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Conserved domains on  [gi|5542452]
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Chain A, CARBONIC ANHYDRASE

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_anhyd super family cl48897
carbonic anhydrase;
1-213 2.78e-152

carbonic anhydrase;


The actual alignment was detected with superfamily member NF040597:

Pssm-ID: 468571  Cd Length: 248  Bit Score: 422.33  E-value: 2.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452     1 QEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVL 80
Cdd:NF040597  36 QEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDVTIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    81 HALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVT 160
Cdd:NF040597 116 HALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGPAYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVT 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5542452   161 IPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS 213
Cdd:NF040597 196 IPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVNLAEGYNAAS 248
 
Name Accession Description Interval E-value
carb_anhyd NF040597
carbonic anhydrase;
1-213 2.78e-152

carbonic anhydrase;


Pssm-ID: 468571  Cd Length: 248  Bit Score: 422.33  E-value: 2.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452     1 QEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVL 80
Cdd:NF040597  36 QEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDVTIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    81 HALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVT 160
Cdd:NF040597 116 HALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGPAYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVT 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5542452   161 IPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS 213
Cdd:NF040597 196 IPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVNLAEGYNAAS 248
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 24-211 2.25e-81

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 239.83  E-value: 2.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   24 SAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETineegepiednivevdgk 103
Cdd:cd00710   1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  104 eYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLP 183
Cdd:cd00710  63 -YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALP 141

                       170       180
                ....*....|....*....|....*...
gi 5542452  184 EVTDDyaYSHTNEAVVYVNVHLAEGYKE 211
Cdd:cd00710 142 DVTDS--AREFNEKVITVNNELAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 25-212 1.02e-48

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 156.73  E-value: 1.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALEtineegepiednivevdgkE 104
Cdd:COG0663  10 TPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDP-------------------G 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLeprsaAIGVTIPDGRYIPAGMVVTsQAEADKLP 183
Cdd:COG0663  70 YPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSPAKVVR 142

                       170       180
                ....*....|....*....|....*....
gi 5542452  184 EVTDDYAYSHTNEAVVYVNvhLAEGYKET 212
Cdd:COG0663 143 ELTEEEIAFLRESAENYVE--LARRYLAE 169
PLN02296 PLN02296
carbonate dehydratase
 25-210 5.63e-16

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 74.39  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETineegepiednivEVDGKE 104
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFKSKVgnncVLEPRSAAIGVTIPDGRYIPAGMvVTSQAEADKLPE 184
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLLDGVV----VEKHAMVAAGALVRQNTRIPSGE-VWAGNPAKFLRK 191

                        170       180
                 ....*....|....*....|....*....
gi 5542452   185 VTDDYAYSHTNEAVVYVN---VHLAEGYK 210
Cdd:PLN02296 192 LTEEEIAFISQSATNYSNlaqVHAAENAK 220
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 109-165 4.66e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.42  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    109 IGNNVSL----------AHQSQVH-GPAAVGDDTFIGMQAFVFK-SKVGNNCVLEPRSA-AIGVTIPDGR 165
Cdd:TIGR02353 134 IGAGTIVrkevmllgyrAERGRLHtGPVTLGRDAFIGTRSTLDIdTSIGDGAQLGHGSAlQGGQSIPDGE 203
 
Name Accession Description Interval E-value
carb_anhyd NF040597
carbonic anhydrase;
1-213 2.78e-152

carbonic anhydrase;


Pssm-ID: 468571  Cd Length: 248  Bit Score: 422.33  E-value: 2.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452     1 QEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVL 80
Cdd:NF040597  36 QEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDVTIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    81 HALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVT 160
Cdd:NF040597 116 HALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGPAYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVT 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 5542452   161 IPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS 213
Cdd:NF040597 196 IPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVNLAEGYNAAS 248
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 24-211 2.25e-81

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 239.83  E-value: 2.25e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   24 SAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETineegepiednivevdgk 103
Cdd:cd00710   1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  104 eYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLP 183
Cdd:cd00710  63 -YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALP 141

                       170       180
                ....*....|....*....|....*...
gi 5542452  184 EVTDDyaYSHTNEAVVYVNVHLAEGYKE 211
Cdd:cd00710 142 DVTDS--AREFNEKVITVNNELAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 25-212 1.02e-48

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 156.73  E-value: 1.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALEtineegepiednivevdgkE 104
Cdd:COG0663  10 TPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDP-------------------G 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLeprsaAIGVTIPDGRYIPAGMVVTsQAEADKLP 183
Cdd:COG0663  70 YPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSPAKVVR 142

                       170       180
                ....*....|....*....|....*....
gi 5542452  184 EVTDDYAYSHTNEAVVYVNvhLAEGYKET 212
Cdd:COG0663 143 ELTEEEIAFLRESAENYVE--LARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 27-207 1.22e-37

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 127.91  E-value: 1.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHAletineegepiednivevdGKEYA 106
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVN-PIRIGERTNIQDGSVLHV-------------------DPGYP 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  107 VYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLEPRSaaigvTIPDGRYIPAGMVVtSQAEADKLPEV 185
Cdd:cd04645  61 TIIGDNVTVGHGAVLHG-CTIGDNCLIGMGAIILdGAVIGKGSIVAAGS-----LVPPGKVIPPGSLV-AGSPAKVVREL 133

                       170       180
                ....*....|....*....|..
gi 5542452  186 TDDYAysHTNEAVVYVNVHLAE 207
Cdd:cd04645 134 TDEEI--AELRESAEHYVELAK 153
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 26-188 2.32e-22

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 88.58  E-value: 2.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:cd04745   1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFG-RIVIRDGANVQDNCVIH--------GFPGQDTVLEENG--- 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452  106 avYIGnnvslaHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLeprsAAIGVtIPDGRYIPAGMVVTSqAEADKLPE 184
Cdd:cd04745  69 --HIG------HGAILHG-CTIGRNALVGMNAVVMdGAVIGEESIV----GAMAF-VKAGTVIPPRSLIAG-SPAKVIRE 133


                ....
gi 5542452  185 VTDD 188
Cdd:cd04745 134 LSDE 137
PLN02296 PLN02296
carbonate dehydratase
 25-210 5.63e-16

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 74.39  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETineegepiednivEVDGKE 104
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFKSKVgnncVLEPRSAAIGVTIPDGRYIPAGMvVTSQAEADKLPE 184
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLLDGVV----VEKHAMVAAGALVRQNTRIPSGE-VWAGNPAKFLRK 191

                        170       180
                 ....*....|....*....|....*....
gi 5542452   185 VTDDYAYSHTNEAVVYVN---VHLAEGYK 210
Cdd:PLN02296 192 LTEEEIAFISQSATNYSNlaqVHAAENAK 220
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 26-144 4.00e-15

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 70.61  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIfVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLI-VQAGANLQDGCIMH--------GYCDTDTIVGENG--- 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 5542452   106 avYIGnnvslaHQSQVHGpAAVGDDTFIGMQAFVFKSKV 144
Cdd:PRK13627  79 --HIG------HGAILHG-CVIGRDALVGMNSVIMDGAV 108
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 26-173 7.39e-15

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 69.14  E-value: 7.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletiNEEGEPIEdnivevdgkey 105
Cdd:cd04650   1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDND-SIYIGKYSNVQENVSIH-----TDHGYPTE----------- 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5542452  106 avyIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFK-SKVGNNCVLeprsaAIGVTIPDGRYIPAGMVV 173
Cdd:cd04650  64 ---IGDYVTIGHNAVVHG-AKVGNYVIVGMGAILLNgAKIGDHVII-----GAGAVVTPGKEIPDYSLV 123
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 44-139 2.52e-13

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 62.65  E-value: 2.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   44 VTIGANVMVSPMASIRSdegmPIFVGDRSNVQDGVVLHALETINEEGEPIednivevdgkeyavyIGNNVSLAHQSQVHG 123
Cdd:cd00208   1 VFIGEGVKIHPKAVIRG----PVVIGDNVNIGPGAVIGAATGPNEKNPTI---------------IGDNVEIGANAVIHG 61

                        90
                ....*....|....*.
gi 5542452  124 PAAVGDDTFIGMQAFV 139
Cdd:cd00208  62 GVKIGDNAVIGAGAVV 77
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 27-149 8.23e-09

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 52.71  E-value: 8.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVL-HALETINEEGEPI---EDNIVEVDG 102
Cdd:cd04646   1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAG-PIIIGENNIIEEQVTIvNKKPKDPAEPKPMiigSNNVFEVGC 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5542452  103 KEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCV 149
Cdd:cd04646  80 KCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENT 126
PLN02472 PLN02472
uncharacterized protein
 26-205 2.13e-07

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 49.96  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETiNEEGEPIEDNIvevdgkEY 105
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLN-KITVGFCSNVQERCVLHAAWN-SPTGLPAETLI------DR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   106 AVYIGNNVSLAhqsqvhgPAAVGDDTFIGMQAFVFK-SKVGNNCVLEPrsaaiGVTIPDGRYIPAGMV-----------V 173
Cdd:PLN02472 132 YVTIGAYSLLR-------SCTIEPECIIGQHSILMEgSLVETHSILEA-----GSVLPPGRRIPTGELwagnparfvrtL 199

                        170       180       190
                 ....*....|....*....|....*....|....
gi 5542452   174 TSQA--EADKLPEVTDDYAYSHTNEAVVYVNVHL 205
Cdd:PLN02472 200 TNEEtlEIPKLAVAINDLSQSHFSEFLPYSTAYL 233
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 21-167 2.18e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 47.32  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   21 PEPSAPVIDPTAYIDPQAsVIGE-VTIGANVMVSPMASIrsdeGmpifvgdrsnvqDGVVLHAletineegepiednive 99
Cdd:COG1044  92 PPAPAPGIHPSAVIDPSA-KIGEgVSIGPFAVIGAGVVI----G------------DGVVIGP----------------- 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5542452  100 vdgkeyAVYIGNNVSlahqsqvhgpaaVGDDTFIGMQAFVFK-SKVGNNCVLEPrSAAIG------VTIPDGRYI 167
Cdd:COG1044 138 ------GVVIGDGVV------------IGDDCVLHPNVTIYErCVIGDRVIIHS-GAVIGadgfgfAPDEDGGWV 193
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
28-142 1.48e-05

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 43.32  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   28 IDPTAYIDPQASV-IGEVTIGANVMVSPMASIrsDEGMPIFVGDRSNVQDGVVL----HALETINEEGEPIEDnivevdg 102
Cdd:COG0110  11 IGDGVVIGPGVRIyGGNITIGDNVYIGPGVTI--DDPGGITIGDNVLIGPGVTIltgnHPIDDPATFPLRTGP------- 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5542452  103 keyaVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKS 142
Cdd:COG0110  82 ----VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD 117
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 23-132 6.83e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 6.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    23 PSAPVIDPTAYIDPQAsVIGE-VTIGANVMVSPMASIrsDEGMPI----FVGDRSNVQDGVVLHALETINEegepiedni 97
Cdd:PRK00892  98 SPAAGIHPSAVIDPSA-KIGEgVSIGPNAVIGAGVVI--GDGVVIgagaVIGDGVKIGADCRLHANVTIYH--------- 165

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 5542452    98 vevdgkeyAVYIGNNVSlahqsqVHGPAAVGDDTF 132
Cdd:PRK00892 166 --------AVRIGNRVI------IHSGAVIGSDGF 186
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
44-174 1.24e-04

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 40.62  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   44 VTIGANVMVSPMASIRsdeGMPIFVGDRSNVQDGVVLHALETINeegepIEDNivevdgkeyaVYIGNNVSL-------- 115
Cdd:COG0110   9 ARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIDDPGGIT-----IGDN----------VLIGPGVTIltgnhpid 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5542452  116 --AHQSQVHGPAAVGDDTFIGMQAFVFKskvgnncvleprsaaiGVTIPDGRYIPAGMVVT 174
Cdd:COG0110  71 dpATFPLRTGPVTIGDDVWIGAGATILP----------------GVTIGDGAVVGAGSVVT 115
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 28-150 1.69e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    28 IDPTAYIDPQASVIGEVTIGANVMVspmasirsdeGMPIFVGDRSNVQDGVVLHALETINEE---------GEPIEDniV 98
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVI----------GANVEIGDGTWIGPHAVILGPTRIGKNnkihqgavvGDEPQD--F 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 5542452    99 EVDGKEYAVYIGNN------VSLAHQSQVHGPAAVGDDTFigmqaFVFKSKVGNNCVL 150
Cdd:PRK12461  70 TYKGEESRLEIGDRnviregVTIHRGTKGGGVTRIGNDNL-----LMAYSHVAHDCQI 122
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 27-175 2.75e-04

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.47  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   27 VIDPTAYIDPQAsVIGE-VTIGANVMVSPMASIRSDegmpIFVGDRSNVQDGVVLHA--LETINEEGEP----------I 93
Cdd:cd03352  21 VIGDGVVIGPGV-VIGDgVVIGDDCVIHPNVTIYEG----CIIGDRVIIHSGAVIGSdgFGFAPDGGGWvkipqlggviI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   94 EDNiVE------VD-GKEYAVYIGNNVSLAHQSQV-HGpAAVGDDTFIGMQAFVFKS-KVGNNCVLEPRSAAIG-VTIPD 163
Cdd:cd03352  96 GDD-VEiganttIDrGALGDTVIGDGTKIDNLVQIaHN-VRIGENCLIAAQVGIAGStTIGDNVIIGGQVGIAGhLTIGD 173

                       170
                ....*....|..
gi 5542452  164 GRYIPAGMVVTS 175
Cdd:cd03352 174 GVVIGAGSGVTS 185
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 28-86 4.32e-03

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 37.03  E-value: 4.32e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   28 IDPTAYIDPQAsVIGE-VTIGANVMVSPMASIrsdegmpifvGDRSNVQDGVVLHALETI 86
Cdd:cd03351   2 IHPTAIVDPGA-KIGEnVEIGPFCVIGPNVEI----------GDGTVIGSHVVIDGPTTI 50
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 109-165 4.66e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.42  E-value: 4.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452    109 IGNNVSL----------AHQSQVH-GPAAVGDDTFIGMQAFVFK-SKVGNNCVLEPRSA-AIGVTIPDGR 165
Cdd:TIGR02353 134 IGAGTIVrkevmllgyrAERGRLHtGPVTLGRDAFIGTRSTLDIdTSIGDGAQLGHGSAlQGGQSIPDGE 203
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 66-174 6.46e-03

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 35.12  E-value: 6.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   66 IFVGDRSNVQDGVVLHALETINeegepIEDNivevdgkeyaVYIGNNVSL-------------AHQSQVHGPAAVGDDTF 132
Cdd:cd04647   2 ISIGDNVYIGPGCVISAGGGIT-----IGDN----------VLIGPNVTIydhnhdiddperpIEQGVTSAPIVIGDDVW 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 5542452  133 IGMQAFVFKskvgnncvleprsaaiGVTIPDGRYIPAGMVVT 174
Cdd:cd04647  67 IGANVVILP----------------GVTIGDGAVVGAGSVVT 92
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 27-182 7.32e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 36.24  E-value: 7.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEgmpifVGDRSNVQDGVVLHAlETINEE-----------GEPIED 95
Cdd:cd03353  17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDST-----IGDGVVIKASSVIEG-AVIGNGatvgpfahlrpGTVLGE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5542452   96 -----NIVEVdgKEyaVYIGNNVSLAHQSQVhGPAAVGDDTFIGmqAFV----------FKSKVGNNCVleprsaaIG-- 158
Cdd:cd03353  91 gvhigNFVEI--KK--STIGEGSKANHLSYL-GDAEIGEGVNIG--AGTitcnydgvnkHRTVIGDNVF-------IGsn 156

                       170       180       190
                ....*....|....*....|....*....|
gi 5542452  159 ------VTIPDGRYIPAGMVVTSQAEADKL 182
Cdd:cd03353 157 sqlvapVTIGDGATIAAGSTITKDVPPGAL 186
 
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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