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Conserved domains on  [gi|2101331932|gb|UBM10579|]
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D-alanine--D-alanine ligase [Cupriavidus metallidurans]

Protein Classification

D-alanine--D-alanine ligase( domain architecture ID 11479603)

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

EC:  6.3.2.4
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 PRK01372
D-alanine--D-alanine ligase; Reviewed
 11-317 0e+00

D-alanine--D-alanine ligase; Reviewed


:

Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 523.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  11 PKSLGKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPGLQPISELAAAGFDRVFIALHGRYGEDGTMQGLLEQ 90
Cdd:PRK01372    1 PKMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGEDGTIQGLLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  91 LGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRA 170
Cdd:PRK01372   81 LGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 171 AFEKAAGLDADVIAETFIDGAELTCPIVGEgptaEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALA 250
Cdd:PRK01372  161 ALELAFKYDDEVLVEKYIKGRELTVAVLGG----KALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2101331932 251 VEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAATLD 317
Cdd:PRK01372  237 LKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
 
Name Accession Description Interval E-value
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 11-317 0e+00

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 523.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  11 PKSLGKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPGLQPISELAAAGFDRVFIALHGRYGEDGTMQGLLEQ 90
Cdd:PRK01372    1 PKMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGEDGTIQGLLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  91 LGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRA 170
Cdd:PRK01372   81 LGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 171 AFEKAAGLDADVIAETFIDGAELTCPIVGEgptaEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALA 250
Cdd:PRK01372  161 ALELAFKYDDEVLVEKYIKGRELTVAVLGG----KALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2101331932 251 VEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAATLD 317
Cdd:PRK01372  237 LKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 15-314 3.38e-156

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: 3.38e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  15 GKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPGLQPISE-LAAAGFDRVFIALHGRYGEDGTMQGLLEQLGI 93
Cdd:COG1181     1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDLPAaLKELKPDVVFPALHGRGGEDGTIQGLLELLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  94 PYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANT--DFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAA 171
Cdd:COG1181    81 PYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 172 FEKAAGLDADVIAETFIDGAELTCPIVGeGPTAEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAV 251
Cdd:COG1181   161 LEEAFKYDDKVLVEEFIDGREVTVGVLG-NGGPRALPPIEIVPENGFYDYEAKYTDGGTEYICPARLPEELEERIQELAL 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2101331932 252 EAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:COG1181   240 KAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELA 302
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 16-314 6.16e-129

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: 370.46  E-value: 6.16e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPG----------LQPISELAAA--GFDRVFIALHGRYGEDGT 83
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDkmgswtykdlPQLILELGALleGIDVVFPVLHGRYGEDGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  84 MQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAML---YANTDF---DAVVADLGLPLIVKPAREGSSI 157
Cdd:TIGR01205  81 IQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLtqnRASADElecEQVAEPLGFPVIVKPAREGSSV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 158 GLTKVIAADQMRAAFEKAAGLDADVIAETFIDGAELTCPIVGEGptaEALPVIKIVaPESN--YDYQNKYFTDDTQYLCP 235
Cdd:TIGR01205 161 GVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNE---EALPIIEIV-PEIEgfYDYEAKYLDGSTEYVIP 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2101331932 236 STLPDALEREVRALAVEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:TIGR01205 237 APLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 115-311 2.42e-69

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: 214.87  E-value: 2.42e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 115 LWMTHGLATPRFAMLYANTD-------FDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADVIAETF 187
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWklnpkewCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 188 IDGAELTCPIVGEGPtAEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADV 267
Cdd:pfam07478  81 IEGREIECAVLGNED-PEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2101331932 268 MLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVL 311
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLI 203
 
Name Accession Description Interval E-value
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 11-317 0e+00

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 523.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  11 PKSLGKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPGLQPISELAAAGFDRVFIALHGRYGEDGTMQGLLEQ 90
Cdd:PRK01372    1 PKMFGKVAVLMGGTSAEREVSLNSGAAVLAALREAGYDAHPIDPGEDIAAQLKELGFDRVFNALHGRGGEDGTIQGLLEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  91 LGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRA 170
Cdd:PRK01372   81 LGIPYTGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 171 AFEKAAGLDADVIAETFIDGAELTCPIVGEgptaEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALA 250
Cdd:PRK01372  161 ALELAFKYDDEVLVEKYIKGRELTVAVLGG----KALPVIEIVPAGEFYDYEAKYLAGGTQYICPAGLPAEIEAELQELA 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2101331932 251 VEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAATLD 317
Cdd:PRK01372  237 LKAYRALGCRGWGRVDFMLDEDGKPYLLEVNTQPGMTSHSLVPMAARAAGISFSELVDRILEDALCD 303
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 15-314 3.38e-156

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: 3.38e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  15 GKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPGLQPISE-LAAAGFDRVFIALHGRYGEDGTMQGLLEQLGI 93
Cdd:COG1181     1 MRVAVLFGGRSAEREVSLKSGRAVAAALDKAGYDVVPIGIDVEDLPAaLKELKPDVVFPALHGRGGEDGTIQGLLELLGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  94 PYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANT--DFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAA 171
Cdd:COG1181    81 PYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRRGElaDLEAIEEELGLPLFVKPAREGSSVGVSKVKNAEELAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 172 FEKAAGLDADVIAETFIDGAELTCPIVGeGPTAEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAV 251
Cdd:COG1181   161 LEEAFKYDDKVLVEEFIDGREVTVGVLG-NGGPRALPPIEIVPENGFYDYEAKYTDGGTEYICPARLPEELEERIQELAL 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2101331932 252 EAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:COG1181   240 KAFRALGCRGYARVDFRLDEDGEPYLLEVNTLPGMTPTSLLPKAAAAAGISYEELIERIIELA 302
D_ala_D_alaTIGR TIGR01205
D-alanine--D-alanine ligase; This model describes D-Ala--D-Ala ligase, an enzyme that makes a ...
 16-314 6.16e-129

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: 370.46  E-value: 6.16e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPG----------LQPISELAAA--GFDRVFIALHGRYGEDGT 83
Cdd:TIGR01205   1 RVAVLFGGKSAEHEISLVSAAAVLKALRDLGYDVYPVDIDkmgswtykdlPQLILELGALleGIDVVFPVLHGRYGEDGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  84 MQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAML---YANTDF---DAVVADLGLPLIVKPAREGSSI 157
Cdd:TIGR01205  81 IQGLLELMGIPYTGSGVLASALSMDKLLTKLLWKALGLPTPDYIVLtqnRASADElecEQVAEPLGFPVIVKPAREGSSV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 158 GLTKVIAADQMRAAFEKAAGLDADVIAETFIDGAELTCPIVGEGptaEALPVIKIVaPESN--YDYQNKYFTDDTQYLCP 235
Cdd:TIGR01205 161 GVSKVKSEEELQAALDEAFEYDEEVLVEQFIKGRELEVSILGNE---EALPIIEIV-PEIEgfYDYEAKYLDGSTEYVIP 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2101331932 236 STLPDALEREVRALAVEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:TIGR01205 237 APLDEELEEKIKELALKAYKALGCRGLARVDFFLDEEGEIYLNEINTIPGMTAISLFPKAAAAAGIEFSQLVERILELA 315
ddl PRK01966
D-alanine--D-alanine ligase;
16-307 5.06e-104

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 307.82  E-value: 5.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPF------------------------DPGLQPISELAA--AGFDR 69
Cdd:PRK01966    5 RVALLFGGRSAEHEVSLVSAKSVLKALDKEKYEVVPIgitkdgrwylidadnmeladddndKEDLSLLILPSGgsEEVDV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  70 VFIALHGRYGEDGTMQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAML----YANTDFDAVVADLGLP 145
Cdd:PRK01966   85 VFPVLHGPPGEDGTIQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVAPYVVLtrgdWEEASLAEIEAKLGLP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 146 LIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADVIAETFIDGAELTCPIVGEGPtaEALPVIKIVAPESNYDYQNKY 225
Cdd:PRK01966  165 VFVKPANLGSSVGISKVKNEEELAAALDLAFEYDRKVLVEQGIKGREIECAVLGNDP--KASVPGEIVKPDDFYDYEAKY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 226 FTDDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYED 305
Cdd:PRK01966  243 LDGSAELIIPADLSEELTEKIRELAIKAFKALGCSGLARVDFFLTEDGEIYLNEINTMPGFTPISMYPKLWEASGLSYPE 322


                  ..
gi 2101331932 306 FV 307
Cdd:PRK01966  323 LI 324
PRK14571 PRK14571
D-alanyl-alanine synthetase A; Provisional
 16-318 3.42e-70

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 184751 [Multi-domain]  Cd Length: 299  Bit Score: 220.46  E-value: 3.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDPG---LQPISELAAagFDRVFIALHGRYGEDGTMQGLLEQLG 92
Cdd:PRK14571    2 RVALLMGGVSREREISLRSGERVKKALEKLGYEVTVFDVDedfLKKVDQLKS--FDVVFNVLHGTFGEDGTLQAILDFLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  93 IPYTGSGVLASALAMDKQATKRLwMTHGLATPRFAMLYANTDfdavVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAF 172
Cdd:PRK14571   80 IRYTGSDAFSSMICFDKLLTYRF-LKGTVEIPDFVEIKEFMK----TSPLGYPCVVKPRREGSSIGVFICESDEEFQHAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 173 EKAAGLDADVIAETFIDGAELTCPIVGEGPTAEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAVE 252
Cdd:PRK14571  155 KEDLPRYGSVIVQEYIPGREMTVSILETEKGFEVLPILELRPKRRFYDYVAKYTKGETEFILPAPLNPEEERLVKETALK 234

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2101331932 253 AFRVLGCRGWARADVMLtRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAATLDL 318
Cdd:PRK14571  235 AFVEAGCRGFGRVDGIF-SDGRFYFLEINTVPGLTELSDLPASAKAGGIEFEELVDIIIKSAFLKG 299
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
 115-311 2.42e-69

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: 214.87  E-value: 2.42e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 115 LWMTHGLATPRFAMLYANTD-------FDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADVIAETF 187
Cdd:pfam07478   1 LLKAAGLPVVPFVTFTRADWklnpkewCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEKVLVEEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 188 IDGAELTCPIVGEGPtAEALPVIKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADV 267
Cdd:pfam07478  81 IEGREIECAVLGNED-PEVSPVGEIVPSGGFYDYEAKYIDDSAQIVVPADLEEEQEEQIQELALKAYKALGCRGLARVDF 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2101331932 268 MLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVL 311
Cdd:pfam07478 160 FLTEDGEIVLNEVNTIPGFTSISMFPKLAAAAGVSFPDLVDQLI 203
PRK14569 PRK14569
D-alanyl-alanine synthetase A; Provisional
 16-314 1.37e-59

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173033 [Multi-domain]  Cd Length: 296  Bit Score: 192.97  E-value: 1.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFDP-GLQPISELAAAGFDRVFIALHGRYGEDGTMQGLLEQLGIP 94
Cdd:PRK14569    5 KIVVLYGGDSPEREVSLKSGKAVLDSLISQGYDAVGVDAsGKELVAKLLELKPDKCFVALHGEDGENGRVSALLEMLEIK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  95 YTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLyanTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEK 174
Cdd:PRK14569   85 HTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFL---TDKLVAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 175 AAGLdADVIAETFIDGAELTCPIVGEgptaEALPVIKIVAPESNYDYQNKYfTDDTQYLCPSTLPDALEREVRALAVEAF 254
Cdd:PRK14569  162 ASKY-GEVMIEQWVTGKEITVAIVND----EVYSSVWIEPQNEFYDYESKY-SGKSIYHSPSGLCEQKELEVRQLAKKAY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 255 RVLGCRGWARADVMLTRDGKPYLLEMNTSPGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:PRK14569  236 DLLGCSGHARVDFIYDDRGNFYIMEINSSPGMTDNSLSPKSAAAEGVDFDSFVKRIIEQA 295
PRK14572 PRK14572
D-alanyl-alanine synthetase A; Provisional
 16-305 7.64e-57

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173036 [Multi-domain]  Cd Length: 347  Bit Score: 187.42  E-value: 7.64e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVD--------------------AHPFDPGLQPI---------------S 60
Cdd:PRK14572    3 KIAVFFGGSSTEHSISIRTGCFICATLHTMGHSvkpilltpdggwvvptvyrpSIPDESGNSEDlfleefqkangvsepA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  61 ELAAAGFDRVFIALHGRYGEDGTMQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGL-ATPRFAM--LYANTDFDA 137
Cdd:PRK14572   83 DISQLDADIAFLGLHGGAGEDGRIQGFLDTLGIPYTGSGVLASALAMDKTRANQIFLQSGQkVAPFFELekLKYLNSPRK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 138 VVADL---GLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADVIAETFIDGAELTCPIVgEGPTAE-----ALPV 209
Cdd:PRK14572  163 TLLKLeslGFPQFLKPVEGGSSVSTYKITNAEQLMTLLALIFESDSKVMSQSFLSGTEVSCGVL-ERYRGGkrnpiALPA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 210 IKIVAPESNYDYQNKYFTDDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADVMLTrDGKPYLLEMNTSPGMTGH 289
Cdd:PRK14572  242 TEIVPGGEFFDFESKYKQGGSEEITPARISDQEMKRVQELAIRAHESLGCKGYSRTDFIIV-DGEPHILETNTLPGMTET 320

                         330
                  ....*....|....*.
gi 2101331932 290 SLVPMAARANGISYED 305
Cdd:PRK14572  321 SLIPQQAKAAGINMEE 336
PRK14573 PRK14573
bifunctional UDP-N-acetylmuramate--L-alanine ligase/D-alanine--D-alanine ligase;
10-314 4.55e-34

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


Pssm-ID: 184752 [Multi-domain]  Cd Length: 809  Bit Score: 132.25  E-value: 4.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  10 DPKSLgKVGVLLGGKSAEREISLLSGNGVLAALKSRGVDA---------------------------HPFDPglqPISEl 62
Cdd:PRK14573  448 EPKKL-SLGLVCGGKSCEHDISLLSAKNIAKYLSPEFYDVsyflinrqglwetvssletaieedsgkSVLSS---EIAQ- 522

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  63 AAAGFDRVFIALHGRYGEDGTMQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGLA--------------TPRFAM 128
Cdd:PRK14573  523 ALAKVDVVLPILHGPFGEDGTMQGFLEIIGKPYTGPSLAFSAIAMDKVLTKRFASDVGVPvvpyqpltlagwkrEPELCL 602

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 129 lyantdfDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADV-IAETFIDGAELTCPIVGEGPTAEAL 207
Cdd:PRK14573  603 -------AHIVEAFSFPMFVKTAHLGSSIGVFEVHNVEELRDKISEAFLYDTDVfVEESRLGSREIEVSCLGDGSSAYVI 675

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 208 PVIKIVAPESNY-DYQNKY-FT--DDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADVMLTRDGKPYLLEMNTS 283
Cdd:PRK14573  676 AGPHERRGSGGFiDYQEKYgLSgkSSAQIVFDLDLSKESQEQVLELAERIYRLLQGKGSCRIDFFLDEEGNFWLSEMNPI 755

                         330       340       350
                  ....*....|....*....|....*....|.
gi 2101331932 284 PGMTGHSLVPMAARANGISYEDFVMQVLAAA 314
Cdd:PRK14573  756 PGMTEASPFLTAFVRKGWTYEQIVHQLIIDG 786
PRK14570 PRK14570
D-alanyl-alanine synthetase A; Provisional
 19-314 9.98e-33

D-alanyl-alanine synthetase A; Provisional


Pssm-ID: 173034 [Multi-domain]  Cd Length: 364  Bit Score: 124.56  E-value: 9.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  19 VLLGGKSAEREISLLSGNGVLAAL--------------KSRGV----DAHPFDPGLQPISELAAAGF------------- 67
Cdd:PRK14570    7 LIFGGVSFEHEISLRSAYGIYSALlkldkyniysvfidKCTGIwyllDSVPDPPKLIKRDVLPIVSLipgcgifvnnknl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  68 --DRVFIALHGRYGEDGTMQGLLEQLGIPYTGSGVLASALAMDKQATKRLWMTHGLATPRFaMLYANTDF--------DA 137
Cdd:PRK14570   87 eiDVVFPIVHGRTGEDGAIQGFLKVMDIPCVGAGILGSAISINKYFCKLLLKSFNIPLVPF-IGFRKYDYfldkegikKD 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 138 VVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGLDADVIAETFIDGAELTCPIVGEGPTAEALPVIKIVAPES 217
Cdd:PRK14570  166 IKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKYDLTVVIEKFIEAREIECSVIGNEQIKIFTPGEIVVQDFI 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 218 NYDYQNKYFT---DDTQYLCPSTLPDALEREVRALAVEAFRVLGCRGWARADVMLTRD-GKPYLLEMNTSPGMTGHSLVP 293
Cdd:PRK14570  246 FYDYDAKYSTipgNSIVFNIPAHLDTKHLLDIKEYAFLTYKNLELRGMARIDFLIEKDtGLIYLNEINTIPGFTDISMFA 325

                         330       340
                  ....*....|....*....|.
gi 2101331932 294 MAARANGISYEDFVMQVLAAA 314
Cdd:PRK14570  326 KMCEHDGLQYKSLVDNLIDLA 346
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 87-312 6.97e-32

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: 119.59  E-value: 6.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  87 LLEQLGIPYTGsgvLASALAM-DKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAA 165
Cdd:COG0439    35 LAEELGLPGPS---PEAIRAMrDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 166 DQMRAAFEKAAG------LDADVIAETFIDGAELTC-PIVGEGptaealpVIKIVAPeSNYDYQNKYFTdDTQYLCPSTL 238
Cdd:COG0439   112 EELEAALAEARAeakagsPNGEVLVEEFLEGREYSVeGLVRDG-------EVVVCSI-TRKHQKPPYFV-ELGHEAPSPL 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2101331932 239 PDALEREVRALAVEAFRVLG-CRGWARADVMLTRDGKPYLLEMNTSPGmtGHSLVPMAARANGISYEDFVMQVLA 312
Cdd:COG0439   183 PEELRAEIGELVARALRALGyRRGAFHTEFLLTPDGEPYLIEINARLG--GEHIPPLTELATGVDLVREQIRLAL 255
Dala_Dala_lig_N pfam01820
D-ala D-ala ligase N-terminus; This family represents the N-terminal region of the ...
 16-98 5.19e-28

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: 104.99  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  16 KVGVLLGGKSAEREISLLSGNGVLAALKSRGVDAHPFD-------------------------------------PGLQP 58
Cdd:pfam01820   1 KVAVLFGGRSSEHEVSLVSARSVLKALDKEKYEVIPIGitkdgrlgeaalrelasddglllevddapdggpagllFGPNV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2101331932  59 ISELAAagFDRVFIALHGRYGEDGTMQGLLEQLGIPYTGS 98
Cdd:pfam01820  81 LELLIE--VDVVFPVLHGPNGEDGTLQGLLELAGIPYVGS 118
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 38-285 7.75e-14

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: 70.74  E-value: 7.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  38 VLAALKSRGVDAHPFDP---------GLQPISELAAAGFDRVFIalhgRYGEDGTMQGLLEQLgipyTGSGVL------A 102
Cdd:COG0189    19 LIEAAQRRGHEVEVIDPddltldlgrAPELYRGEDLSEFDAVLP----RIDPPFYGLALLRQL----EAAGVPvvndpeA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 103 SALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAGL-DAD 181
Cdd:COG0189    91 IRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESILEALTELgSEP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 182 VIAETFI---DGAELTCPIVGEgptaEALPVIKIVAPE----SNYDYQNKYftddtqylCPSTLPDalerEVRALAVEAF 254
Cdd:COG0189   171 VLVQEFIpeeDGRDIRVLVVGG----EPVAAIRRIPAEgefrTNLARGGRA--------EPVELTD----EERELALRAA 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2101331932 255 RVLGCrGWARADVMLTRDGkPYLLEMNTSPG 285
Cdd:COG0189   235 PALGL-DFAGVDLIEDDDG-PLVLEVNVTPG 263
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 97-281 1.41e-10

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 61.44  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  97 GSGVLAS-----ALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAV--VADLGLPLIVKPAREGSSIGLTKVIAADQMR 169
Cdd:PRK12767   95 GVKVLVSskeviEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 170 AAFEKAagldADVIAETFIDGAELTCPIV--GEGPTAEALPVIKIVAPESNYDyqnKYFTDDTQylcpstlpdalerEVR 247
Cdd:PRK12767  175 FLLEYV----PNLIIQEFIEGQEYTVDVLcdLNGEVISIVPRKRIEVRAGETS---KGVTVKDP-------------ELF 234

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2101331932 248 ALAVEAFRVLGCRGWARADVMLTrDGKPYLLEMN 281
Cdd:PRK12767  235 KLAERLAEALGARGPLNIQCFVT-DGEPYLFEIN 267
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
93-192 4.26e-09

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


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 57.25  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  93 IPYTGSGVLASAlaMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAR-----EGSSIGLTKVIAAD- 166
Cdd:COG3919   104 LPYPDADLLDRL--LDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPADsvgydELSFPGKKKVFYVDd 181

                          90       100
                  ....*....|....*....|....*...
gi 2101331932 167 --QMRAAFEKAAGLDADVIAETFIDGAE 192
Cdd:COG3919   182 reELLALLRRIAAAGYELIVQEYIPGDD 209
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 106-288 2.09e-07

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 49.69  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 106 AMDKQATKRLWMTHGLATPRfamlyanTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEkaagldaDVIAE 185
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPE-------TLQAEELLREEKKYVVKPRDGCGGEGVRKVENGREDEAFIE-------NVLVQ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 186 TFIDGAELTCPIVGEGPTAEALPVIKIVApeSNYDYQNKYFTDDTQYlcpstlPDALEREVRALAVEAFRVL-GCRGWAR 264
Cdd:pfam02655  67 EFIEGEPLSVSLLSDGEKALPLSVNRQYI--DNGGSGFVYAGNVTPS------RTELKEEIIELAEEVVECLpGLRGYVG 138

                         170       180
                  ....*....|....*....|....
gi 2101331932 265 ADVMLTrDGKPYLLEMNtsPGMTG 288
Cdd:pfam02655 139 VDLVLK-DNEPYVIEVN--PRITT 159
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 98-192 6.77e-07

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 50.93  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  98 SGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKP-----AReGSSIGLTKviaADQMRAAF 172
Cdd:PRK14016  204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPldgnhGR-GVTVNITT---REEIEAAY 279

                          90       100
                  ....*....|....*....|
gi 2101331932 173 EKAAGLDADVIAETFIDGAE 192
Cdd:PRK14016  280 AVASKESSDVIVERYIPGKD 299
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
 119-289 7.26e-07

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: 48.40  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 119 HGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVI-AADQMRAAFEKAAglDADVIAETFID-GAELTCP 196
Cdd:pfam02222   3 LGLPTPRFMAAESLEELIEAGQELGYPCVVKARRGGYDGKGQYVVrSEADLPQAWEELG--DGPVIVEEFVPfDRELSVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 197 IV--GEGPTAeALPVIKIVapESNYDYQNKYftddtqylCPSTLPDALEREVRALAVEAFRVLGCRGWARADVMLTRDGK 274
Cdd:pfam02222  81 VVrsVDGETA-FYPVVETI--QEDGICRLSV--------APARVPQAIQAEAQDIAKRLVDELGGVGVFGVELFVTEDGD 149

                         170
                  ....*....|....*
gi 2101331932 275 PYLLEMNTSPGMTGH 289
Cdd:pfam02222 150 LLINELAPRPHNSGH 164
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
102-189 1.25e-06

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 49.75  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 102 ASALAMDKQATKRLWM-THGLATPRFAmlYANT--DFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAA-- 176
Cdd:PRK09288  107 ATRLTMNREGIRRLAAeELGLPTSPYR--FADSleELRAAVEEIGYPCVVKPVMSSSGKGQSVVRSPEDIEKAWEYAQeg 184

                          90
                  ....*....|....*
gi 2101331932 177 --GLDADVIAETFID 189
Cdd:PRK09288  185 grGGAGRVIVEEFID 199
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 91-320 3.76e-06

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 48.69  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  91 LGIPytGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGSSIGLTKVIAADQMRA 170
Cdd:PRK02186   92 LGLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 171 AFEKAAGLDA-DVIAETFIDGAELTCPIVGEGPTAEALPVI-KIVAP-----ESNYDYqnkyftddtqylcPSTLPDALE 243
Cdd:PRK02186  170 HCAALRRAGTrAALVQAYVEGDEYSVETLTVARGHQVLGITrKHLGPpphfvEIGHDF-------------PAPLSAPQR 236

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2101331932 244 REVRALAVEAFRVLGCR-GWARADVMLtRDGKPYLLEMNtsPGMTGHSLVPMAARANGISYEDFVMQVLAAATLDLHP 320
Cdd:PRK02186  237 ERIVRTVLRALDAVGYAfGPAHTELRV-RGDTVVIIEIN--PRLAGGMIPVLLEEAFGVDLLDHVIDLHLGVAAFADP 311
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 102-189 2.31e-05

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: 45.45  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 102 ASALAM--DKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGss-iGLTKVIAADQMRAAFEKAAGl 178
Cdd:COG0026    81 PEALEIaqDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTRRGGydgkGQVVIKSAADLEAAWAALGG- 159

                          90
                  ....*....|.
gi 2101331932 179 dADVIAETFID 189
Cdd:COG0026   160 -GPCILEEFVP 169
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 104-189 6.19e-05

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 44.37  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 104 ALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGLPLIVKPAREGssiglTKVIA-ADQMRAAFEKAAGldADV 182
Cdd:PRK06019   96 AIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLKTRRGGydgkgQWVIRsAEDLEAAWALLGS--VPC 173


                  ....*..
gi 2101331932 183 IAETFID 189
Cdd:PRK06019  174 ILEEFVP 180
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
 106-288 1.86e-04

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: 41.72  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 106 AMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLGL--PLIVKPARegSSIGLtKVIAADQMRAAFEKAAGLDADVI 183
Cdd:pfam08443   1 ARDKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIKRqfPVIVKSIY--GSQGI-GVFLAEDEQKLRQTLSATNEQIL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 184 AETFID---GAELTCPIVGEgptaEALPVIKIVAPESNYDyqnkyftdDTQYLCPSTLPDALEREVRALAVEAFRVLGCR 260
Cdd:pfam08443  78 VQEFIAeanNEDIRCLVVGD----QVVGALHRQSNEGDFR--------SNLHRGGVGEKYQLSQEETELAIKAAQAMQLD 145

                         170       180
                  ....*....|....*....|....*...
gi 2101331932 261 gWARADVMLTRDGkPYLLEMNTSPGMTG 288
Cdd:pfam08443 146 -VAGVDLLRQKRG-LLVCEVNSSPGLEG 171
PRK07206 PRK07206
hypothetical protein; Provisional
 142-313 2.25e-03

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 39.63  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 142 LGLPLIVKPAREGSSIGLTKVIAADQMRAAFEKAAG-------LDADVIAETFIDGAELTCPIV---GEGPTAEALPVIK 211
Cdd:PRK07206  145 IDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAILGkanklglVNETVLVQEYLIGTEYVVNFVsldGNHLVTEIVRYHK 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 212 IVAPESN--YDYqnkyftDDtqylcpstLPDALEREVRALAVEAFRVLGC----RGWARADVMLTRDGkPYLLEMNTSPG 285
Cdd:PRK07206  225 TSLNSGStvYDY------DE--------FLDYSEPEYQELVDYTKQALDAlgikNGPAHAEVMLTADG-PRLIEIGARLD 289

                         170       180
                  ....*....|....*....|....*....
gi 2101331932 286 MTGHslvPMAAR-ANGISYEDFVMQVLAA 313
Cdd:PRK07206  290 GGLH---PDVARlATGDSQLDATVESLAD 315
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
88-288 2.86e-03

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


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 38.73  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932  88 LEQLGiPYTGSGVLASALAMDKQATKRLWMTHGLATPRFAMLYANTDFDAVVADLG-LPLIVKPAREGSSIGltkVIAAD 166
Cdd:PRK10446   80 FEMLG-SYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGgAPLVVKLVEGTQGIG---VVLAE 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 167 QMRAA---FEKAAGLDADVIAETFID---GAELTCPIVGEgptaEALPVIKIVAPESNydyqnkyFTDDTQYLCPSTLPD 240
Cdd:PRK10446  156 TRQAAesvIDAFRGLNAHILVQEYIKeaqGCDIRCLVVGD----EVVAAIERRAKEGD-------FRSNLHRGGAASVAS 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2101331932 241 ALEREvRALAVEAFRVLGCrGWARADVMLTRDGkPYLLEMNTSPGMTG 288
Cdd:PRK10446  225 ITPQE-REIAIKAARTMAL-DVAGVDILRANRG-PLVMEVNASPGLEG 269
ATPgrasp_ST pfam14397
Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved ...
 108-293 4.63e-03

Sugar-transfer associated ATP-grasp; A member of the ATP-grasp fold predicted to be involved in the biosynthesis of cell surface polysaccharides.


Pssm-ID: 405145 [Multi-domain]  Cd Length: 278  Bit Score: 38.09  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 108 DKQATKRLWMTHGLATPR-FAMLYAN---TDFDAVVADLGLPLIVKPAREGSSIGLtkVIAADQMRAAFEKA-------- 175
Cdd:pfam14397  21 DKLKFKQLALRAGLPVPKlYGVISIGhdiSRLDAFVRSLPPGFVIKPAKGSGGKGI--LVITRRGDQDYFKSsgcrilld 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 176 ---------AGLDADVIAETFIdgaeLTCPIVgEGPTAEALPVIKIVA------------------PESNYD-------- 220
Cdd:pfam14397  99 elkrhvsslGGKPDVALVEERI----VQDPVF-AKLSPESVNTIRVITflldngvpvmpamlrlgtGASLVDnlhqggvg 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101331932 221 --------YQNKYFTDDTQYLCPSTL-PDALER----------EVRALAVEAFRVLGCRGWARADVMLTRDGKPYLLEMN 281
Cdd:pfam14397 174 vgidlatgVLFKPALQAVQYGEPIEHhPDTGVKfrgfqipnwdQILELAAECAQTLPGLGYVGWDIVIDENGGPLLLELN 253

                         250
                  ....*....|....*...
gi 2101331932 282 TSPGMT------GHSLVP 293
Cdd:pfam14397 254 ARPGLGifqianGEGLLP 271
 
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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