DI 278
Cdd:COG0439  245 DL 246
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 99-267 1.17e-11

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 63.98  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  99 DKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVIKLVEGTQGIGVVLAETRQA-AESVIDAFRgLNAHILVQ 177
Cdd:PRK01372  98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLG-LPLVVKPAREGSSVGVSKVKEEDElQAALELAFK-YDDEVLVE 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 178 EYIeeaKGRDIRCFVVGNEVVAAIERQAKEG--DFRSNLHRGG-----IARV-ATISDREREIAVKAAQTLGLDVAG-VD 248
Cdd:PRK01372 176 KYI---KGRELTVAVLGGKALPVIEIVPAGEfyDYEAKYLAGGtqyicPAGLpAEIEAELQELALKAYRALGCRGWGrVD 252

                        170       180
                 ....*....|....*....|
gi 647318756 249 L-LRATRGPLVMEVNASPGL 267
Cdd:PRK01372 253 FmLDEDGKPYLLEVNTQPGM 272
MfnD COG1821
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ...
 83-262 1.42e-08

Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme transport and metabolism];


Pssm-ID: 441426 [Multi-domain]  Cd Length: 323  Bit Score: 54.93  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  83 LGSYPlnESVAIsrARDKLRSLQLLARQGIDLPVTgiaHSPDDTSDLidmvGGAPLVIKLVEGTQGIGVVLAETRQAAES 162
Cdd:COG1821  112 LGSSP--EAIAL--AADKLLTAELLAAAGIPTPPT---FPADDAPPL----LAGPWVVKPDDGAGSEGTRLFDDPAALRA 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 163 VIDAFRGLnahiLVQEYIEeakGRDIR-CFVVGNE--VVAAIERQA---KEGDFRsnlHRGGIARVAT-ISDREREIAVK 235
Cdd:COG1821  181 REARGAGL----IVQPYIE---GEAASlSLLCGRGgaLLLSINRQRievDGGRFS---YLGGTVPAEHpRKEELQALAQK 250

                        170       180       190
                 ....*....|....*....|....*....|.
gi 647318756 236 AAQTL----GLdvAGVDLLRATRGPLVMEVN 262
Cdd:COG1821  251 VAEALpglrGY--VGVDLILTADGPVVVEVN 279
ATPgrasp_YheCD pfam14398
YheC/D like ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the ...
 124-266 2.98e-08

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: 53.72  E-value: 2.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  124 DDTSDLIDMVGGAPLV-IKLVEGTQGIGVVLAE------------TRQAAESVIDAFRGLNAHI---------LVQEYIE 181
Cdd:pfam14398  36 QSPEDLERMLEKYGSVyLKPVNGSLGKGILRIEkdgggyylygryGKNSKTNRFLDFSELESFLrrllgkkryIIQQGID 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  182 --EAKGR--DIRCFVVGNE-----VVAAIERQAKEGDFRSNLHRGGIA--------------RVATISDREREIAVKAAQ 238
Cdd:pfam14398 116 laTIDGRpfDFRVLVQKNGkgkwvVTGIAARIAGPGSITTNLSGGGTAipleealrrafgeeRAEKILEKLEELALELAR 195

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 647318756  239 T----------LGLDVaGVDllraTRGPLVM-EVNASPG 266
Cdd:pfam14398 196 AleesfgglgeLGLDL-GID----KNGRVWLlEVNSKPG 229
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 97-266 3.12e-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: 52.00  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   97 ARDKLRSLQLLARQGIDLPVTGIAHSPDdtsdlidmVGGAPLVIKLVEGTQGIGVVLAETRQAAESVIDafrglnaHILV 176
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQAEELL--------REEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  177 QEYIEeakGRDIRCFVVGN---EVVAAIERQAKEGDFRSNLHRGGIARVATISDRE-REIAVKAAQTL-GL-DVAGVDLL 250
Cdd:pfam02655  66 QEFIE---GEPLSVSLLSDgekALPLSVNRQYIDNGGSGFVYAGNVTPSRTELKEEiIELAEEVVECLpGLrGYVGVDLV 142

                         170
                  ....*....|....*.
gi 647318756  251 RATRGPLVMEVNASPG 266
Cdd:pfam02655 143 LKDNEPYVIEVNPRIT 158
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 65-293 1.24e-07

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 52.93  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  65 IGSQITYYGTAALRQFEMLGsYPLNESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDmvGGA-PLVIKLV 143
Cdd:PRK02186  74 IMSSSEYFIEVASEVARRLG-LPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALD--GLTyPVVVKPR 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 144 EGTQGIGVVLAETRQAA-ESVIDAFRGLNAHILVQEYIEEAKGRDIRCFVVGNEVVAAIERQ--AKEGDFRSNLHRGGIA 220
Cdd:PRK02186 151 MGSGSVGVRLCASVAEAaAHCAALRRAGTRAALVQAYVEGDEYSVETLTVARGHQVLGITRKhlGPPPHFVEIGHDFPAP 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 221 RVATISDREREIAVKAAQTLGLDV--AGVDLLRATRGPLVMEVNasPGLEG------VEKTTGVDIAGKMI-AWIERHAT 291
Cdd:PRK02186 231 LSAPQRERIVRTVLRALDAVGYAFgpAHTELRVRGDTVVIIEIN--PRLAGgmipvlLEEAFGVDLLDHVIdLHLGVAAF 308


                 ..
gi 647318756 292 PG 293
Cdd:PRK02186 309 AD 310
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 135-266 2.19e-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: 50.39  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  135 GAPLVIKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIEeakGRDIRCFVVGNE---VVAAIERQAKEG--D 209
Cdd:pfam07478  36 GYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIE---GREIECAVLGNEdpeVSPVGEIVPSGGfyD 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647318756  210 FRSNLHRGGI-----ARVAT-ISDREREIAVKAAQTLGL-DVAGVDL-LRATRGPLVMEVNASPG 266
Cdd:pfam07478 113 YEAKYIDDSAqivvpADLEEeQEEQIQELALKAYKALGCrGLARVDFfLTEDGEIVLNEVNTIPG 177
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 99-271 6.74e-07

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: 49.65  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   99 DKLRSLQLLARQGIDLPVT-GIAHSPDDTSDLIDMVGGAP--LVIKLVEGTQGIGVVLAETR-----QAAESVIDAFRGL 170
Cdd:pfam14397  21 DKLKFKQLALRAGLPVPKLyGVISIGHDISRLDAFVRSLPpgFVIKPAKGSGGKGILVITRRgdqdyFKSSGCRILLDEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  171 NAHI----------LVQEYIEEAKG---------RDIRCFVV----GNEVVAAIERQAKEGDFRSNLHRGGIA------- 220
Cdd:pfam14397 101 KRHVsslggkpdvaLVEERIVQDPVfaklspesvNTIRVITFlldnGVPVMPAMLRLGTGASLVDNLHQGGVGvgidlat 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  221 -RVATISDRER----------------------------EIAVKAAQTL-GLDVAGVDL-LRATRGPLVMEVNASPGLEG 269
Cdd:pfam14397 181 gVLFKPALQAVqygepiehhpdtgvkfrgfqipnwdqilELAAECAQTLpGLGYVGWDIvIDENGGPLLLELNARPGLGI 260


                  ..
gi 647318756  270 VE 271
Cdd:pfam14397 261 FQ 262
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 94-263 7.20e-07

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 49.88  E-value: 7.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  94 ISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTS-DLIDMVGGAPLVIKLVEGTQGIGVVLAETRQAAESVIDafrgLNA 172
Cdd:PRK12767 106 IEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKaALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLE----YVP 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 173 HILVQEYIEEAK-GRDIRCFVVGNeVVAAIERqaKEGDFRSnlhrGGIARVATISDRE-REIAVKAAQTLG----LDvag 246
Cdd:PRK12767 182 NLIIQEFIEGQEyTVDVLCDLNGE-VISIVPR--KRIEVRA----GETSKGVTVKDPElFKLAERLAEALGargpLN--- 251

                        170
                 ....*....|....*..
gi 647318756 247 VDLLRATRGPLVMEVNA 263
Cdd:PRK12767 252 IQCFVTDGEPYLFEINP 268
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
93-266 1.00e-06

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 49.54  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  93 AISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGaPLVIKLVEGTQ--------GIGVVLAETRQAAESVI 164
Cdd:COG3919  111 LLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF-PVVVKPADSVGydelsfpgKKKVFYVDDREELLALL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 165 DAFRGLNAHILVQEYIEEAKGRDIRCFVVGN---EVVAAIERQAkegdFRSNLHRGGIArVATISDREREIaVKAAQTL- 240
Cdd:COG3919  190 RRIAAAGYELIVQEYIPGDDGEMRGLTAYVDrdgEVVATFTGRK----LRHYPPAGGNS-AARESVDDPEL-EEAARRLl 263

                        170       180       190
                 ....*....|....*....|....*....|..
gi 647318756 241 -GLD---VAGVDLLRATRG--PLVMEVNASPG 266
Cdd:COG3919  264 eALGyhgFANVEFKRDPRDgeYKLIEINPRFW 295
PLN02735 PLN02735
carbamoyl-phosphate synthase
 14-284 3.21e-05

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 45.54  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   14 SCKRLREaaakRGHQVEILDPMSCYMNIDPAASSIHYKGRKLPHF----------DAVIPRIGSQITYYGTAALRQFEML 83
Cdd:PLN02735   49 ACKALKE----EGYEVVLINSNPATIMTDPETADRTYIAPMTPELveqviakerpDALLPTMGGQTALNLAVALAESGIL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756   84 GSYPLN----ESVAISRARDKLRSLQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVIKLVEGTQGIGVVLAETRQA 159
Cdd:PLN02735  125 EKYGVEligaKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGEFPLIIRPAFTLGGTGGGIAYNKEE 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  160 AESVIDAfrGLNAHILVQEYIEEA----------KGRDIRCFVVgneVVAAIERQAKEGdfrsnLHRGGIARVA---TIS 226
Cdd:PLN02735  205 FETICKA--GLAASITSQVLVEKSllgwkeyeleVMRDLADNVV---IICSIENIDPMG-----VHTGDSITVApaqTLT 274

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647318756  227 DRE----REIAVKAAQTLGLDVAGVDLLRATrGP-----LVMEVNA----SPGLegVEKTTGVDIAgKMIA 284
Cdd:PLN02735  275 DKEyqrlRDYSVAIIREIGVECGGSNVQFAV-NPvdgevMIIEMNPrvsrSSAL--ASKATGFPIA-KMAA 341
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 78-278 5.26e-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: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  78 RQFEMLGsyplNESVAISRARDKLRSLQLLARQGIDLPVTgIAHSPDDTSdlidmvggaPLVIKLVEGTQGIGVVLAETR 157
Cdd:COG2232   95 RRLPLLG----NPPEVVRRVKDPLRFFALLDELGIPHPET-RFEPPPDPG---------PWLVKPIGGAGGWHIRPADSE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 158 QAAEsvidafrglnAHILVQEYIEeakGRDIRCFVVGNE---VVAAIERQ----AKEGDFRsnlHRGGIARVA---TISD 227
Cdd:COG2232  161 APPA----------PGRYFQRYVE---GTPASVLFLADGsdaRVLGFNRQligpAGERPFR---YGGNIGPLAlppALAE 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 647318756 228 REREIAVKAAQTLGL-DVAGVDLLRATRGPLVMEVNASPG--LEGVEKTTGVDI 278
Cdd:COG2232  225 EMRAIAEALVAALGLvGLNGVDFILDGDGPYVLEVNPRPQasLDLYEDATGGNL 278
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 92-269 6.79e-04

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 40.66  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756  92 VAISRARDKLRSLQLLARQGI------DLPVTGIAHSPDDTsdLIDMVG-GAPLVIKLVEGTQGIGVVLAETRQAAESVI 164
Cdd:PRK14572 123 LASALAMDKTRANQIFLQSGQkvapffELEKLKYLNSPRKT--LLKLESlGFPQFLKPVEGGSSVSTYKITNAEQLMTLL 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 165 DAFRGLNAHILVQEYIeeaKGRDIRCFVVGN------EVVAAIERQAKEG----DFRSNLHRGGIARV--ATISDRE--- 229
Cdd:PRK14572 201 ALIFESDSKVMSQSFL---SGTEVSCGVLERyrggkrNPIALPATEIVPGgeffDFESKYKQGGSEEItpARISDQEmkr 277

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 647318756 230 -REIAVKAAQTLGLD-VAGVDLLRATRGPLVMEVNASPGLEG 269
Cdd:PRK14572 278 vQELAIRAHESLGCKgYSRTDFIIVDGEPHILETNTLPGMTE 319
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
105-249 1.81e-03

bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 39.91  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 105 QLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVIKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAH---ILVQEYIe 181
Cdd:PRK02471 494 KILAEAGFPVPAGDEFTSLEEALADYSLFADKAIVVKPKSTNFGLGISIFKEPASLEDYEKALEIAFREdssVLVEEFI- 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647318756 182 eaKGRDIRCFVVGNEVVAAIER-----------------QAKEGD------FR--------------------------- 211
Cdd:PRK02471 573 --VGTEYRFFVLDGKVEAVLLRvpanvvgdgihtvrelvAQKNQDplrgtdHRtplekiqlgeierlmlkqqgltpdsip 650

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 647318756 212 -----------SNLHRGG--IARVATISDREREIAVKAAQTLGLDVAGVDL 249
Cdd:PRK02471 651 kkgeivylrenSNISTGGdsIDMTDDMDDSYKQIAVKAAKALGAKICGVDL 701
 
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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