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Conserved domains on  [gi|490310162|ref|WP_004204880|]
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MULTISPECIES: D-alanine--D-alanine ligase [Klebsiella]

Protein Classification

D-alanine--D-alanine ligase family protein( domain architecture ID 11479728)

D-alanine--D-alanine ligase family protein similar to D-alanine--D-alanine ligase that catalyzes the synthesis of D-alanyl-D-alanine, an essential component of bacterial peptidoglycan, and is involved in cell wall formation

EC:  6.3.2.-
Gene Ontology:  GO:0009252|GO:0008716|GO:0046872|GO:0005524
SCOP:  4002041|4003870

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ddl PRK01966
D-alanine--D-alanine ligase;
1-352 0e+00

D-alanine--D-alanine ligase;


:

Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 542.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAGNYLLNAQDPARIALRpstvtlaqip 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDKEDLS---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 greaqQLINAESGQplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01966  71 -----LLILPSGGS--EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDhPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 241 ASTCGEIVLNSEFYAYDTKYIDDQgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLDGS-AELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301

                        330       340       350
                 ....*....|....*....|....*....|..
gi 490310162 321 GFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
 
Name Accession Description Interval E-value
ddl PRK01966
D-alanine--D-alanine ligase;
1-352 0e+00

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 542.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAGNYLLNAQDPARIALRpstvtlaqip 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDKEDLS---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 greaqQLINAESGQplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01966  71 -----LLILPSGGS--EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDhPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 241 ASTCGEIVLNSEFYAYDTKYIDDQgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLDGS-AELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301

                        330       340       350
                 ....*....|....*....|....*....|..
gi 490310162 321 GFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 4-351 3.72e-159

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: 448.02  E-value: 3.72e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   4 MRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLwhindagnyllnaqdPARIALrpstvtlaqipgre 83
Cdd:COG1181    1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDL---------------PAALKE-------------- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  84 aqqlinaesgqplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTR 163
Cdd:COG1181   52 -------------LKPDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 164 ANRAqfSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDHPQAST 243
Cdd:COG1181  119 GELA--DLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 244 CGEIVLNSEFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLPGFT 323
Cdd:COG1181  197 PIEIVPENGFYDYEAKYTDG-GTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275

                        330       340
                 ....*....|....*....|....*...
gi 490310162 324 NISMYPKLWQASGLDYTSLITRLIELAL 351
Cdd:COG1181  276 PTSLLPKAAAAAGISYEELIERIIELAL 303
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 5-350 4.89e-151

D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273498 [Multi-domain]  Cd Length: 315  Bit Score: 428.24  E-value: 4.89e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162    5 RVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWhindagnyllNAQDPARIALrpstvtlaqipgrea 84
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLIL--------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   85 qqlinaESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTRa 164
Cdd:TIGR01205  56 ------ELGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  165 NRAQFSFAD---VEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDH--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  240 QASTCGEIVLnseFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIEG---FYDYEAKYLDG-STEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284

                         330       340       350
                  ....*....|....*....|....*....|.
gi 490310162  320 PGFTNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 147-348 1.73e-106

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: 310.79  E-value: 1.73e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  147 LLRDAGLAVAPFITLTRANRAQ---FSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQG 223
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWKLnpkEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  224 IKGREIECAVLGNDHPQASTCGEIVLNSEFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDV 303
Cdd:pfam07478  81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDD-SAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 490310162  304 FLTADNEVVINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIE 348
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
 
Name Accession Description Interval E-value
ddl PRK01966
D-alanine--D-alanine ligase;
1-352 0e+00

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 542.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAGNYLLNAQDPARIALRpstvtlaqip 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADDDNDKEDLS---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 greaqQLINAESGQplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01966  71 -----LLILPSGGS--EEVDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDhPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 241 ASTCGEIVLNSEFYAYDTKYIDDQgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLDGS-AELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301

                        330       340       350
                 ....*....|....*....|....*....|..
gi 490310162 321 GFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 4-351 3.72e-159

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: 448.02  E-value: 3.72e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   4 MRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLwhindagnyllnaqdPARIALrpstvtlaqipgre 83
Cdd:COG1181    1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDL---------------PAALKE-------------- 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  84 aqqlinaesgqplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTR 163
Cdd:COG1181   52 -------------LKPDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 164 ANRAqfSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDHPQAST 243
Cdd:COG1181  119 GELA--DLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 244 CGEIVLNSEFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLPGFT 323
Cdd:COG1181  197 PIEIVPENGFYDYEAKYTDG-GTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275

                        330       340
                 ....*....|....*....|....*...
gi 490310162 324 NISMYPKLWQASGLDYTSLITRLIELAL 351
Cdd:COG1181  276 PTSLLPKAAAAAGISYEELIERIIELAL 303
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 5-350 4.89e-151

D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases, but a number of antibiotic resistance proteins score above the trusted cutoff of this model. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273498 [Multi-domain]  Cd Length: 315  Bit Score: 428.24  E-value: 4.89e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162    5 RVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWhindagnyllNAQDPARIALrpstvtlaqipgrea 84
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLIL--------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   85 qqlinaESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTRa 164
Cdd:TIGR01205  56 ------ELGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  165 NRAQFSFAD---VEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNDH--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  240 QASTCGEIVLnseFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIEG---FYDYEAKYLDG-STEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284

                         330       340       350
                  ....*....|....*....|....*....|.
gi 490310162  320 PGFTNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 1-353 4.45e-109

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 321.29  E-value: 4.45e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVllGIDkqglwhindagnyllnaqdparialrpstvtlaqiP 80
Cdd:PRK01372   2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAH--PID-----------------------------------P 44

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 GREAQQLINAEsgqplaAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK01372  45 GEDIAAQLKEL------GFDRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIV 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTRANraqfSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGNdhpQ 240
Cdd:PRK01372 119 LTREE----DLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGG---K 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 241 ASTCGEIVLNSEFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINTLP 320
Cdd:PRK01372 192 ALPVIEIVPAGEFYDYEAKYLAG-GTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQP 270

                        330       340       350
                 ....*....|....*....|....*....|...
gi 490310162 321 GFTNISMYPKLWQASGLDYTSLITRLIELALER 353
Cdd:PRK01372 271 GMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 147-348 1.73e-106

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: 310.79  E-value: 1.73e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  147 LLRDAGLAVAPFITLTRANRAQ---FSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQG 223
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWKLnpkEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  224 IKGREIECAVLGNDHPQASTCGEIVLNSEFYAYDTKYIDDqGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDV 303
Cdd:pfam07478  81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYIDD-SAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 490310162  304 FLTADNEVVINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIE 348
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 3-355 1.39e-74

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 235.11  E-value: 1.39e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAI-DKSRFDVVLLGIDK-QGLWHINDAgnyllnAQDPARIALRPSTVTLAQIP 80
Cdd:PRK14570   2 KKNLMLIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWYLLDS------VPDPPKLIKRDVLPIVSLIP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 GreAQQLINAESGQplaaIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK14570  76 G--CGIFVNNKNLE----IDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTR----ANRAQFSfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLGN 236
Cdd:PRK14570 150 FRKydyfLDKEGIK-KDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGN 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 237 DHPQASTCGEIVLNS-EFYAYDTKYIDDQGAKVV--VPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTAD-NEVV 312
Cdd:PRK14570 229 EQIKIFTPGEIVVQDfIFYDYDAKYSTIPGNSIVfnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIY 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 490310162 313 INEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALERHA 355
Cdd:PRK14570 309 LNEINTIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYI 351
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
3-353 6.87e-56

bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 195.42  E-value: 6.87e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWhindagnyllnaqdparialrpSTVTL--AQIP 80
Cdd:PRK14573 451 KLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLW----------------------ETVSSleTAIE 508

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 GREAQQLINAESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFIT 160
Cdd:PRK14573 509 EDSGKSVLSSEIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQP 588

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 161 LTRANRAQ---FSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKG-REIECAVLGN 236
Cdd:PRK14573 589 LTLAGWKRepeLCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGsREIEVSCLGD 668

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 237 dhpqASTCGEIVLNSE------FYAYDTKYIDD--QGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTAD 308
Cdd:PRK14573 669 ----GSSAYVIAGPHErrgsggFIDYQEKYGLSgkSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEE 744

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 490310162 309 NEVVINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALER 353
Cdd:PRK14573 745 GNFWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHK 789
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 3-352 2.19e-55

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 185.11  E-value: 2.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   3 KMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHINDAgnyllnaqdpARIALrPSTVTLAQIPGR 82
Cdd:PRK14572   1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVPTV----------YRPSI-PDESGNSEDLFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  83 EAQQLINAESGQPLAA---IDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPFI 159
Cdd:PRK14572  70 EEFQKANGVSEPADISqldADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 160 TLTR---ANRAQFSFADVEAkLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVL-- 234
Cdd:PRK14572 150 ELEKlkyLNSPRKTLLKLES-LGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLer 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 235 ---GNDHPQASTCGEIVLNSEFYAYDTKYiDDQGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDvFLTADNEV 311
Cdd:PRK14572 229 yrgGKRNPIALPATEIVPGGEFFDFESKY-KQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTD-FIIVDGEP 306

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 490310162 312 VINEINTLPGFTNISMYPKLWQASGLDYTSLITRLIELALE 352
Cdd:PRK14572 307 HILETNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK 347
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 4-350 1.64e-49

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 168.08  E-value: 1.64e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   4 MRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKqglwhindagNYLlnaqdparialrpstvtlaqipgRE 83
Cdd:PRK14571   1 MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDE----------DFL-----------------------KK 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  84 AQQLinaesgqplAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDaglavapfiTLTR 163
Cdd:PRK14571  48 VDQL---------KSFDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKG---------TVEI 109

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 164 ANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQGIKGREIECAVLG-NDHPQAS 242
Cdd:PRK14571 110 PDFVEIKEFMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVL 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 243 TCGEIVLNSEFYAYDTKYIDDQgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTaDNEVVINEINTLPGF 322
Cdd:PRK14571 190 PILELRPKRRFYDYVAKYTKGE-TEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGL 267

                        330       340
                 ....*....|....*....|....*...
gi 490310162 323 TNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:PRK14571 268 TELSDLPASAKAGGIEFEELVDIIIKSA 295
Dala_Dala_lig_N pfam01820
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ...
 5-130 6.64e-46

D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4 which is thought to be involved in substrate binding. 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). This domain is structurally related to the PreATP-grasp domain.


Pssm-ID: 460346 [Multi-domain]  Cd Length: 118  Bit Score: 152.76  E-value: 6.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162    5 RVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVLLGIDKQGLWHinDAGNYLLNAQDPARIALRpstvtlAQIPGREA 84
Cdd:pfam01820   1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLG--EAALRELASDDGLLLEVD------DAPDGGPA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 490310162   85 QQLINAESGQPLAAIDVIFPIVHGTLGEDGSLQGMLRMANLPFVGS 130
Cdd:pfam01820  73 GLLFGPNVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
 1-350 3.81e-35

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 130.57  E-value: 3.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162   1 MAKMRVGIVFGGKSAEHEVSLQSAKNIVEAIDKSRFDVVllGIDKQGlwhiNDAGNYLLNaqdpariaLRPstvtlaqip 80
Cdd:PRK14569   1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAV--GVDASG----KELVAKLLE--------LKP--------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  81 greaqqlinaesgqplaaiDVIFPIVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLA--VAPF 158
Cdd:PRK14569  58 -------------------DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPtpMAKF 118

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 159 ITLTRANRAQFSFadveaklglPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDhKVVVEQGIKGREIECAVLGNDh 238
Cdd:PRK14569 119 LTDKLVAEDEISF---------PVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDE- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 239 pqASTCGEIVLNSEFYAYDTKYiddQGAKVV-VPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEIN 317
Cdd:PRK14569 188 --VYSSVWIEPQNEFYDYESKY---SGKSIYhSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEIN 262

                        330       340       350
                 ....*....|....*....|....*....|...
gi 490310162 318 TLPGFTNISMYPKLWQASGLDYTSLITRLIELA 350
Cdd:PRK14569 263 SSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 124-351 9.00e-26

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: 104.18  E-value: 9.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 124 NLPFVGSDVlgSAACMDKDVTKRLLRDAGLAVAPFITLTRANRAqfsfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQ 203
Cdd:COG0439   40 GLPGPSPEA--IRAMRDKVLMREALAAAGVPVPGFALVDSPEEA----LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 204 YHQAVALA------FEFDHKVVVEQGIKGREIECAVLGNDhpqastcGEIVLNSEF-YAYDTKYIDDQGAkvVVPAAIAP 276
Cdd:COG0439  114 LEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVVVCSITrKHQKPPYFVELGH--EAPSPLPE 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490310162 277 EINDKIRAIAVQAYQTLG-CSGMARVDVFLTADNEVVINEINT-LPGftniSMYPKLWQ-ASGLDytsLITRLIELAL 351
Cdd:COG0439  185 ELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTElATGVD---LVREQIRLAL 255
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 91-356 3.45e-16

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: 78.06  E-value: 3.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  91 ESGQPLAAIDVIF----PIVHGTlgedgSLQGMLRMANLPFVgSDVLGSAACMDKDVTKRLLRDAGLAVAPFITLTRANR 166
Cdd:COG0189   49 YRGEDLSEFDAVLpridPPFYGL-----ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDD 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 167 AqfsfADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVALAFEFDHKVVVEQ----GIKGREIECAVLGndhpqas 242
Cdd:COG0189  123 L----RAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPVLVQefipEEDGRDIRVLVVG------- 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 243 tcGEIV-------LNSEFYAYDTkyiddQGAKVVvpaaiAPEINDKIRAIAVQAYQTLGCsGMARVDVFLTADNEVVInE 315
Cdd:COG0189  192 --GEPVaairripAEGEFRTNLA-----RGGRAE-----PVELTDEERELALRAAPALGL-DFAGVDLIEDDDGPLVL-E 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490310162 316 INTLPGFTNISmypklwQASGLDytslITRLIELALERHAA 356
Cdd:COG0189  258 VNVTPGFRGLE------RATGVD----IAEAIADYLEARAA 288
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 149-316 1.53e-14

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 70.75  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  149 RDAGLAVAPFITLTRANraqfSFADVEAKLGLPLFVKPANQGSS-VGVSKVKNEEQYHQAVALAFefDHKVVVEQGIKgR 227
Cdd:pfam02222   1 QKLGLPTPRFMAAESLE----ELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVP-F 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  228 EIECAVLGndhpqASTcgeivLNSEFYAYD---TKYIDDQGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCSGMARVDVF 304
Cdd:pfam02222  74 DRELSVLV-----VRS-----VDGETAFYPvveTIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELF 143

                         170
                  ....*....|..
gi 490310162  305 LTADNEVVINEI 316
Cdd:pfam02222 144 VTEDGDLLINEL 155
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 138-317 4.74e-14

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 72.22  E-value: 4.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 138 CMDKDVTKRLLRDAGLAVApfITLTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQyhqaVALAFEFDHK 217
Cdd:PRK12767 109 CNDKWLTYEFLKENGIPTP--KSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPN 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 218 VVVEQGIKGREIECAVLgNDhpqastcgeivLNSEFYAYDT-KYID------DQGakVVVPaaiAPEINDKIRAIAvqay 290
Cdd:PRK12767 183 LIIQEFIEGQEYTVDVL-CD-----------LNGEVISIVPrKRIEvragetSKG--VTVK---DPELFKLAERLA---- 241

                        170       180
                 ....*....|....*....|....*..
gi 490310162 291 QTLGCSGMARVDVFLTaDNEVVINEIN 317
Cdd:PRK12767 242 EALGARGPLNIQCFVT-DGEPYLFEIN 267
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 129-316 1.16e-11

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 65.10  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 129 GSDVLgsAACMDKDVTKRLLRDAGLAVAPFITLTranraqfSFADVEA---KLGLPLFVKPANQGSS-VGVSKVKNEEQY 204
Cdd:COG0026   80 GPEAL--EIAQDRLLEKAFLAELGIPVAPFAAVD-------SLEDLEAaiaELGLPAVLKTRRGGYDgKGQVVIKSAADL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 205 HQAVALAFEFDhkVVVEQGIK-GREIecAVLGndhpqA-STCGEIVlnsefyAYD---TKYIDDQGAKVVVPAAIAPEIN 279
Cdd:COG0026  151 EAAWAALGGGP--CILEEFVPfEREL--SVIV-----ArSPDGEVA------TYPvveNVHRNGILDESIAPARISEALA 215

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490310162 280 DKIRAIAVQAYQTLGCSG-MArVDVFLTADNEVVINEI 316
Cdd:COG0026  216 AEAEEIAKRIAEALDYVGvLA-VEFFVTKDGELLVNEI 252
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 127-316 7.12e-10

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 59.78  E-value: 7.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 127 FVGSDVLGSAAcmDKDVTKRLLRDAGLAVAPFITLTRANraqfSFADVEAKLGLPLFVKPANQGss-vGVSKVKNEEQYH 205
Cdd:PRK06019  89 PPGPDALAIAQ--DRLTEKQFLDKLGIPVAPFAVVDSAE----DLEAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 206 QAVAlafEFDHK-VVVEQGIKGREiECAVLGndhpqA-STCGEIVlnsefyAYD-TKYIDDQG--AKVVVPAAIAPEIND 280
Cdd:PRK06019 163 AAWA---LLGSVpCILEEFVPFER-EVSVIV-----ArGRDGEVV------FYPlVENVHRNGilRTSIAPARISAELQA 227

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490310162 281 KIRAIAVQAYQTLGCSG-MArVDVFLTADNEVVINEI 316
Cdd:PRK06019 228 QAEEIASRIAEELDYVGvLA-VEFFVTGDGELLVNEI 263
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 137-228 8.67e-09

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 57.09  E-value: 8.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 137 ACmDKDVTKRLLRDAGLAVAPFITLTRANRAqfsfadVEA--KLGLPLFVKP--ANQGSsvGVS-KVKNEEQYHQAVALA 211
Cdd:PRK14016 212 AC-DKELTKRLLAAAGVPVPEGRVVTSAEDA------WEAaeEIGYPVVVKPldGNHGR--GVTvNITTREEIEAAYAVA 282

                         90
                 ....*....|....*..
gi 490310162 212 FEFDHKVVVEQGIKGRE 228
Cdd:PRK14016 283 SKESSDVIVERYIPGKD 299
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
141-237 7.00e-07

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


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 51.08  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 141 KDVTKRLLRDAGLAVAPFITLTRANRAQFSFADVEAKlglPLFVKPANQGSSVGVS---KVKNEEQYHQAVALAFEFDHK 217
Cdd:PRK02471 489 KVVTKKILAEAGFPVPAGDEFTSLEEALADYSLFADK---AIVVKPKSTNFGLGISifkEPASLEDYEKALEIAFREDSS 565

                         90       100
                 ....*....|....*....|
gi 490310162 218 VVVEQGIKGREIECAVLGND 237
Cdd:PRK02471 566 VLVEEFIVGTEYRFFVLDGK 585
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
179-363 1.19e-06

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 49.51  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 179 GLPLFVKPANQGSSVGVSkVKNEEQYHQAVALAFE-FDHKVVVEQGI---KGREIECAVLGNdhpqastcgEIVLNSEFY 254
Cdd:PRK10446 135 GAPLVVKLVEGTQGIGVV-LAETRQAAESVIDAFRgLNAHILVQEYIkeaQGCDIRCLVVGD---------EVVAAIERR 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 255 AYDTKYIDD--QGAkvvvpAAIAPEINDKIRAIAVQAYQTLGCSgMARVDVfLTADNEVVINEINTLPGFTNISmypklw 332
Cdd:PRK10446 205 AKEGDFRSNlhRGG-----AASVASITPQEREIAIKAARTMALD-VAGVDI-LRANRGPLVMEVNASPGLEGIE------ 271

                        170       180       190
                 ....*....|....*....|....*....|..
gi 490310162 333 QASGLDYTSLITRLIelalERHAADR-ALKTS 363
Cdd:PRK10446 272 KTTGIDIAGKMIRWI----ERHATTEyCLKTG 299
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
 140-316 1.57e-05

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 46.59  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 140 DKDVTKRLLRDAGLAVAPFITLTRANRAQfsfaDVEAKLGLPLFVKP---ANQGSsvGVSKVKNEEQYHQAVALAFEFDH 216
Cdd:PLN02948 121 DKYAQKVHFSKHGIPLPEFMEIDDLESAE----KAGDLFGYPLMLKSrrlAYDGR--GNAVAKTEEDLSSAVAALGGFER 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 217 KVVVEQGIKGREiECAVL---GNDhpqastcGEIVLnseFYAYDTKYIDDQGAKVVVPAAIAPEINDKIRAIAVQAYQTL 293
Cdd:PLN02948 195 GLYAEKWAPFVK-ELAVMvarSRD-------GSTRC---YPVVETIHKDNICHVVEAPANVPWKVAKLATDVAEKAVGSL 263

                        170       180
                 ....*....|....*....|...
gi 490310162 294 GCSGMARVDVFLTADNEVVINEI 316
Cdd:PLN02948 264 EGAGVFGVELFLLKDGQILLNEV 286
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
92-318 2.69e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 45.89  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  92 SGQPLAAIDVIFPiVHGTLGEDGSLQGMLRMANLPFVGSDVLGSAACMDKDVTKRLLRDAGLAVAPfitltranRAQFSF 171
Cdd:PRK08462  70 SAAEIFEADAIFP-GYGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIP--------GSDGAL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 172 ADVEA------KLGLPLFVKPANQGSSVGVSKVKNEEQYHQAV------ALAFEFDHKVVVEQGI-KGREIECAVLGNDH 238
Cdd:PRK08462 141 KSYEEakkiakEIGYPVILKAAAGGGGRGMRVVEDESDLENLYlaaeseALSAFGDGTMYMEKFInNPRHIEVQILGDKH 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 239 PQASTCGEivLNSEFYAYDTKYIDDQGAKVvvpaaIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINT 318
Cdd:PRK08462 221 GNVIHVGE--RDCSLQRRHQKLIEESPAVV-----LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSNLDFYFMEMNT 293
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 136-347 3.60e-05

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: 45.03  E-value: 3.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  136 AACMDKDVTKRLLRDAGLAVApfITLTRANRAQFS-FADveaKLGLPLFVKPANQGSSVGVSKVkNEEQYHQAVALAFE- 213
Cdd:TIGR00768  84 LNAGDKFLSHQLLAKAGIPLP--RTGLAGSPEEALkLIE---EIGFPVVLKPVFGSWGRGVSLA-RDRQAAESLLEHFEq 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  214 ---FDHKVVVEQGIK---GREIECAVLGNdhpQASTCGEIVLNSEFYAYDTKyiddqGAKvvvpaAIAPEINDKIRAIAV 287
Cdd:TIGR00768 158 lngPQNLFLVQEYIKkpgGRDIRVFVVGD---EVVAAIYRITSGHWRSNLAR-----GGK-----AEPCSLTEEIEELAI 224

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  288 QAYQTLGcSGMARVDvFLTADNEVVINEINTLPGFTNISMYpklwqaSGLDYTSLITRLI 347
Cdd:TIGR00768 225 KAAKALG-LDVAGVD-LLESEDGLLVNEVNANPEFKNSVKT------TGVNIAGKLLDYI 276
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 97-318 1.47e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 43.48  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  97 AAIDVIFPiVHGTLGEDGSLQGMLRMANLPFVGSdvlgSAACM----DKDVTKRLLRDAGLAVAPFITltranraqFSFA 172
Cdd:PRK06111  73 TGAEAIHP-GYGLLSENASFAERCKEEGIVFIGP----SADIIakmgSKIEARRAMQAAGVPVVPGIT--------TNLE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 173 DVE------AKLGLPLFVKPANQGSSVGVSKVKNEEQYHQAVAL----AFEF--DHKVVVEQGI-KGREIECAVLGNDHP 239
Cdd:PRK06111 140 DAEeaiaiaRQIGYPVMLKASAGGGGIGMQLVETEQELTKAFESnkkrAANFfgNGEMYIEKYIeDPRHIEIQLLADTHG 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 240 QASTCGEivlnsefyaYDTKyIDDQGAKVVVPAAiAPEINDKIRA----IAVQAYQTLGCSGMARVDVFLTADNEVVINE 315
Cdd:PRK06111 220 NTVYLWE---------RECS-VQRRHQKVIEEAP-SPFLDEETRKamgeRAVQAAKAIGYTNAGTIEFLVDEQKNFYFLE 288


                 ...
gi 490310162 316 INT 318
Cdd:PRK06111 289 MNT 291
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
108-318 6.13e-04

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 41.62  E-value: 6.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 108 GTLGEDGSLQGMLRMANLPFVGSDvlgsAACMD----KDVTKRLLRDAGLAVAP-FITLTRANRAQFSFADveaKLGLPL 182
Cdd:PRK05586  83 GFLSENSKFAKMCKECNIVFIGPD----SETIElmgnKSNAREIMIKAGVPVVPgSEGEIENEEEALEIAK---EIGYPV 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 183 FVKPANQGSSVGVSKVKNEEQYHQAV------ALAFEFDHKVVVEQGI-KGREIECAVLGNDHPQASTCGEivLNSEFYA 255
Cdd:PRK05586 156 MVKASAGGGGRGIRIVRSEEELIKAFntakseAKAAFGDDSMYIEKFIeNPKHIEFQILGDNYGNVVHLGE--RDCSLQR 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490310162 256 YDTKYIDDQGAKVvvpaaIAPEINDKIRAIAVQAYQTLGCSGMARVDVFLTADNEVVINEINT 318
Cdd:PRK05586 234 RNQKVLEEAPSPV-----MTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNT 291
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 178-209 7.73e-04

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 39.57  E-value: 7.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 490310162  178 LGLPLFVKPANQGSSVGVSKVKNEEQYHQAVA 209
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFA 32
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 125-346 1.86e-03

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 40.22  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 125 LPfvGSDVLGSAACMDKDVTKRLLRDAGLAVAPfitlTRANRAQFSFADVEAKLGLPLFVKPANQGSSVGVSKVKNEEQY 204
Cdd:PRK02186  94 LP--AANTEAIRTCRDKKRLARTLRDHGIDVPR----THALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162 205 --HQAVALAfEFDHKVVVEQGIKGREIECAVLGNDHPQAstCGEIVlnSEFYAYDTKYIDdqgAKVVVPAAIAPEINDKI 282
Cdd:PRK02186 168 aaHCAALRR-AGTRAALVQAYVEGDEYSVETLTVARGHQ--VLGIT--RKHLGPPPHFVE---IGHDFPAPLSAPQRERI 239

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490310162 283 RAIAVQAYQTLGCS-GMARVDVFLTADNEVVInEINT-LPGftniSMYPKLW-QASGLDYTSLITRL 346
Cdd:PRK02186 240 VRTVLRALDAVGYAfGPAHTELRVRGDTVVII-EINPrLAG----GMIPVLLeEAFGVDLLDHVIDL 301
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 177-331 6.29e-03

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: 37.48  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310162  177 KLGLPLFVKPANQGSSVGVSKVKNEEQyhqAVALAFEFDHKVVVEQGIK---GREIECAVLGNDhpQASTCGEIVLNSEF 253
Cdd:pfam08443  38 KRQFPVIVKSIYGSQGIGVFLAEDEQK---LRQTLSATNEQILVQEFIAeanNEDIRCLVVGDQ--VVGALHRQSNEGDF 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490310162  254 YAYDTKyiddqGAkVVVPAAIAPEIndkiRAIAVQAYQTLGCSgMARVDVFLTADNEVVInEINTLPGFTNISMYPKL 331
Cdd:pfam08443 113 RSNLHR-----GG-VGEKYQLSQEE----TELAIKAAQAMQLD-VAGVDLLRQKRGLLVC-EVNSSPGLEGIEKTLGI 178
 
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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