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Conserved domains on  [gi|2526693799|ref|WP_288062648|]
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RimK family alpha-L-glutamate ligase [Rodentibacter caecimuris]

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

 Zoom to residue level

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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 ...
 1-294 2.87e-97

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: 287.99  E-value: 2.87e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPHFDiyyqpkegnTYLLPDYDAVIPRfgTASTKMG 80
Cdd:COG0189     2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPELYR---------GEDLSEFDAVLPR--IDPPFYG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  81 CAVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLM 160
Cdd:COG0189    71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 161 ENAQSAVSILETLKQV-SVPVLLQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIA 239
Cdd:COG0189   151 EDEDALESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2526693799 240 IKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILYLEK 294
Cdd:COG0189   231 LRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEA 285
 
Name Accession Description Interval E-value
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-294 2.87e-97

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: 287.99  E-value: 2.87e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPHFDiyyqpkegnTYLLPDYDAVIPRfgTASTKMG 80
Cdd:COG0189     2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPELYR---------GEDLSEFDAVLPR--IDPPFYG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  81 CAVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLM 160
Cdd:COG0189    71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 161 ENAQSAVSILETLKQV-SVPVLLQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIA 239
Cdd:COG0189   151 EDEDALESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2526693799 240 IKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILYLEK 294
Cdd:COG0189   231 LRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEA 285
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
1-294 1.23e-96

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 286.80  E-value: 1.23e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPhfDIYYQPKEgntylLPDYDAVIPRFGTASTKMG 80
Cdd:PRK10446    1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAAS--SIHYKGRK-----LPHFDAVIPRIGTAITFYG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  81 CAVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEvEAKASVQKMV--SPLILKTLNGSQGIGVM 158
Cdd:PRK10446   74 TAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSP-DDTSDLIDMVggAPLVVKLVEGTQGIGVV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 159 LMENAQSAVSILETLKQVSVPVLLQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQI 238
Cdd:PRK10446  153 LAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREI 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2526693799 239 AIKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILYLEK 294
Cdd:PRK10446  233 AIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIER 288
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-291 1.84e-96

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: 285.39  E-value: 1.84e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   2 KFLMLCREPRLySSQRLKEAAIQCGHEMDILDPNRCILKLTEnsphfdiyyQPKEgntylLPDYDAVIPRFgtASTKMGC 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE---------GPRA-----LAELDVVIVRI--VSMFRGL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  82 AVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLME 161
Cdd:TIGR00768  64 AVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 162 NAQSAVSILETLKQVSVPV---LLQDFIEEADGADIRCFVIGDKVVASMQRFgQDGEFRANIHRGGSAQKITLSEQEKQI 238
Cdd:TIGR00768 144 DRQAAESLLEHFEQLNGPQnlfLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEEL 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2526693799 239 AIKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILY 291
Cdd:TIGR00768 223 AIKAAKALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDY 275
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 104-292 3.46e-75

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: 228.15  E-value: 3.46e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMV--SPLILKTLNGSQGIGVMLMENAQSAVSILETLKQvsvPVL 181
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNE---QIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 182 LQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIAIKATKALGLAVSGVDFIRSKSG 261
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2526693799 262 LLVLEVNASPGLDMIEKTSGVDIALQMILYL 292
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
18-285 1.17e-43

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 150.46  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  18 LKEAAIQCGHEMDILDPNRcilklTENSPHFDIYYQPKEGNtylLPDYDAVIPR------FGTASTKMGcaVLRHFQAKG 91
Cdd:NF040720   17 LIRACEKKDIDPVLIDLSK-----IEVSIGSDIKFKYGKIN---LLDLDAIFVRdigagsNEGVSFRFD--VLRYLEELG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  92 IYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMvSPLILKTLNGSQGIGVMLMENAQSAVSILE 171
Cdd:NF040720   87 IPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKF-EDAVLKPVFGYKGKGIVRIKNGESIATKLE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 172 TLKQV--SVPVL-LQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIAIKATKALGL 248
Cdd:NF040720  166 LLNEFkeERGMLyIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQEELAIKAAEALGL 245

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2526693799 249 AVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIA 285
Cdd:NF040720  246 VYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIA 282
 
Name Accession Description Interval E-value
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 1-294 2.87e-97

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: 287.99  E-value: 2.87e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPHFDiyyqpkegnTYLLPDYDAVIPRfgTASTKMG 80
Cdd:COG0189     2 MKIAILTDPPDKDSTKALIEAAQRRGHEVEVIDPDDLTLDLGRAPELYR---------GEDLSEFDAVLPR--IDPPFYG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  81 CAVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLM 160
Cdd:COG0189    71 LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 161 ENAQSAVSILETLKQV-SVPVLLQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIA 239
Cdd:COG0189   151 EDEDALESILEALTELgSEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEERELA 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2526693799 240 IKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILYLEK 294
Cdd:COG0189   231 LRAAPALGLDFAGVDLIEDDDGPLVLEVNVTPGFRGLERATGVDIAEAIADYLEA 285
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
1-294 1.23e-96

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 286.80  E-value: 1.23e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPhfDIYYQPKEgntylLPDYDAVIPRFGTASTKMG 80
Cdd:PRK10446    1 MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAAS--SIHYKGRK-----LPHFDAVIPRIGTAITFYG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  81 CAVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEvEAKASVQKMV--SPLILKTLNGSQGIGVM 158
Cdd:PRK10446   74 TAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSP-DDTSDLIDMVggAPLVVKLVEGTQGIGVV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 159 LMENAQSAVSILETLKQVSVPVLLQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQI 238
Cdd:PRK10446  153 LAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREI 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2526693799 239 AIKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILYLEK 294
Cdd:PRK10446  233 AIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIER 288
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 2-291 1.84e-96

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: 285.39  E-value: 1.84e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   2 KFLMLCREPRLySSQRLKEAAIQCGHEMDILDPNRCILKLTEnsphfdiyyQPKEgntylLPDYDAVIPRFgtASTKMGC 81
Cdd:TIGR00768   1 KIAILYDRIRL-DEKMLKEAAEELGIDYKVVTPPAINLTFNE---------GPRA-----LAELDVVIVRI--VSMFRGL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  82 AVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLME 161
Cdd:TIGR00768  64 AVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 162 NAQSAVSILETLKQVSVPV---LLQDFIEEADGADIRCFVIGDKVVASMQRFgQDGEFRANIHRGGSAQKITLSEQEKQI 238
Cdd:TIGR00768 144 DRQAAESLLEHFEQLNGPQnlfLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTEEIEEL 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2526693799 239 AIKATKALGLAVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIALQMILY 291
Cdd:TIGR00768 223 AIKAAKALGLDVAGVDLLESEDGLLVNEVNANPEFKNSVKTTGVNIAGKLLDY 275
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 104-292 3.46e-75

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: 228.15  E-value: 3.46e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMV--SPLILKTLNGSQGIGVMLMENAQSAVSILETLKQvsvPVL 181
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKrqFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATNE---QIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 182 LQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIAIKATKALGLAVSGVDFIRSKSG 261
Cdd:pfam08443  78 VQEFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2526693799 262 LLVLEVNASPGLDMIEKTSGVDIALQMILYL 292
Cdd:pfam08443 158 LLVCEVNSSPGLEGIEKTLGINIAIKIIASI 188
MptN_Meth NF040720
tetrahydromethanopterin:alpha-L-glutamate ligase;
18-285 1.17e-43

tetrahydromethanopterin:alpha-L-glutamate ligase;


Pssm-ID: 468684 [Multi-domain]  Cd Length: 290  Bit Score: 150.46  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  18 LKEAAIQCGHEMDILDPNRcilklTENSPHFDIYYQPKEGNtylLPDYDAVIPR------FGTASTKMGcaVLRHFQAKG 91
Cdd:NF040720   17 LIRACEKKDIDPVLIDLSK-----IEVSIGSDIKFKYGKIN---LLDLDAIFVRdigagsNEGVSFRFD--VLRYLEELG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  92 IYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMvSPLILKTLNGSQGIGVMLMENAQSAVSILE 171
Cdd:NF040720   87 IPVINPPEAIQNAANKYHTSFLLAKAGIPTPKTVVTEDIEKALEWIEKF-EDAVLKPVFGYKGKGIVRIKNGESIATKLE 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 172 TLKQV--SVPVL-LQDFIEEADGADIRCFVIGDKVVASMQRFGQDGEFRANIHRGGSAQKITLSEQEKQIAIKATKALGL 248
Cdd:NF040720  166 LLNEFkeERGMLyIQEFIENNPGRDIRAFVVDDEVIGAIYRKAPEGNWINNLSQGGTPERCELTEEQEELAIKAAEALGL 245

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2526693799 249 AVSGVDFIRSKSGLLVLEVNASPGLDMIEKTSGVDIA 285
Cdd:NF040720  246 VYAGVDLIESKDGLKVLEVNATPSWAGIYKVWGINIA 282
Rimk_N pfam18030
RimK PreATP-grasp domain; This is the N-terminal domain found in Escherichia coli RimK ...
 1-97 1.49e-37

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: 128.36  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799   1 MKFLMLCREPRLYSSQRLKEAAIQCGHEMDILDPNRCILKLTENSPHfdIYYQPKEgntylLPDYDAVIPRFGTASTKMG 80
Cdd:pfam18030   1 MKIAILSRNPNLYSTRRLVEAAEARGHEVEVIDPLRCYMNIESGKPE--IHYKGEP-----LPDFDAVIPRIGASITFYG 73

                          90
                  ....*....|....*..
gi 2526693799  81 CAVLRHFQAKGIYCLNT 97
Cdd:pfam18030  74 TAVLRQFEMMGVFSLNS 90
PRK12458 PRK12458
glutathione synthetase; Provisional
 13-294 6.30e-22

glutathione synthetase; Provisional


Pssm-ID: 183536 [Multi-domain]  Cd Length: 338  Bit Score: 93.93  E-value: 6.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  13 YSSQRLKEAAIQCGHEMDILDPNRCIL------------------KLTENSPHFdiyYQPKEGNTYLLP--DYDAVIPRF 72
Cdd:PRK12458   11 DTTLRLAHEAVNRGHEVAYTTPGDLTIrddealafcavtkkgkkyKKPENFLSF---LKKAEFKKERLPlaGFDVIFLRA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  73 GTASTKM--------GCAVLRHFQAKGIYCLNTEKAFLTARDK--WQSLqilrEQNIaVPNSQLSGTEVEAKASVQKMVS 142
Cdd:PRK12458   88 NPPLDPLarnwadsvGIAFGRLAARDGVLVVNDPDGLRIANNKlyFQSF----PEEV-RPTTHISRNKEYIREFLEESPG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 143 -PLILKTLNGSQGIGVMLME-NAQSAV-SILETLKQvSVPVLLQDFIEEADGADIRCFVI------GDKVVASMQRFGQD 213
Cdd:PRK12458  163 dKMILKPLQGSGGQGVFLIEkSAQSNLnQILEFYSG-DGYVIAQEYLPGAEEGDVRILLLngepleRDGHYAAMRRVPAG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 214 GEFRANIHRGGSAQKITLSEQEKQIAIKATKAL---GLAVSGVDFIRSKsgllVLEVNA-SP-GLDMIEKTSGVDIALQM 288
Cdd:PRK12458  242 GDVRSNVHAGGSVVKHTLTKEELELCEAIRPKLvrdGLFFVGLDIVGDK----LVEVNVfSPgGLTRINKLNKIDFVEDI 317


                  ....*.
gi 2526693799 289 ILYLEK 294
Cdd:PRK12458  318 IEALER 323
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 96-289 1.14e-15

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: 74.91  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  96 NTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLMENAQSAVSILETLKQ 175
Cdd:COG0439    44 PSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 176 VSV------PVLLQDFIE----EADGadircFVIGDKVV-ASMQRFGQDGEFRanIHRGGSAQ-KITLSEQEK--QIAIK 241
Cdd:COG0439   124 EAKagspngEVLVEEFLEgreySVEG-----LVRDGEVVvCSITRKHQKPPYF--VELGHEAPsPLPEELRAEigELVAR 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2526693799 242 ATKALGLA--VSGVDFIRSKSGLLVL-EVNASPG----LDMIEKTSGVDIALQMI 289
Cdd:COG0439   197 ALRALGYRrgAFHTEFLLTPDGEPYLiEINARLGgehiPPLTELATGVDLVREQI 251
PRK05246 PRK05246
glutathione synthetase; Provisional
 145-294 2.28e-15

glutathione synthetase; Provisional


Pssm-ID: 235371 [Multi-domain]  Cd Length: 316  Bit Score: 74.75  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 145 ILKTLNGSQGIGV-MLMENAQSAVSILETL-KQVSVPVLLQDFIEEADGADIRCFVIGDKVV-ASMQRFGQDGEFRANIH 221
Cdd:PRK05246  158 ILKPLDGMGGAGIfRVKADDPNLGSILETLtEHGREPVMAQRYLPEIKEGDKRILLVDGEPVgYALARIPAGGETRGNLA 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526693799 222 RGGSAQKITLSEQEKQIAIK---ATKALGLAVSGVDFIrsksGLLVLEVN-ASP-GLDMIEKTSGVDIALQMILYLEK 294
Cdd:PRK05246  238 AGGRGEATPLTERDREICAAigpELKERGLIFVGIDVI----GDYLTEINvTSPtGIREIERLTGVDIAGMLWDAIEA 311
GSH-S_ATP pfam02955
Prokaryotic glutathione synthetase, ATP-grasp domain;
145-272 6.10e-15

Prokaryotic glutathione synthetase, ATP-grasp domain;


Pssm-ID: 427078 [Multi-domain]  Cd Length: 175  Bit Score: 71.44  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 145 ILKTLNGSQGIGVMLMENAQSAV-SILETLKQV-SVPVLLQDFIEEADGADIRCFVI-GDKVVASMQRFGQDGEFRANIH 221
Cdd:pfam02955  35 ILKPLDGMGGAGIFRVKKGDPNLnVILETLTQYgTRPVMAQRYLPEIKEGDKRILLInGEPIGYALARIPAAGEFRGNLA 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2526693799 222 RGGSAQKITLSEQEKQIA--IKAT-KALGLAVSGVDFIrsksGLLVLEVN-ASPG 272
Cdd:pfam02955 115 AGGRGEATPLTERDREICetIGPKlKERGLFFVGLDVI----GDYLTEINvTSPT 165
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 104-273 1.21e-11

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: 63.97  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAVPNSQL--SGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLMENAQSAVSILETLKQVSVPVL 181
Cdd:COG1181    93 AMDKALTKRVLAAAGLPTPPYVVlrRGELADLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVL 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 182 LQDFIeeaDGADIRCFVIGDK-VVAS-MQRFGQDGEFR--ANIHRGGSAQKIT---LSEQE----KQIAIKATKALGLA- 249
Cdd:COG1181   173 VEEFI---DGREVTVGVLGNGgPRALpPIEIVPENGFYdyEAKYTDGGTEYICparLPEELeeriQELALKAFRALGCRg 249

                         170       180
                  ....*....|....*....|....*
gi 2526693799 250 VSGVDFIRSKSG-LLVLEVNASPGL 273
Cdd:COG1181   250 YARVDFRLDEDGePYLLEVNTLPGM 274
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 104-275 2.19e-11

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 64.41  E-value: 2.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVML-MENAQSAVSILETLKQVSVPVLL 182
Cdd:PRK14016  212 ACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSDVIV 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 183 QDFIEeadGADIRCFVIGDKVVASMQR---------------------------FGQD---------------------- 213
Cdd:PRK14016  292 ERYIP---GKDHRLLVVGGKLVAAARRepphvigdgkhtirelieivnqdprrgEGHEkpltkiklddiallelakqgyt 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 214 -------GE---FR--ANIHRGGSAQKIT--LSEQEKQIAIKATKALGLAVSGVDFI-----RS--KSGLLVLEVNASPG 272
Cdd:PRK14016  369 ldsvppkGEkvyLRrnANLSTGGTAIDVTdeVHPENAAIAERAAKIIGLDIAGVDVVcedisKPleEQGGAIVEVNAAPG 448


                  ...
gi 2526693799 273 LDM 275
Cdd:PRK14016  449 LRM 451
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 104-272 4.52e-10

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: 57.40  E-value: 4.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAVPNS-QLSGTEVEAKasvqkmvsPLILKTLNGSQGIGVMLMENAQSAVSILEtlkqvsvPVLL 182
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETlQAEELLREEK--------KYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLV 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 183 QDFIEE--------ADGADIRCFVIGDKVVasmqrfgqDGEFRANIHRGGSAQKIT-LSEQEKQIAIKATKAL-GLA-VS 251
Cdd:pfam02655  66 QEFIEGeplsvsllSDGEKALPLSVNRQYI--------DNGGSGFVYAGNVTPSRTeLKEEIIELAEEVVECLpGLRgYV 137

                         170       180
                  ....*....|....*....|.
gi 2526693799 252 GVDFIRSKSGLLVLEVNASPG 272
Cdd:pfam02655 138 GVDLVLKDNEPYVIEVNPRIT 158
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 88-292 9.34e-10

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 59.48  E-value: 9.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  88 QAKGIYCLNTEkAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLMENAQSAV 167
Cdd:PRK02186   90 RRLGLPAANTE-AIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 168 SILETLKQVSVP-VLLQDFIeEADGADIRCFVIGDK--VVASMQRF----------GQDgeFRANIhrggsaqkitLSEQ 234
Cdd:PRK02186  169 AHCAALRRAGTRaALVQAYV-EGDEYSVETLTVARGhqVLGITRKHlgppphfveiGHD--FPAPL----------SAPQ 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526693799 235 EKQI---AIKATKALGLAV--SGVDFIRSKSGLLVLEVNA--SPGL--DMIEKTSGVDIALQMI-LYL 292
Cdd:PRK02186  236 RERIvrtVLRALDAVGYAFgpAHTELRVRGDTVVIIEINPrlAGGMipVLLEEAFGVDLLDHVIdLHL 303
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 106-273 3.59e-09

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 56.66  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 106 DKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQGIGVMLMENAQSAVSILETLKQVSVPVLLQDF 185
Cdd:PRK01372   98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 186 IEeadGADIRCFVIGDKVVASMqRFGQDGEF---RANIHRGGSAQKIT--LS-EQEKQI---AIKATKALGLA-VSGVDF 255
Cdd:PRK01372  178 IK---GRELTVAVLGGKALPVI-EIVPAGEFydyEAKYLAGGTQYICPagLPaEIEAELqelALKAYRALGCRgWGRVDF 253

                         170
                  ....*....|....*....
gi 2526693799 256 IRSKSGLL-VLEVNASPGL 273
Cdd:PRK01372  254 MLDEDGKPyLLEVNTQPGM 272
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 87-269 2.47e-08

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 54.12  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  87 FQAKGIYCLNTEKAFL-TARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVS--PLILKTLNGSQGIGVMLMENA 163
Cdd:PRK12767   91 FEEIGVKVLVSSKEVIeICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGELqfPLFVKPRDGSASIGVFKVNDK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 164 QSavsiLETLKQVSVPVLLQDFIEEAD-GADIRCFVIGdKVVAS--MQRFgqdgEFRAnihrGGSAQKITLSEQE-KQIA 239
Cdd:PRK12767  171 EE----LEFLLEYVPNLIIQEFIEGQEyTVDVLCDLNG-EVISIvpRKRI----EVRA----GETSKGVTVKDPElFKLA 237

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2526693799 240 IKATKALGLAvsG---VDFIRSKSGLLVLEVNA 269
Cdd:PRK12767  238 ERLAEALGAR--GplnIQCFVTDGEPYLFEINP 268
PylC COG2232
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ...
 82-284 1.24e-07

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: 52.23  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  82 AVLRHFQAKGIYCLNTEKAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEakasvqkmvSPLILKTLNGSQGIGVMLME 161
Cdd:COG2232    88 ELLERLARRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPETRFEPPPDP---------GPWLVKPIGGAGGWHIRPAD 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 162 NAQSAvsiletlkqvSVPVLLQDFIEE--------ADGADIRcfVIGdkvvASMQRFGQDGE--FRAnihrGGSAQKITL 231
Cdd:COG2232   159 SEAPP----------APGRYFQRYVEGtpasvlflADGSDAR--VLG----FNRQLIGPAGErpFRY----GGNIGPLAL 218

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 232 SEQEKQ----IAIKATKALGLAVS-GVDFIRSKSGLLVLEVNASPG--LDMIEKTSGVDI 284
Cdd:COG2232   219 PPALAEemraIAEALVAALGLVGLnGVDFILDGDGPYVLEVNPRPQasLDLYEDATGGNL 278
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 105-268 2.81e-06

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 48.34  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 105 RDKWQslQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILK---TLNGSqgiGVMLMENAQSAVSILETLKQVSV--P 179
Cdd:COG0458   115 RELFK--ELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRpsyVLGGR---GMGIVYNEEELEEYLERALKVSPdhP 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 180 VLLQDFIEEA---------DGADiRCFVIGdkvvaSMQRFgqdgEfRANIHRGGSA-----QkiTLSEQEKQIAIKATKA 245
Cdd:COG0458   190 VLIDESLLGAkeievdvvrDGED-NVIIVG-----IMEHI----E-PAGVHSGDSIcvappQ--TLSDKEYQRLRDATLK 256

                         170       180
                  ....*....|....*....|....*...
gi 2526693799 246 L--GLAVSG---VDFIRSKSGLLVLEVN 268
Cdd:COG0458   257 IarALGVVGlcnIQFAVDDGRVYVIEVN 284
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 95-277 1.02e-05

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: 46.18  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  95 LNTEKAFLTARDKWQSLQILREQNIAVPnsQLSGTEV------EAKASVQKMVSPLILKTLNGSQGIGVML-------ME 161
Cdd:pfam14397  10 YNPRALYPLVDDKLKFKQLALRAGLPVP--KLYGVISighdisRLDAFVRSLPPGFVIKPAKGSGGKGILVitrrgdqDY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 162 NAQSAVSILE--------TLKQVSVPVLLQDFIEEADG---------ADIR--CFVIGDK--VVASMQRFGQDGEFRANI 220
Cdd:pfam14397  88 FKSSGCRILLdelkrhvsSLGGKPDVALVEERIVQDPVfaklspesvNTIRviTFLLDNGvpVMPAMLRLGTGASLVDNL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 221 HRGGSAQKI----------TLSEQEKQIAIK---------------------------ATKALGLAVSGVDF-IRSKSGL 262
Cdd:pfam14397 168 HQGGVGVGIdlatgvlfkpALQAVQYGEPIEhhpdtgvkfrgfqipnwdqilelaaecAQTLPGLGYVGWDIvIDENGGP 247

                         250
                  ....*....|....*
gi 2526693799 263 LVLEVNASPGLDMIE 277
Cdd:pfam14397 248 LLLELNARPGLGIFQ 262
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
106-292 2.58e-05

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 45.30  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 106 DKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTLNGSQ--------GIGVMLMENAQSAVSILETLKQVS 177
Cdd:COG3919   117 DKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPADSVGydelsfpgKKKVFYVDDREELLALLRRIAAAG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 178 VPVLLQDFIEEADGADIRCFVIgdkvvasmqrFGQDGEFRAN-IHR---------GGSAQKITLSEQE-KQIAIKATKAL 246
Cdd:COG3919   197 YELIVQEYIPGDDGEMRGLTAY----------VDRDGEVVATfTGRklrhyppagGNSAARESVDDPElEEAARRLLEAL 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2526693799 247 GLA-VSGVDFIR-SKSG-LLVLEVNASPG--LDMIEKtSGVDIALQMILYL 292
Cdd:COG3919   267 GYHgFANVEFKRdPRDGeYKLIEINPRFWrsLYLATA-AGVNFPYLLYDDA 316
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
14-275 3.42e-05

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


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 45.30  E-value: 3.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  14 SSQRLKEAAIQCGHEMDILDPNRCILKLTENSpHFDiYYqpKEGNTYLLPDYdaVIPrfgtastkmgcavlrhfqakgiy 93
Cdd:PRK02471  433 STQILLFDAIQRGIQVEILDEQDQFLKLQKGD-HVE-YV--KNGNMTSKDNY--ISP----------------------- 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  94 clntekafLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVS-PLILKTLNGSQGIGVMLMENAQSAVSILET 172
Cdd:PRK02471  484 --------LIMENKVVTKKILAEAGFPVPAGDEFTSLEEALADYSLFADkAIVVKPKSTNFGLGISIFKEPASLEDYEKA 555

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 173 LKQV---SVPVLLQDFIEeadGADIRCFVIGDKVVASMQRF-----GqDGEF-------RANIH--RGGSA----QKITL 231
Cdd:PRK02471  556 LEIAfreDSSVLVEEFIV---GTEYRFFVLDGKVEAVLLRVpanvvG-DGIHtvrelvaQKNQDplRGTDHrtplEKIQL 631

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 232 SEQE----------------------------------------------KQIAIKATKALGLAVSGVDFI--------- 256
Cdd:PRK02471  632 GEIErlmlkqqgltpdsipkkgeivylrensnistggdsidmtddmddsyKQIAVKAAKALGAKICGVDLIipdltqpas 711

                         330
                  ....*....|....*....
gi 2526693799 257 RSKSGLLVLEVNASPGLDM 275
Cdd:PRK02471  712 PEHPNYGIIELNFNPAMYM 730
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 143-283 1.74e-03

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: 38.84  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 143 PLILKTLNGSQGIGVMLMENAQSAVSILETLKQVSVPVLLQDFIEeadGADIRCFVIGD---KVVASMQRFGQDGEFRAN 219
Cdd:pfam07478  38 PVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEGIE---GREIECAVLGNedpEVSPVGEIVPSGGFYDYE 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 220 IHRGGSAQKI--------TLSEQEKQIAIKATKALGLAVSG-VDFIRSKSGLLVL-EVNASPG------LDMIEKTSGVD 283
Cdd:pfam07478 115 AKYIDDSAQIvvpadleeEQEEQIQELALKAYKALGCRGLArVDFFLTEDGEIVLnEVNTIPGftsismFPKLAAAAGVS 194
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 105-285 2.50e-03

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: 39.60  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  105 RDKWQslQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKTlngSQGIGVMLMENAQSAVSILETLKQVSV-----P 179
Cdd:TIGR01369  670 REKFS--ELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRP---SYVLGGRAMEIVYNEEELRRYLEEAVAvspehP 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  180 VLLQDFIEEADGADIRCFVIGDKVVAS--MQRFgqdgEfRANIHRGGSA-----QKITLSEQEKQIAIKATKALGLAVSG 252
Cdd:TIGR01369  745 VLIDKYLEDAVEVDVDAVSDGEEVLIPgiMEHI----E-EAGVHSGDSTcvlppQTLSAEIVDRIKDIVRKIAKELNVKG 819

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2526693799  253 ---VDFIRSKSGLLVLEVN--ASPGLDMIEKTSGVDIA 285
Cdd:TIGR01369  820 lmnIQFAVKDGEVYVIEVNprASRTVPFVSKATGVPLA 857
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 104-273 3.19e-03

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 38.73  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 104 ARDKWQSLQILREQNIAV-PNSQLS--GTEVEAKASVQKMVS---PLILKTLNGSQGIGVMLMENAQSAVSILETLKQVS 177
Cdd:PRK14572  128 AMDKTRANQIFLQSGQKVaPFFELEklKYLNSPRKTLLKLESlgfPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESD 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 178 VPVLLQDFIEeadGADIRCFVIGDKVVASMQRF----------GQDGEFRANIHRGGSaQKIT---LSEQE----KQIAI 240
Cdd:PRK14572  208 SKVMSQSFLS---GTEVSCGVLERYRGGKRNPIalpateivpgGEFFDFESKYKQGGS-EEITparISDQEmkrvQELAI 283

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2526693799 241 KATKALGL-AVSGVDFIRSKSGLLVLEVNASPGL 273
Cdd:PRK14572  284 RAHESLGCkGYSRTDFIIVDGEPHILETNTLPGM 317
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 99-268 4.43e-03

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 38.21  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799  99 KAFLTARDKWQSLQILREQNIAVPNSQLSGTEVEAKASVQKMVSPLILKT-LNGSQGIGVMLMENAQSAVSILETLKqvS 177
Cdd:PRK06019   93 DALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTrRGGYDGKGQWVIRSAEDLEAAWALLG--S 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526693799 178 VPVLLQDFIEeadgadircFvigDK---VVASmqRfGQDGEFRA-----NIHRGG--------SAQKITLSEQEKQIAIK 241
Cdd:PRK06019  171 VPCILEEFVP---------F---ERevsVIVA--R-GRDGEVVFyplveNVHRNGilrtsiapARISAELQAQAEEIASR 235

                         170       180
                  ....*....|....*....|....*...
gi 2526693799 242 ATKALGLA-VSGVDFIRSKSGLLVleVN 268
Cdd:PRK06019  236 IAEELDYVgVLAVEFFVTGDGELL--VN 261
 
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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