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Conserved domains on  [gi|851268552|ref|WP_048140392|]
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carbonic anhydrase [Methanosarcina horonobensis]

Protein Classification

LbH_gamma_CA domain-containing protein( domain architecture ID 10091094)

LbH_gamma_CA domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
carb_anhyd super family cl48897
carbonic anhydrase;
1-247 1.01e-162

carbonic anhydrase;


The actual alignment was detected with superfamily member NF040597:

Pssm-ID: 468571  Cd Length: 248  Bit Score: 450.07  E-value: 1.01e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552   1 MKFNRVFMVLLLSLALTLAGSGCVSESEGAQENdNIEADAESEVLNIRANPVTPWNPEPTEPVIDSTAYIHPQASVIGSV 80
Cdd:NF040597   1 MKFNQIFTILILSLSLTLAGSGCVSEGEGAEDN-VAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  81 TIGARVMVSPMASVRSDEGMPIFVGDDSNIQDGVVLHALETIDEEGESVEKNLVEVDGKKYAVYVGERVSLAHQSQVHGP 160
Cdd:NF040597  80 TIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 161 AYVGNDTFIGMQALVFKAKVGNNCVLEPTSAAIGVTIPDGRYVPAGTVITSQVEADKLPKVTDDYAYRHTNEGVVYVNTN 240
Cdd:NF040597 160 AYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVN 239


                 ....*..
gi 851268552 241 LAEGYNA 247
Cdd:NF040597 240 LAEGYNA 246
 
Name Accession Description Interval E-value
carb_anhyd NF040597
carbonic anhydrase;
1-247 1.01e-162

carbonic anhydrase;


Pssm-ID: 468571  Cd Length: 248  Bit Score: 450.07  E-value: 1.01e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552   1 MKFNRVFMVLLLSLALTLAGSGCVSESEGAQENdNIEADAESEVLNIRANPVTPWNPEPTEPVIDSTAYIHPQASVIGSV 80
Cdd:NF040597   1 MKFNQIFTILILSLSLTLAGSGCVSEGEGAEDN-VAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  81 TIGARVMVSPMASVRSDEGMPIFVGDDSNIQDGVVLHALETIDEEGESVEKNLVEVDGKKYAVYVGERVSLAHQSQVHGP 160
Cdd:NF040597  80 TIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 161 AYVGNDTFIGMQALVFKAKVGNNCVLEPTSAAIGVTIPDGRYVPAGTVITSQVEADKLPKVTDDYAYRHTNEGVVYVNTN 240
Cdd:NF040597 160 AYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVN 239


                 ....*..
gi 851268552 241 LAEGYNA 247
Cdd:NF040597 240 LAEGYNA 246
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 61-245 4.06e-79

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: 235.21  E-value: 4.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  61 EPVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGMPIFVGDDSNIQDGVVLHALETideegesveknlvevdgkk 140
Cdd:cd00710    2 EPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 141 YAVYVGERVSLAHQSQVHGPAYVGNDTFIGMQALVFKAKVGNNCVLEPTSAAIGVTIPDGRYVPAGTVITSQVEADKLPK 220
Cdd:cd00710   63 YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPD 142

                        170       180
                 ....*....|....*....|....*
gi 851268552 221 VTDDyaYRHTNEGVVYVNTNLAEGY 245
Cdd:cd00710  143 VTDS--AREFNEKVITVNNELAEGY 165
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 56-224 1.41e-46

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 152.49  E-value: 1.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  56 NPEPTEPVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHALEtideegesveknlve 135
Cdd:COG0663    5 SFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDP--------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 136 vdgkKYAVYVGERVSLAHQSQVHGpAYVGNDTFIGMQALVF-KAKVGNNCVLeptsaAIGVTIPDGRYVPAGTVITsQVE 214
Cdd:COG0663   69 ----GYPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSP 137

                        170
                 ....*....|
gi 851268552 215 ADKLPKVTDD 224
Cdd:COG0663  138 AKVVRELTEE 147
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 62-180 2.52e-14

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 69.07  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  62 PVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGMPIfVGDDSNIQDGVVLHALETIDeegesvekNLVEVDGKky 141
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLI-VQAGANLQDGCIMHGYCDTD--------TIVGENGH-- 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 851268552 142 avyvgervsLAHQSQVHGpAYVGNDTFIGMQALVFKAKV 180
Cdd:PRK13627  80 ---------IGHGAILHG-CVIGRDALVGMNSVIMDGAV 108
 
Name Accession Description Interval E-value
carb_anhyd NF040597
carbonic anhydrase;
1-247 1.01e-162

carbonic anhydrase;


Pssm-ID: 468571  Cd Length: 248  Bit Score: 450.07  E-value: 1.01e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552   1 MKFNRVFMVLLLSLALTLAGSGCVSESEGAQENdNIEADAESEVLNIRANPVTPWNPEPTEPVIDSTAYIHPQASVIGSV 80
Cdd:NF040597   1 MKFNQIFTILILSLSLTLAGSGCVSEGEGAEDN-VAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  81 TIGARVMVSPMASVRSDEGMPIFVGDDSNIQDGVVLHALETIDEEGESVEKNLVEVDGKKYAVYVGERVSLAHQSQVHGP 160
Cdd:NF040597  80 TIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 161 AYVGNDTFIGMQALVFKAKVGNNCVLEPTSAAIGVTIPDGRYVPAGTVITSQVEADKLPKVTDDYAYRHTNEGVVYVNTN 240
Cdd:NF040597 160 AYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVN 239


                 ....*..
gi 851268552 241 LAEGYNA 247
Cdd:NF040597 240 LAEGYNA 246
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 61-245 4.06e-79

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: 235.21  E-value: 4.06e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  61 EPVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGMPIFVGDDSNIQDGVVLHALETideegesveknlvevdgkk 140
Cdd:cd00710    2 EPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 141 YAVYVGERVSLAHQSQVHGPAYVGNDTFIGMQALVFKAKVGNNCVLEPTSAAIGVTIPDGRYVPAGTVITSQVEADKLPK 220
Cdd:cd00710   63 YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPD 142

                        170       180
                 ....*....|....*....|....*
gi 851268552 221 VTDDyaYRHTNEGVVYVNTNLAEGY 245
Cdd:cd00710  143 VTDS--AREFNEKVITVNNELAEGY 165
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 56-224 1.41e-46

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 152.49  E-value: 1.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  56 NPEPTEPVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHALEtideegesveknlve 135
Cdd:COG0663    5 SFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDP--------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 136 vdgkKYAVYVGERVSLAHQSQVHGpAYVGNDTFIGMQALVF-KAKVGNNCVLeptsaAIGVTIPDGRYVPAGTVITsQVE 214
Cdd:COG0663   69 ----GYPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSP 137

                        170
                 ....*....|
gi 851268552 215 ADKLPKVTDD 224
Cdd:COG0663  138 AKVVRELTEE 147
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 63-225 4.69e-32

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: 114.82  E-value: 4.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  63 VIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHAletideegesveknlvevdGKKYA 142
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVN-PIRIGERTNIQDGSVLHV-------------------DPGYP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 143 VYVGERVSLAHQSQVHGpAYVGNDTFIGMQALVF-KAKVGNNCVLEPtsaaiGVTIPDGRYVPAGTVItSQVEADKLPKV 221
Cdd:cd04645   61 TIIGDNVTVGHGAVLHG-CTIGDNCLIGMGAIILdGAVIGKGSIVAA-----GSLVPPGKVIPPGSLV-AGSPAKVVREL 133


                 ....
gi 851268552 222 TDDY 225
Cdd:cd04645  134 TDEE 137
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 62-236 1.22e-20

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: 85.11  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  62 PVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHALETIDeegesvekNLVEVDGkky 141
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFG-RIVIRDGANVQDNCVIHGFPGQD--------TVLEENG--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 142 avYVGervslaHQSQVHGpAYVGNDTFIGMQALVF-KAKVGNNCVLEPTSaaigvTIPDGRYVPAGTVITSqVEADKLPK 220
Cdd:cd04745   69 --HIG------HGAILHG-CTIGRNALVGMNAVVMdGAVIGEESIVGAMA-----FVKAGTVIPPRSLIAG-SPAKVIRE 133

                        170
                 ....*....|....*.
gi 851268552 221 VTDDYAYRHTNEGVVY 236
Cdd:cd04745  134 LSDEEVAWKTRGTKEY 149
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 62-224 1.97e-14

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: 68.37  E-value: 1.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  62 PVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHAletideegesveknlvevdGKKY 141
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDND-SIYIGKYSNVQENVSIHT-------------------DHGY 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 142 AVYVGERVSLAHQSQVHGpAYVGNDTFIGMQALVFK-AKVGNNCVLeptsaAIGVTIPDGRYVPAGTVITSqVEADKLPK 220
Cdd:cd04650   61 PTEIGDYVTIGHNAVVHG-AKVGNYVIVGMGAILLNgAKIGDHVII-----GAGAVVTPGKEIPDYSLVLG-VPAKVVRK 133


                 ....
gi 851268552 221 VTDD 224
Cdd:cd04650  134 LTEE 137
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 62-180 2.52e-14

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 69.07  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  62 PVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGMPIfVGDDSNIQDGVVLHALETIDeegesvekNLVEVDGKky 141
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLI-VQAGANLQDGCIMHGYCDTD--------TIVGENGH-- 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 851268552 142 avyvgervsLAHQSQVHGpAYVGNDTFIGMQALVFKAKV 180
Cdd:PRK13627  80 ---------IGHGAILHG-CVIGRDALVGMNSVIMDGAV 108
PLN02296 PLN02296
carbonate dehydratase
 61-210 3.58e-11

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 61.68  E-value: 3.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  61 EPVIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVLHALETideegesveknlvEVDGKK 140
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 141 YAVYVGERVSLAHQSQVHGpAYVGNDTFIGMQALVFKakvgnncvleptsaaiGVTIPDGRYVPAGTVIT 210
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLLD----------------GVVVEKHAMVAAGALVR 170
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 80-175 1.08e-10

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: 56.10  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  80 VTIGARVMVSPMASVRSdegmPIFVGDDSNIQDGVVLHALETideegesveknlvevDGKKYAVYVGERVSLAHQSQVHG 159
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG----PVVIGDNVNIGPGAVIGAATG---------------PNEKNPTIIGDNVEIGANAVIHG 61

                         90
                 ....*....|....*.
gi 851268552 160 PAYVGNDTFIGMQALV 175
Cdd:cd00208   62 GVKIGDNAVIGAGAVV 77
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 63-209 1.70e-05

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: 43.85  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  63 VIDSTAYIHPQASVIGSVTIGARVMVSPMASVRSDEGmPIFVGDDSNIQDGVVL-HALETIDEEGESV---EKNLVEVDG 138
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAG-PIIIGENNIIEEQVTIvNKKPKDPAEPKPMiigSNNVFEVGC 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851268552 139 KKYAVYVGERVSLahqsQVHgpAYVGNDTfigmqalvfkaKVGNNCVLeptsaAIGVTIPDGRYVPAGTVI 209
Cdd:cd04646   80 KCEALKIGNNNVF----ESK--SFVGKNV-----------IITDGCII-----GAGCKLPSSEILPENTVI 128
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 57-209 2.50e-04

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: 41.54  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  57 PEPTEPVIDSTAYIHPQASVIGSVTIGARVmvspmasvrsdegmpiFVGDDSNIQDGVVLHAletideegesveknlvev 136
Cdd:COG1044   92 PPAPAPGIHPSAVIDPSAKIGEGVSIGPFA----------------VIGAGVVIGDGVVIGP------------------ 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 137 dgkkyAVYVGERVSlahqsqvhgpayVGNDTFIGMQA-LVFKAKVGNNCVLEPtSAAIG------VTIPDGRYVP---AG 206
Cdd:COG1044  138 -----GVVIGDGVV------------IGDDCVLHPNVtIYERCVIGDRVIIHS-GAVIGadgfgfAPDEDGGWVKipqLG 199


                 ...
gi 851268552 207 TVI 209
Cdd:COG1044  200 RVV 202
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-218 4.50e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  73 QASVIGSVTIGARVMVSPMASVRsdegmPifvgdDSNIQDGVVLhaletideegesveKNLVEVdgKKyaVYVGERVSLA 152
Cdd:PRK14354 310 TNSVIEESKVGDNVTVGPFAHLR-----P-----GSVIGEEVKI--------------GNFVEI--KK--STIGEGTKVS 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 153 HQSQVhGPAYVGNDTFIGMQALV--------FKAKVGNNcvleptsAAIG--------VTIPDGRYVPAGTVITSQVEAD 216
Cdd:PRK14354 362 HLTYI-GDAEVGENVNIGCGTITvnydgknkFKTIIGDN-------AFIGcnsnlvapVTVGDNAYIAAGSTITKDVPED 433


                 ..
gi 851268552 217 KL 218
Cdd:PRK14354 434 AL 435
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
64-177 6.15e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.08  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  64 IDSTAYIHPQASV-IGSVTIGARVMVSPMASVrsDEGMPIFVGDDSNIQDGVVL----HALETIDEEGESVEKnlvevdg 138
Cdd:COG0110   11 IGDGVVIGPGVRIyGGNITIGDNVYIGPGVTI--DDPGGITIGDNVLIGPGVTIltgnHPIDDPATFPLRTGP------- 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 851268552 139 kkyaVYVGERVSLAHQSQVHGPAYVGNDTFIGMQALVFK 177
Cdd:COG0110   82 ----VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTK 116
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 63-217 3.09e-03

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: 37.77  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  63 VIDSTAYIHPQAsVIGS-VTIGARVMVSPMASVRSDegmpIFVGDDSNIQDGVVLHA-----------LETIDEEGESVE 130
Cdd:cd03352   21 VIGDGVVIGPGV-VIGDgVVIGDDCVIHPNVTIYEG----CIIGDRVIIHSGAVIGSdgfgfapdgggWVKIPQLGGVII 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 131 KNLVE------VD-GKKYAVYVGERVSLAHQSQV-HGpAYVGNDTFIGMQALVF-KAKVGNNCVLEPTSAAIG-VTIPDG 200
Cdd:cd03352   96 GDDVEiganttIDrGALGDTVIGDGTKIDNLVQIaHN-VRIGENCLIAAQVGIAgSTTIGDNVIIGGQVGIAGhLTIGDG 174

                        170
                 ....*....|....*..
gi 851268552 201 RYVPAGTVITSQVEADK 217
Cdd:cd03352  175 VVIGAGSGVTSIVPPGE 191
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 63-218 6.43e-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: 36.63  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552  63 VIDSTAYIHPQASVIGSVTIGARVMVSPMASVRsdegmpifvgdDSNIQDGVVLHALETIdeEGESVEK----------- 131
Cdd:cd03353   17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-----------DSTIGDGVVIKASSVI--EGAVIGNgatvgpfahlr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 132 ------------NLVEVdgKKyaVYVGERVSLAHQSQVhGPAYVGNDTFIGMQALV--------FKAKVGNNCVleptsa 191
Cdd:cd03353   84 pgtvlgegvhigNFVEI--KK--STIGEGSKANHLSYL-GDAEIGEGVNIGAGTITcnydgvnkHRTVIGDNVF------ 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 851268552 192 aIG--------VTIPDGRYVPAGTVITSQVEADKL 218
Cdd:cd03353  153 -IGsnsqlvapVTIGDGATIAAGSTITKDVPPGAL 186
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 64-118 7.47e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 7.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 851268552  64 IDSTAYIHPQASVIGSVTIGARVMVSpmASVRSDEGMPI----FVGDDSNIQDGVVLHA 118
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIG--AGVVIGDGVVIgagaVIGDGVKIGADCRLHA 159
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 143-213 9.62e-03

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 35.43  E-value: 9.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851268552 143 VYVGERVSLAHQSQVHGPAYVGNDTFIGMQALV-FKAKVGNNC----------VLEPTSAAiGVTIPDGRYVPAGTVITS 211
Cdd:cd03350   14 AFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVgSCAQIGKNVhlsagaviggVLEPLQAT-PVIIEDDVFIGANCEVVE 92


                 ..
gi 851268552 212 QV 213
Cdd:cd03350   93 GV 94
 
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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