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Conserved domains on  [gi|1668705387|ref|WP_138246483|]
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RimK family alpha-L-glutamate ligase [Natrinema versiforme]

Protein Classification

ATP-grasp domain-containing protein( domain architecture ID 11415139)

ATP-grasp domain-containing protein may catalyze the ATP-assisted reaction of a carboxylic acid with a nucleophile via the formation of an acylphosphate intermediate, such as Streptomyces lavendulae cycloserine biosynthesis protein DcsG that is involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine

EC:  6.-.-.-
Gene Ontology:  GO:0005524|GO:0016874
PubMed:  21920581|28488371|9416615

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-287 2.00e-60

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: 193.62  E-value: 2.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387   1 MIDLAVA---NDKETFERMGEPLAERGIRVHHVPVRERTVALDDPP-----WEPDAYDVGFVypgRLMEGGVADALLE-- 70
Cdd:COG0189     1 MMKIAILtdpPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPelyrgEDLSEFDAVLP---RIDPPFYGLALLRql 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  71 ----VPWLNDHETVLTSRNKAEVLARLGRAELPVPKSVYVSNdvgADELADVFERFEPPVVVKPNSTTRGVGVAKAHDLD 146
Cdd:COG0189    78 eaagVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRD---PDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 147 SFLGICDYLslvhdyKATGDQSFLVQEYLP--NATDYRVMILEGEYVGAVERRLpdaavSEGQWKHNVHRGAEATGVELP 224
Cdd:COG0189   155 ALESILEAL------TELGSEPVLVQEFIPeeDGRDIRVLVVGGEPVAAIRRIP-----AEGEFRTNLARGGRAEPVELT 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1668705387 225 DEYRELAERVGAALEIPFLGVDLLETDDRLVINETNARPTIDE-ETKYEPDFYDRLAAAIRTAA 287
Cdd:COG0189   224 DEERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGlERATGVDIAEAIADYLEARA 287
 
Name Accession Description Interval E-value
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-287 2.00e-60

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: 193.62  E-value: 2.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387   1 MIDLAVA---NDKETFERMGEPLAERGIRVHHVPVRERTVALDDPP-----WEPDAYDVGFVypgRLMEGGVADALLE-- 70
Cdd:COG0189     1 MMKIAILtdpPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPelyrgEDLSEFDAVLP---RIDPPFYGLALLRql 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  71 ----VPWLNDHETVLTSRNKAEVLARLGRAELPVPKSVYVSNdvgADELADVFERFEPPVVVKPNSTTRGVGVAKAHDLD 146
Cdd:COG0189    78 eaagVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRD---PDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 147 SFLGICDYLslvhdyKATGDQSFLVQEYLP--NATDYRVMILEGEYVGAVERRLpdaavSEGQWKHNVHRGAEATGVELP 224
Cdd:COG0189   155 ALESILEAL------TELGSEPVLVQEFIPeeDGRDIRVLVVGGEPVAAIRRIP-----AEGEFRTNLARGGRAEPVELT 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1668705387 225 DEYRELAERVGAALEIPFLGVDLLETDDRLVINETNARPTIDE-ETKYEPDFYDRLAAAIRTAA 287
Cdd:COG0189   224 DEERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGlERATGVDIAEAIADYLEARA 287
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 18-263 9.39e-32

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: 118.99  E-value: 9.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  18 EPLAERGIRVHHVPVRERTVALDDPPWEPDAYDVGFVYPGRLMEGGVADALLE---VPWLNDHETVLTSRNKAEVLARLG 94
Cdd:TIGR00768  18 EAAEELGIDYKVVTPPAINLTFNEGPRALAELDVVIVRIVSMFRGLAVLRYLEslgVPVINSSDAILNAGDKFLSHQLLA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  95 RAELPVPKSVYVSNDVGADELAdvfERFEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDYLslvhDYKATGDQSFLVQEY 174
Cdd:TIGR00768  98 KAGIPLPRTGLAGSPEEALKLI---EEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHF----EQLNGPQNLFLVQEY 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 175 L--PNATDYRVMILEGEYVGAVERRlpdaavSEGQWKHNVHRGAEATGVELPDEYRELAERVGAALEIPFLGVDLLETDD 252
Cdd:TIGR00768 171 IkkPGGRDIRVFVVGDEVVAAIYRI------TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAKALGLDVAGVDLLESED 244

                         250
                  ....*....|.
gi 1668705387 253 RLVINETNARP 263
Cdd:TIGR00768 245 GLLVNEVNANP 255
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 83-271 2.09e-21

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: 89.10  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  83 SRNKAEVLARLGRAELPVPKSVYVSNDVGADELADVFERfEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDYLSlvhdyk 162
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKR-QFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATN------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 163 atgdQSFLVQEYL--PNATDYRVMILEGEYVGAVERRlpdaaVSEGQWKHNVHRGAEATGVELPDEYRELAERVGAALEI 240
Cdd:pfam08443  74 ----EQILVQEFIaeANNEDIRCLVVGDQVVGALHRQ-----SNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQL 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1668705387 241 PFLGVDLLETDDRLVINETNARPTIDEETKY 271
Cdd:pfam08443 145 DVAGVDLLRQKRGLLVCEVNSSPGLEGIEKT 175
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
74-266 7.74e-13

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 67.23  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  74 LNDHETVLTSRNKAEVLARLGRA--ELPVPKSVYVSNDVGaDELADVFErfePPVVVKPNSTTRGVGVAKAHD------- 144
Cdd:PRK10446   88 LNESVAIARARDKLRSMQLLARQgiDLPVTGIAHSPDDTS-DLIDMVGG---APLVVKLVEGTQGIGVVLAETrqaaesv 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 145 LDSFLGIcdylslvhdykatgDQSFLVQEYLPNAT--DYRVMILEGEYVGAVERRlpdaaVSEGQWKHNVHRGAEATGVE 222
Cdd:PRK10446  164 IDAFRGL--------------NAHILVQEYIKEAQgcDIRCLVVGDEVVAAIERR-----AKEGDFRSNLHRGGAASVAS 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1668705387 223 LPDEYRELAERVGAALEIPFLGVDLLETDDRLVINETNARPTID 266
Cdd:PRK10446  225 ITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLE 268
 
Name Accession Description Interval E-value
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-287 2.00e-60

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: 193.62  E-value: 2.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387   1 MIDLAVA---NDKETFERMGEPLAERGIRVHHVPVRERTVALDDPP-----WEPDAYDVGFVypgRLMEGGVADALLE-- 70
Cdd:COG0189     1 MMKIAILtdpPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPelyrgEDLSEFDAVLP---RIDPPFYGLALLRql 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  71 ----VPWLNDHETVLTSRNKAEVLARLGRAELPVPKSVYVSNdvgADELADVFERFEPPVVVKPNSTTRGVGVAKAHDLD 146
Cdd:COG0189    78 eaagVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRD---PDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDED 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 147 SFLGICDYLslvhdyKATGDQSFLVQEYLP--NATDYRVMILEGEYVGAVERRLpdaavSEGQWKHNVHRGAEATGVELP 224
Cdd:COG0189   155 ALESILEAL------TELGSEPVLVQEFIPeeDGRDIRVLVVGGEPVAAIRRIP-----AEGEFRTNLARGGRAEPVELT 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1668705387 225 DEYRELAERVGAALEIPFLGVDLLETDDRLVINETNARPTIDE-ETKYEPDFYDRLAAAIRTAA 287
Cdd:COG0189   224 DEERELALRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGlERATGVDIAEAIADYLEARA 287
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 18-263 9.39e-32

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: 118.99  E-value: 9.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  18 EPLAERGIRVHHVPVRERTVALDDPPWEPDAYDVGFVYPGRLMEGGVADALLE---VPWLNDHETVLTSRNKAEVLARLG 94
Cdd:TIGR00768  18 EAAEELGIDYKVVTPPAINLTFNEGPRALAELDVVIVRIVSMFRGLAVLRYLEslgVPVINSSDAILNAGDKFLSHQLLA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  95 RAELPVPKSVYVSNDVGADELAdvfERFEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDYLslvhDYKATGDQSFLVQEY 174
Cdd:TIGR00768  98 KAGIPLPRTGLAGSPEEALKLI---EEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHF----EQLNGPQNLFLVQEY 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 175 L--PNATDYRVMILEGEYVGAVERRlpdaavSEGQWKHNVHRGAEATGVELPDEYRELAERVGAALEIPFLGVDLLETDD 252
Cdd:TIGR00768 171 IkkPGGRDIRVFVVGDEVVAAIYRI------TSGHWRSNLARGGKAEPCSLTEEIEELAIKAAKALGLDVAGVDLLESED 244

                         250
                  ....*....|.
gi 1668705387 253 RLVINETNARP 263
Cdd:TIGR00768 245 GLLVNEVNANP 255
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 83-271 2.09e-21

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: 89.10  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  83 SRNKAEVLARLGRAELPVPKSVYVSNDVGADELADVFERfEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDYLSlvhdyk 162
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKR-QFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATN------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 163 atgdQSFLVQEYL--PNATDYRVMILEGEYVGAVERRlpdaaVSEGQWKHNVHRGAEATGVELPDEYRELAERVGAALEI 240
Cdd:pfam08443  74 ----EQILVQEFIaeANNEDIRCLVVGDQVVGALHRQ-----SNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQL 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1668705387 241 PFLGVDLLETDDRLVINETNARPTIDEETKY 271
Cdd:pfam08443 145 DVAGVDLLRQKRGLLVCEVNSSPGLEGIEKT 175
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
74-266 7.74e-13

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 67.23  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  74 LNDHETVLTSRNKAEVLARLGRA--ELPVPKSVYVSNDVGaDELADVFErfePPVVVKPNSTTRGVGVAKAHD------- 144
Cdd:PRK10446   88 LNESVAIARARDKLRSMQLLARQgiDLPVTGIAHSPDDTS-DLIDMVGG---APLVVKLVEGTQGIGVVLAETrqaaesv 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 145 LDSFLGIcdylslvhdykatgDQSFLVQEYLPNAT--DYRVMILEGEYVGAVERRlpdaaVSEGQWKHNVHRGAEATGVE 222
Cdd:PRK10446  164 IDAFRGL--------------NAHILVQEYIKEAQgcDIRCLVVGDEVVAAIERR-----AKEGDFRSNLHRGGAASVAS 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1668705387 223 LPDEYRELAERVGAALEIPFLGVDLLETDDRLVINETNARPTID 266
Cdd:PRK10446  225 ITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLE 268
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 75-263 7.23e-12

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: 64.12  E-value: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  75 NDHETVLTSRNKAEVLARLGRAELPVPKSVYVSNDvgaDELADVFERFEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDY 154
Cdd:COG0439    44 PSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSP---EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 155 LsLVHDYKATGDQSFLVQEYLPNaTDYRV--MILEGEYV--GAVERRLPDAAVsegqwkhnVHRGAEATGVELPDEYREL 230
Cdd:COG0439   121 A-RAEAKAGSPNGEVLVEEFLEG-REYSVegLVRDGEVVvcSITRKHQKPPYF--------VELGHEAPSPLPEELRAEI 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1668705387 231 AERVGAALEIpfLGVD--------LLETDDRLVINETNARP 263
Cdd:COG0439   191 GELVARALRA--LGYRrgafhtefLLTPDGEPYLIEINARL 229
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 74-262 1.22e-08

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 55.28  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  74 LNDHETVLTSRNK---AEVLARLGraeLPVPKSvYVSNDVGADELADVFERFEPPVVVKPNSTTRGVGVAKAHDLDsflG 150
Cdd:PRK12767  100 VSSKEVIEICNDKwltYEFLKENG---IPTPKS-YLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKE---E 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 151 ICDYLSLVHDYkatgdqsfLVQEYLpNATDYRVMIL---EGEYVGAVERRLPDAavsegqwkhnvhRGAEA-TGVELPD- 225
Cdd:PRK12767  173 LEFLLEYVPNL--------IIQEFI-EGQEYTVDVLcdlNGEVISIVPRKRIEV------------RAGETsKGVTVKDp 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1668705387 226 EYRELAERVGAALeiPFLG---VDLLETDDRLVINETNAR 262
Cdd:PRK12767  232 ELFKLAERLAEAL--GARGplnIQCFVTDGEPYLFEINPR 269
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
20-181 3.00e-07

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 51.08  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  20 LAERGIRVH------HVPVR-----ERTVALDDPPWEPDAY-----------DVGFVYPGrlMEGGVA------DALLE- 70
Cdd:COG3919    24 LGEAGVRVIvvdrdpLGPAArsryvDEVVVVPDPGDDPEAFvdallelaerhGPDVLIPT--GDEYVEllsrhrDELEEh 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  71 --VPWlNDHETVLTSRNKAEVLARLGRAELPVPKSVYVSndvGADELADVFERFEPPVVVKPNSTTR--------GVGVA 140
Cdd:COG3919   102 yrLPY-PDADLLDRLLDKERFYELAEELGVPVPKTVVLD---SADDLDALAEDLGFPVVVKPADSVGydelsfpgKKKVF 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1668705387 141 KAHDLDsflgicDYLSLVHDYKATGdQSFLVQEYLPNATDY 181
Cdd:COG3919   178 YVDDRE------ELLALLRRIAAAG-YELIVQEYIPGDDGE 211
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 20-193 3.57e-07

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: 50.49  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  20 LAERGIRVHHVPVrertvALDDPPWEPDAYDVGFVYP---GRLMEGGVADALLE---VPWLndHETVLTSR---NKA--- 87
Cdd:COG1181    28 LDKAGYDVVPIGI-----DVEDLPAALKELKPDVVFPalhGRGGEDGTIQGLLEllgIPYT--GSGVLASAlamDKAltk 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  88 EVLARLGraeLPVPKSVYVSNDVGADeLADVFERFEPPVVVKPNsttRG---VGVAKAHDLDSFLgicDYLSLVHDYkat 164
Cdd:COG1181   101 RVLAAAG---LPTPPYVVLRRGELAD-LEAIEEELGLPLFVKPA---REgssVGVSKVKNAEELA---AALEEAFKY--- 167

                         170       180
                  ....*....|....*....|....*....
gi 1668705387 165 gDQSFLVQEYLPnATDYRVMILEGEYVGA 193
Cdd:COG1181   168 -DDKVLVEEFID-GREVTVGVLGNGGPRA 194
PRK12458 PRK12458
glutathione synthetase; Provisional
 41-260 4.81e-07

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 50.40  E-value: 4.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  41 DPPWEPD----AYDVGFVYpGRLMEGGvadallEVPWLNDHETVLTSRNKaevlarLGRAELP--VPKSVYVSNDVgaDE 114
Cdd:PRK12458   88 NPPLDPLarnwADSVGIAF-GRLAARD------GVLVVNDPDGLRIANNK------LYFQSFPeeVRPTTHISRNK--EY 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 115 LADVFErfEPP---VVVKP--NSTTRGVGVAKAHDLDSFLGICDYLSlvhdykatGDQSFLVQEYLPNAT--DYRVMILE 187
Cdd:PRK12458  153 IREFLE--ESPgdkMILKPlqGSGGQGVFLIEKSAQSNLNQILEFYS--------GDGYVIAQEYLPGAEegDVRILLLN 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 188 GE-----YVGAVERRLPdaavSEGQWKHNVHRGAEATGVELPDEYRELAERVGAAL---EIPFLGVDLLetDDRLVinET 259
Cdd:PRK12458  223 GEplerdGHYAAMRRVP----AGGDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIV--GDKLV--EV 294


                  .
gi 1668705387 260 N 260
Cdd:PRK12458  295 N 295
PRK05246 PRK05246
glutathione synthetase; Provisional
 163-264 6.70e-07

glutathione synthetase; Provisional


Pssm-ID: 235371 [Multi-domain]  Cd Length: 316  Bit Score: 49.71  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 163 ATGDQSFLVQEYLPNAT--DYRVMILEGEYVGAVERRLPdaavSEGQWKHNVHRGAEATGVELPDEYRELAERVGAALE- 239
Cdd:PRK05246  189 EHGREPVMAQRYLPEIKegDKRILLVDGEPVGYALARIP----AGGETRGNLAAGGRGEATPLTERDREICAAIGPELKe 264

                          90       100
                  ....*....|....*....|....*...
gi 1668705387 240 --IPFLGVDLLetDDRLV-INETNarPT 264
Cdd:PRK05246  265 rgLIFVGIDVI--GDYLTeINVTS--PT 288
PRK07206 PRK07206
hypothetical protein; Provisional
 48-183 8.98e-06

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 46.56  E-value: 8.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  48 AYDVGFVYPGrlMEGGV--ADALLEV---PWLNDHETVLTSRNKAEVLARLGRAELPVPKSVYVSNDVGADELADVFERF 122
Cdd:PRK07206   68 KLGPEAIIAG--AESGVelADRLAEIltpQYSNDPALSSARRNKAEMINALAEAGLPAARQINTADWEEAEAWLRENGLI 145

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1668705387 123 EPPVVVKP-NST-TRGVGVAKAHD-----LDSFLGICDYLSLVHDykatgdqSFLVQEYLpNATDYRV 183
Cdd:PRK07206  146 DRPVVIKPlESAgSDGVFICPAKGdwkhaFNAILGKANKLGLVNE-------TVLVQEYL-IGTEYVV 205
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
79-196 1.45e-05

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


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 46.07  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  79 TVLTSRNKA---EVLARLGraeLPVPKSVYVSNdvgADELADVFERFE-PPVVVKPNSTTRGVGVA---KAHDLDSFLgi 151
Cdd:PRK02471  482 SPLIMENKVvtkKILAEAG---FPVPAGDEFTS---LEEALADYSLFAdKAIVVKPKSTNFGLGISifkEPASLEDYE-- 553

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1668705387 152 cdylslvhdyKA-----TGDQSFLVQEYLPnATDYRVMILEGEYVGAVER 196
Cdd:PRK02471  554 ----------KAleiafREDSSVLVEEFIV-GTEYRFFVLDGKVEAVLLR 592
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 76-186 1.78e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 42.91  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  76 DHETVLTSRNKAEVLARLGRAELPVPKSVYVSNDVgadELADVFERFEPPVVVKPNSTTRGVGVAKAHDLDSFLGICDYL 155
Cdd:PRK02186   98 NTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRA---VALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAAL 174

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1668705387 156 slvhdyKATGDQSFLVQEYLPNAtDYRVMIL 186
Cdd:PRK02186  175 ------RRAGTRAALVQAYVEGD-EYSVETL 198
MfnD COG1821
Tyramine-glutamate ligase MfnD (methanofuran biosynthesis), ATP-grasp superfamily [Coenzyme ...
 85-264 1.97e-04

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


Pssm-ID: 441426 [Multi-domain]  Cd Length: 323  Bit Score: 42.22  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  85 NKAEVLARLGRAELPVPKSVyvsndvgadELADVFERFEPPVVVKPNsttRGVGVAKAHdldsflgICDYLSLVHDYKAT 164
Cdd:COG1821   124 DKLLTAELLAAAGIPTPPTF---------PADDAPPLLAGPWVVKPD---DGAGSEGTR-------LFDDPAALRAREAR 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 165 GDqSFLVQEYLPN--------ATDYRVMILegeyvgAVERRLpdAAVSEGQWKHNvhrgaeatGVELP------DEYREL 230
Cdd:COG1821   185 GA-GLIVQPYIEGeaaslsllCGRGGALLL------SINRQR--IEVDGGRFSYL--------GGTVPaehprkEELQAL 247

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1668705387 231 AERVGAAleIPFL----GVDLLETDDRLVINETNARPT 264
Cdd:COG1821   248 AQKVAEA--LPGLrgyvGVDLILTADGPVVVEVNPRLT 283
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 20-195 3.63e-04

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 41.25  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  20 LAERGIRVHHVPVRERTVA-LDDppwepDAYDVGF-VYPGRLMEGGVADALLEvpWLN---DHETVLTS-------RNKA 87
Cdd:PRK01372   32 LREAGYDAHPIDPGEDIAAqLKE-----LGFDRVFnALHGRGGEDGTIQGLLE--LLGipyTGSGVLASalamdklRTKL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  88 eVLARLGraeLPVPKSVYVSndvGADELADVFERFEPPVVVKPNSTTRGVGVAKAHDLDSFLGICdylslvhDYKATGDQ 167
Cdd:PRK01372  105 -VWQAAG---LPTPPWIVLT---REEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL-------ELAFKYDD 170

                         170       180
                  ....*....|....*....|....*...
gi 1668705387 168 SFLVQEYLPnATDYRVMILEGEYVGAVE 195
Cdd:PRK01372  171 EVLVEKYIK-GRELTVAVLGGKALPVIE 197
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 85-264 1.52e-03

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: 38.52  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387  85 NKAEVLARLGRAELPVPKSVyvsndvGADELADVFERFeppvVVKPNSTTRGVGVAKAHDLDSFLGICDYLslvhdykat 164
Cdd:pfam02655   3 DKLKTYKALKNAGVPTPETL------QAEELLREEKKY----VVKPRDGCGGEGVRKVENGREDEAFIENV--------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1668705387 165 gdqsfLVQEYLPnATDYRVMIL---EGEYVGAVERRLPDAAVSEgqwkhNVHRGAEATG-VELPDEYRELAERVGAALE- 239
Cdd:pfam02655  64 -----LVQEFIE-GEPLSVSLLsdgEKALPLSVNRQYIDNGGSG-----FVYAGNVTPSrTELKEEIIELAEEVVECLPg 132

                         170       180
                  ....*....|....*....|....*.
gi 1668705387 240 -IPFLGVDLLETDDRLVINETNARPT 264
Cdd:pfam02655 133 lRGYVGVDLVLKDNEPYVIEVNPRIT 158
 
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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