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Conserved domains on  [gi|446335834|ref|WP_000413689|]
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D-alanine--D-alanine ligase [Escherichia coli]

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

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: 544.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSDASNYLLNADdpahIALRPSATSLAQVP 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADD----DNDKEDLSLLILPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  81 GKHEHqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFIT 160
Cdd:PRK01966  77 GGSEE-------------VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 161 LTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDnPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 241 ASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLD-GSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446335834 321 GFTNISMYPKLWQASGLGYTDLITRLIELALE 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: 544.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSDASNYLLNADdpahIALRPSATSLAQVP 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADD----DNDKEDLSLLILPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  81 GKHEHqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFIT 160
Cdd:PRK01966  77 GGSEE-------------VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 161 LTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDnPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 241 ASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLD-GSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446335834 321 GFTNISMYPKLWQASGLGYTDLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
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 1.18e-156

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: 442.49  E-value: 1.18e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834    5 RVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWhvsdasnyllNADDPAHIALRpsatslaqvpgkhe 84
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLILE-------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   85 hqlidaqNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTRa 164
Cdd:TIGR01205  57 -------LGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  165 NRNNISFAE---VESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDN--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  240 QASTCGEIVltsDFYAYDTKYIDEDgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIE---GFYDYEAKYLDGS-TEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284
                         330       340       350
                  ....*....|....*....|....*....|.
gi 446335834  320 PGFTNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
4-351 1.18e-155

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: 439.16  E-value: 1.18e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   4 LRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQgqwhvsdasnyllnaDDPAHIALRPsatslaqvpgkh 83
Cdd:COG1181    1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVE---------------DLPAALKELK------------ 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  84 ehqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTR 163
Cdd:COG1181   54 ---------------PDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 ANRNNIsfAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQAST 243
Cdd:COG1181  119 GELADL--EAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 244 CGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLPGFT 323
Cdd:COG1181  197 PIEIVPENGFYDYEAKYTD-GGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275
                        330       340
                 ....*....|....*....|....*...
gi 446335834 324 NISMYPKLWQASGLGYTDLITRLIELAL 351
Cdd:COG1181  276 PTSLLPKAAAAAGISYEELIERIIELAL 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 1.58e-109

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: 318.49  E-value: 1.58e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  147 LLRDAGLNIAPFITLTRANRNNI---SFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQG 223
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWKLNpkeWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  224 IKGREIECAVLGNDNPQASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDV 303
Cdd:pfam07478  81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYID-DSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446335834  304 FLTPENEVVINEINTLPGFTNISMYPKLWQASGLGYTDLITRLIE 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: 544.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSDASNYLLNADdpahIALRPSATSLAQVP 80
Cdd:PRK01966   1 MMKMRVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIGITKDGRWYLIDADNMELADD----DNDKEDLSLLILPS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  81 GKHEHqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFIT 160
Cdd:PRK01966  77 GGSEE-------------VDVVFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVV 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 161 LTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDnPQ 240
Cdd:PRK01966 144 LTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGND-PK 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 241 ASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLP 320
Cdd:PRK01966 223 ASVPGEIVKPDDFYDYEAKYLD-GSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMP 301
                        330       340       350
                 ....*....|....*....|....*....|..
gi 446335834 321 GFTNISMYPKLWQASGLGYTDLITRLIELALE 352
Cdd:PRK01966 302 GFTPISMYPKLWEASGLSYPELIDRLIELALE 333
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 1.18e-156

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: 442.49  E-value: 1.18e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834    5 RVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWhvsdasnyllNADDPAHIALRpsatslaqvpgkhe 84
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDKMGSW----------TYKDLPQLILE-------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   85 hqlidaqNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTRa 164
Cdd:TIGR01205  57 -------LGALLEGIDVVFPVLHGRYGEDGTIQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLTQ- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  165 NRNNISFAE---VESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDN--P 239
Cdd:TIGR01205 129 NRASADELEceqVAEPLGFPVIVKPAREGSSVGVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNEEalP 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  240 QASTCGEIVltsDFYAYDTKYIDEDgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTL 319
Cdd:TIGR01205 209 IIEIVPEIE---GFYDYEAKYLDGS-TEYVIPAPLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTI 284
                         330       340       350
                  ....*....|....*....|....*....|.
gi 446335834  320 PGFTNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:TIGR01205 285 PGMTAISLFPKAAAAAGIEFSQLVERILELA 315
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
4-351 1.18e-155

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: 439.16  E-value: 1.18e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   4 LRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQgqwhvsdasnyllnaDDPAHIALRPsatslaqvpgkh 83
Cdd:COG1181    1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVE---------------DLPAALKELK------------ 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  84 ehqlidaqngqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTR 163
Cdd:COG1181   54 ---------------PDVVFPALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRR 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 ANRNNIsfAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQAST 243
Cdd:COG1181  119 GELADL--EAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAALEEAFKYDDKVLVEEFIDGREVTVGVLGNGGPRALP 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 244 CGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINTLPGFT 323
Cdd:COG1181  197 PIEIVPENGFYDYEAKYTD-GGTEYICPARLPEELEERIQELALKAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMT 275
                        330       340
                 ....*....|....*....|....*...
gi 446335834 324 NISMYPKLWQASGLGYTDLITRLIELAL 351
Cdd:COG1181  276 PTSLLPKAAAAAGISYEELIERIIELAL 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 1.58e-109

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: 318.49  E-value: 1.58e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  147 LLRDAGLNIAPFITLTRANRNNI---SFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQG 223
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWKLNpkeWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  224 IKGREIECAVLGNDNPQASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDV 303
Cdd:pfam07478  81 IEGREIECAVLGNEDPEVSPVGEIVPSGGFYDYEAKYID-DSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446335834  304 FLTPENEVVINEINTLPGFTNISMYPKLWQASGLGYTDLITRLIE 348
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLIE 204
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
1-353 1.12e-106

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 315.13  E-value: 1.12e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVllGIDKqgqwhvsdasnyllnADDPAHI--ALRPsatslaq 78
Cdd:PRK01372   2 KMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAH--PIDP---------------GEDIAAQlkELGF------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  79 vpgkhehqlidaqngqplptvDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPF 158
Cdd:PRK01372  58 ---------------------DRVFNALHGRGGEDGTIQGLLELLGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPW 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 159 ITLTRANrnniSFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNdn 238
Cdd:PRK01372 117 IVLTREE----DLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKGRELTVAVLGG-- 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 239 pQASTCGEIVLTSDFYAYDTKYIDeDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINT 318
Cdd:PRK01372 191 -KALPVIEIVPAGEFYDYEAKYLA-GGTQYICPAGLPAEIEAELQELALKAYRALGCRGWGRVDFMLDEDGKPYLLEVNT 268
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 446335834 319 LPGFTNISMYPKLWQASGLGYTDLITRLIELALER 353
Cdd:PRK01372 269 QPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
8-355 2.46e-67

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 216.62  E-value: 2.46e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   8 IVFGGKSAEHEVSLQSAKNIVDAI-DKSRFDVVLLGIDK-QGQWHVSDAsnyllnADDPAHIALRPSATSLAQVPGKHEH 85
Cdd:PRK14570   7 LIFGGVSFEHEISLRSAYGIYSALlKLDKYNIYSVFIDKcTGIWYLLDS------VPDPPKLIKRDVLPIVSLIPGCGIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  86 QlidaqNGQPLpTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLTR-- 163
Cdd:PRK14570  81 V-----NNKNL-EIDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPFIGFRKyd 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 --ANRNNISfAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQA 241
Cdd:PRK14570 155 yfLDKEGIK-KDIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 242 STCGEIVLTS-DFYAYDTKYIDEDGAKVV--VPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPE-NEVVINEIN 317
Cdd:PRK14570 234 FTPGEIVVQDfIFYDYDAKYSTIPGNSIVfnIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNEIN 313
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 446335834 318 TLPGFTNISMYPKLWQASGLGYTDLITRLIELALERHA 355
Cdd:PRK14570 314 TIPGFTDISMFAKMCEHDGLQYKSLVDNLIDLAFQSYI 351
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
3-352 6.20e-56

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 186.26  E-value: 6.20e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   3 KLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHVSdaSNYLLNADDPAHIALRPSATSLAQVPGK 82
Cdd:PRK14572   1 MAKIAVFFGGSSTEHSISIRTGCFICATLHTMGHSVKPILLTPDGGWVVP--TVYRPSIPDESGNSEDLFLEEFQKANGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  83 HEHQLIDAQNgqplptVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITLT 162
Cdd:PRK14572  79 SEPADISQLD------ADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPFFELE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 163 RANRNNISFAEVES--KLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVL-----G 235
Cdd:PRK14572 153 KLKYLNSPRKTLLKleSLGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVLeryrgG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 236 NDNPQASTCGEIVLTSDFYAYDTKYiDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDvFLTPENEVVINE 315
Cdd:PRK14572 233 KRNPIALPATEIVPGGEFFDFESKY-KQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTD-FIIVDGEPHILE 310
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 446335834 316 INTLPGFTNISMYPKLWQASGLGYTDLITRLIELALE 352
Cdd:PRK14572 311 TNTLPGMTETSLIPQQAKAAGINMEEVFTDLIEIGLK 347
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
2-353 2.84e-54

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


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 190.80  E-value: 2.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   2 EKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWhvSDASNYLLNADDPAhialrpsatslaqvpG 81
Cdd:PRK14573 450 KKLSLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVSYFLINRQGLW--ETVSSLETAIEEDS---------------G 512
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  82 KHehqLIDAQNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPFITL 161
Cdd:PRK14573 513 KS---VLSSEIAQALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPVVPYQPL 589
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 162 TRA--NRN-NISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKG-REIECAVLGND 237
Cdd:PRK14573 590 TLAgwKREpELCLAHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVFVEESRLGsREIEVSCLGDG 669
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 238 N-------PQaSTCGEivltSDFYAYDTKY--IDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPE 308
Cdd:PRK14573 670 SsayviagPH-ERRGS----GGFIDYQEKYglSGKSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEE 744
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 446335834 309 NEVVINEINTLPGFTNISMYPKLWQASGLGYTDLITRLIELALER 353
Cdd:PRK14573 745 GNFWLSEMNPIPGMTEASPFLTAFVRKGWTYEQIVHQLIIDGLHK 789
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
4-350 1.38e-49

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 168.46  E-value: 1.38e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   4 LRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKqgqwhvsdasNYLLNADDpahialrpsatslaqvpgkh 83
Cdd:PRK14571   1 MRVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDE----------DFLKKVDQ-------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  84 ehqlidaqngqpLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAgLNIAPFITltr 163
Cdd:PRK14571  51 ------------LKSFDVVFNVLHGTFGEDGTLQAILDFLGIRYTGSDAFSSMICFDKLLTYRFLKGT-VEIPDFVE--- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 164 anrnnISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQGIKGREIECAVLG-NDNPQAS 242
Cdd:PRK14571 115 -----IKEFMKTSPLGYPCVVKPRREGSSIGVFICESDEEFQHALKEDLPRYGSVIVQEYIPGREMTVSILEtEKGFEVL 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 243 TCGEIVLTSDFYAYDTKYIDEDgAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTpENEVVINEINTLPGF 322
Cdd:PRK14571 190 PILELRPKRRFYDYVAKYTKGE-TEFILPAPLNPEEERLVKETALKAFVEAGCRGFGRVDGIFS-DGRFYFLEINTVPGL 267
                        330       340
                 ....*....|....*....|....*...
gi 446335834 323 TNISMYPKLWQASGLGYTDLITRLIELA 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 1.05e-44

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: 149.68  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834    5 RVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVLLGIDKQGQWHvsDASNYLLNADDPAHIALRPSAtslaqvPGKHE 84
Cdd:pfam01820   1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGITKDGRLG--EAALRELASDDGLLLEVDDAP------DGGPA 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446335834   85 HQLIDAQNGQPLPTVDVIFPIVHGTLGEDGSLQGMLRVANLPFVGS 130
Cdd:pfam01820  73 GLLFGPNVLELLIEVDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
1-350 8.30e-34

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 126.71  E-value: 8.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834   1 MEKLRVGIVFGGKSAEHEVSLQSAKNIVDAIDKSRFDVVllGIDKQGQWHVSDAsnyllnaddpahIALRPsatslaqvp 80
Cdd:PRK14569   1 MKNEKIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAV--GVDASGKELVAKL------------LELKP--------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  81 gkhehqlidaqngqplptvDVIFPIVHGTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLN--IAPF 158
Cdd:PRK14569  58 -------------------DKCFVALHGEDGENGRVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPtpMAKF 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 159 ITLTRANRNNISFaevesklglPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDhKVIVEQGIKGREIECAVLGNDn 238
Cdd:PRK14569 119 LTDKLVAEDEISF---------PVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG-EVMIEQWVTGKEITVAIVNDE- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 239 pqASTCGEIVLTSDFYAYDTKYideDGAKVV-VPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEIN 317
Cdd:PRK14569 188 --VYSSVWIEPQNEFYDYESKY---SGKSIYhSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIYDDRGNFYIMEIN 262
                        330       340       350
                 ....*....|....*....|....*....|...
gi 446335834 318 TLPGFTNISMYPKLWQASGLGYTDLITRLIELA 350
Cdd:PRK14569 263 SSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
124-351 3.77e-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: 105.34  E-value: 3.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 124 NLPFVGSDvlASAACMDKDVTKRLLRDAGLNIAPFITLTRANRNnISFAEvesKLGLPLFVKPANQGSSVGVSKVTSEEQ 203
Cdd:COG0439   40 GLPGPSPE--AIRAMRDKVLMREALAAAGVPVPGFALVDSPEEA-LAFAE---EIGYPVVVKPADGAGSRGVRVVRDEEE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 204 YAIAVDLA------FEFDHKVIVEQGIKGREIECAVLGNDnpqastcGEIVLTSDF-YAYDTKYIDEDGAkvVVPAAIAP 276
Cdd:COG0439  114 LEAALAEAraeakaGSPNGEVLVEEFLEGREYSVEGLVRD-------GEVVVCSITrKHQKPPYFVELGH--EAPSPLPE 184
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446335834 277 EINDKIRAIAVQAYQTLG-CAGMARVDVFLTPENEVVINEINT-LPGftniSMYPKLWQ-ASGLgytDLITRLIELAL 351
Cdd:COG0439  185 ELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINArLGG----EHIPPLTElATGV---DLVREQIRLAL 255
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
93-356 5.57e-15

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: 74.21  E-value: 5.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  93 GQPLPTVDVIF----PIVHGTlgedgslqGMLRVA---NLPFVgSDVLASAACMDKDVTKRLLRDAGLNIAPfitlTRAN 165
Cdd:COG0189   51 GEDLSEFDAVLpridPPFYGL--------ALLRQLeaaGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP----TLVT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 166 RNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQYAIAVDLAFEFDHKVIVEQ----GIKGREIECAVLGndnpqa 241
Cdd:COG0189  118 RDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELGSEPVLVQefipEEDGRDIRVLVVG------ 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 242 stcGEIVltsdfYAYDtKYIDEDGAKVVVPA---AIAPEINDKIRAIAVQAYQTLGcAGMARVDVFLTPENEVVInEINT 318
Cdd:COG0189  192 ---GEPV-----AAIR-RIPAEGEFRTNLARggrAEPVELTDEERELALRAAPALG-LDFAGVDLIEDDDGPLVL-EVNV 260
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 446335834 319 LPGFTNISmypklwQASGLgytDLITRLIElALERHAA 356
Cdd:COG0189  261 TPGFRGLE------RATGV---DIAEAIAD-YLEARAA 288
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
149-316 5.35e-13

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: 66.51  E-value: 5.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  149 RDAGLNIAPFITLTRANrnniSFAEVESKLGLPLFVKPANQGSS-VGVSKVTSEEQYAIAVDLAFefDHKVIVEQGIKgR 227
Cdd:pfam02222   1 QKLGLPTPRFMAAESLE----ELIEAGQELGYPCVVKARRGGYDgKGQYVVRSEADLPQAWEELG--DGPVIVEEFVP-F 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  228 EIECAVLGNDNPQASTcgeivltsdfYAYD---TKYIDEDGAKVVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVF 304
Cdd:pfam02222  74 DRELSVLVVRSVDGET----------AFYPvveTIQEDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELF 143
                         170
                  ....*....|..
gi 446335834  305 LTPENEVVINEI 316
Cdd:pfam02222 144 VTEDGDLLINEL 155
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
138-317 3.61e-12

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 66.45  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 138 CMDKDVTKRLLRDAGLNIApfITLTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQyaiaVDLAFEFDHK 217
Cdd:PRK12767 109 CNDKWLTYEFLKENGIPTP--KSYLPESLEDFKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPN 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 218 VIVEQGIKGREIECAVL--GNDNPQASTCGE-IVLTSDfyAYDTKYIDEDgakvvvpaaiaPEINDKIRAIAvqayQTLG 294
Cdd:PRK12767 183 LIIQEFIEGQEYTVDVLcdLNGEVISIVPRKrIEVRAG--ETSKGVTVKD-----------PELFKLAERLA----EALG 245
                        170       180
                 ....*....|....*....|...
gi 446335834 295 CAGMARVDVFLTpENEVVINEIN 317
Cdd:PRK12767 246 ARGPLNIQCFVT-DGEPYLFEIN 267
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
129-316 7.68e-10

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: 59.70  E-value: 7.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 129 GSDVLAsaACMDKDVTKRLLRDAGLNIAPFITLTranrnniSFAEVES---KLGLPLFVKPANQGSS-VGVSKVTSEEQY 204
Cdd:COG0026   80 GPEALE--IAQDRLLEKAFLAELGIPVAPFAAVD-------SLEDLEAaiaELGLPAVLKTRRGGYDgKGQVVIKSAADL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 205 AIAVDlafEFDHK-VIVEQGIK-GREIecAVLGNDNPQastcGEIVltsdfyAYD-TKYIDEDG--AKVVVPAAIAPEIN 279
Cdd:COG0026  151 EAAWA---ALGGGpCILEEFVPfEREL--SVIVARSPD----GEVA------TYPvVENVHRNGilDESIAPARISEALA 215
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446335834 280 DKIRAIAVQAYQTLGCAG-MArVDVFLTPENEVVINEI 316
Cdd:COG0026  216 AEAEEIAKRIAEALDYVGvLA-VEFFVTKDGELLVNEI 252
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
127-316 2.09e-09

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 58.24  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 127 FVGSDVLASAAcmDKDVTKRLLRDAGLNIAPFITLTRANrnniSFAEVESKLGLPLFVKPANQGss-vGVSKVTSEEQYA 205
Cdd:PRK06019  89 PPGPDALAIAQ--DRLTEKQFLDKLGIPVAPFAVVDSAE----DLEAALADLGLPAVLKTRRGGydgkGQWVIRSAEDLE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 206 IAVDlafEFDHK-VIVEQGIKGREiECAVLGNDNPQastcGEIVltsdfyAYD-TKYIDEDG--AKVVVPAAIAPEINDK 281
Cdd:PRK06019 163 AAWA---LLGSVpCILEEFVPFER-EVSVIVARGRD----GEVV------FYPlVENVHRNGilRTSIAPARISAELQAQ 228
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446335834 282 IRAIAVQAYQTLGCAG-MArVDVFLTPENEVVINEI 316
Cdd:PRK06019 229 AEEIASRIAEELDYVGvLA-VEFFVTGDGELLVNEI 263
PRK14016 PRK14016
cyanophycin synthetase; Provisional
137-228 2.94e-08

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 55.55  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 137 ACmDKDVTKRLLRDAGLNIApfitLTRANRNNISFAEVESKLGLPLFVKP--ANQGSsvGVS-KVTSEEQYAIAVDLAFE 213
Cdd:PRK14016 212 AC-DKELTKRLLAAAGVPVP----EGRVVTSAEDAWEAAEEIGYPVVVKPldGNHGR--GVTvNITTREEIEAAYAVASK 284
                         90
                 ....*....|....*
gi 446335834 214 FDHKVIVEQGIKGRE 228
Cdd:PRK14016 285 ESSDVIVERYIPGKD 299
PRK02471 PRK02471
bifunctional glutamate--cysteine ligase GshA/glutathione synthetase GshB;
131-237 5.64e-07

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


Pssm-ID: 179427 [Multi-domain]  Cd Length: 752  Bit Score: 51.47  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 131 DVLASAACMD-KDVTKRLLRDAGLNI---APFITLTRANRnniSFAEVESKlglPLFVKPANQGSSVGVS---KVTSEEQ 203
Cdd:PRK02471 478 DNYISPLIMEnKVVTKKILAEAGFPVpagDEFTSLEEALA---DYSLFADK---AIVVKPKSTNFGLGISifkEPASLED 551
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446335834 204 YAIAVDLAFEFDHKVIVEQGIKGREIECAVLGND 237
Cdd:PRK02471 552 YEKALEIAFREDSSVLVEEFIVGTEYRFFVLDGK 585
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
134-328 3.07e-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: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  134 ASAACMDKDVTKRLLRDAGLNIApfITLTRANRNN-ISFAEvesKLGLPLFVKPANQGSSVGVSKVTsEEQYAIAVDLAF 212
Cdd:TIGR00768  82 AILNAGDKFLSHQLLAKAGIPLP--RTGLAGSPEEaLKLIE---EIGFPVVLKPVFGSWGRGVSLAR-DRQAAESLLEHF 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834  213 E----FDHKVIVEQGIK---GREIECAVLGNDNPQA-STCGEivltSDFYAYDTKyidedGAKvvvpaAIAPEINDKIRA 284
Cdd:TIGR00768 156 EqlngPQNLFLVQEYIKkpgGRDIRVFVVGDEVVAAiYRITS----GHWRSNLAR-----GGK-----AEPCSLTEEIEE 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446335834  285 IAVQAYQTLGcAGMARVDvFLTPENEVVINEINTLPGFTNISMY 328
Cdd:TIGR00768 222 LAIKAAKALG-LDVAGVD-LLESEDGLLVNEVNANPEFKNSVKT 263
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
179-362 1.58e-04

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 42.97  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 179 GLPLFVKPANQGSSVGVskVTSE-EQYAIAVDLAFE-FDHKVIVEQGI---KGREIECAVLGNdnpqastcgEIVLTSDF 253
Cdd:PRK10446 135 GAPLVVKLVEGTQGIGV--VLAEtRQAAESVIDAFRgLNAHILVQEYIkeaQGCDIRCLVVGD---------EVVAAIER 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 254 YAYDTKY---IDEDGAKVVVpaaiapEINDKIRAIAVQAYQTLGCaGMARVDVFLTPENEVVInEINTLPGFTNISmypk 330
Cdd:PRK10446 204 RAKEGDFrsnLHRGGAASVA------SITPQEREIAIKAARTMAL-DVAGVDILRANRGPLVM-EVNASPGLEGIE---- 271
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446335834 331 lwQASGLgytDLITRLIELaLERHAADN-ALKT 362
Cdd:PRK10446 272 --KTTGI---DIAGKMIRW-IERHATTEyCLKT 298
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
268-316 6.13e-04

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 41.58  E-value: 6.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446335834 268 VVVPAAIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEI 316
Cdd:PLN02948 238 VEAPANVPWKVAKLATDVAEKAVGSLEGAGVFGVELFLLKDGQILLNEV 286
PRK02186 PRK02186
argininosuccinate lyase; Provisional
125-346 6.51e-04

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 41.76  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 125 LPfvGSDVLASAACMDKDVTKRLLRDAGLNIAPfitlTRANRNNISFAEVESKLGLPLFVKPANQGSSVGVSKVTSEEQY 204
Cdd:PRK02186  94 LP--AANTEAIRTCRDKKRLARTLRDHGIDVPR----THALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 205 -AIAVDLAFEFDHKVIVEQGIKGREIECAVLGNDNPQAStcgeIVLTSDFYAYDTKYIDedgAKVVVPAAIAPEINDKIR 283
Cdd:PRK02186 168 aAHCAALRRAGTRAALVQAYVEGDEYSVETLTVARGHQV----LGITRKHLGPPPHFVE---IGHDFPAPLSAPQRERIV 240
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446335834 284 AIAVQAYQTLGCA-GMARVDVFLTpENEVVINEINT-LPGftniSMYPKLW-QASGLGYTDLITRL 346
Cdd:PRK02186 241 RTVLRALDAVGYAfGPAHTELRVR-GDTVVIIEINPrLAG----GMIPVLLeEAFGVDLLDHVIDL 301
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
108-318 4.72e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 38.92  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 108 GTLGEDGSLQGMLRVANLPFVGSDVLASAACMDKDVTKRLLRDAGLNIAPfiTLTRANRNNISFAEVESKLGLPLFVKPA 187
Cdd:PRK05586  83 GFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVP--GSEGEIENEEEALEIAKEIGYPVMVKAS 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446335834 188 NQGSSVGVSKVTSEEQYAIAVD------LAFEFDHKVIVEQGI-KGREIECAVLGNDnpqastCGEIVLTSD----FYAY 256
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNtakseaKAAFGDDSMYIEKFIeNPKHIEFQILGDN------YGNVVHLGErdcsLQRR 234
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446335834 257 DTKYIDEDGAKVvvpaaIAPEINDKIRAIAVQAYQTLGCAGMARVDVFLTPENEVVINEINT 318
Cdd:PRK05586 235 NQKVLEEAPSPV-----MTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGNFYFMEMNT 291
 
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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