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Conserved domains on  [gi|5542452|pdb|1QRG|A]
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Chain A, A Closer Look And The Active Site Of Gamma-Carbonic Anhydrases: High Resolution Crystallographic Studies Of The Carbonic Anhydrase From Methanosarcina Thermophila

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
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
24-211 1.92e-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: 1.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       24 SAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETineegepiednivevdgk 103
Cdd:cd00710   1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------ 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A      104 eYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLP 183
Cdd:cd00710  63 -YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALP 141
                       170       180
                ....*....|....*....|....*...
1QRG_A      184 EVTDDyaYSHTNEAVVYVNVHLAEGYKE 211
Cdd:cd00710 142 DVTDS--AREFNEKVITVNNELAEGYKA 167
 
Name Accession Description Interval E-value
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
24-211 1.92e-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: 1.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       24 SAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETineegepiednivevdgk 103
Cdd:cd00710   1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------ 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A      104 eYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLP 183
Cdd:cd00710  63 -YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALP 141
                       170       180
                ....*....|....*....|....*...
1QRG_A      184 EVTDDyaYSHTNEAVVYVNVHLAEGYKE 211
Cdd:cd00710 142 DVTDS--AREFNEKVITVNNELAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
15-213 1.86e-47

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


Pssm-ID: 223735 [Multi-domain]  Cd Length: 176  Bit Score: 153.51  E-value: 1.86e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       15 PVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALEtineegepie 94
Cdd:COG0663   1 MMMIYSYEGLSPKIDPTAFVAPSATVIGDVRIGAGVSIWPGAVLRGDVE-PIRIGARTNIQDGVVIHADP---------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       95 dnivevdgkEYAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFK-SKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVV 173
Cdd:COG0663  70 ---------GYPVTIGDDVTIGHGAVVHG-CTIGDNVLIGMGATVLDgAVIGDGSIVGAGALVTPGKEIPGGSLVVGSPA 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1QRG_A      174 TSQAEADKLPevtdDYAYSHTNEAVVYVNVHLAEGYKETS 213
Cdd:COG0663 140 KVVRPLDDEE----LAWLRENAENYVKLADRYLAGLKETQ 175
PLN02296 PLN02296
carbonate dehydratase
25-210 4.80e-16

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 74.39  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETineegepiednivEVDGKE 104
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFKSKVgnncVLEPRSAAIGVTIPDGRYIPAGMvVTSQAEADKLPE 184
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLLDGVV----VEKHAMVAAGALVRQNTRIPSGE-VWAGNPAKFLRK 191
                        170       180
                 ....*....|....*....|....*....
1QRG_A       185 VTDDYAYSHTNEAVVYVN---VHLAEGYK 210
Cdd:PLN02296 192 LTEEEIAFISQSATNYSNlaqVHAAENAK 220
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
26-150 7.09e-16

phenylacetic acid degradation protein PaaY; Members of this family are located next to other genes organized into apparent operons for phenylacetic acid degradation. PaaY is located near the end of these gene clusters and often next to PaaX, a transcriptional regulator. [Energy metabolism, Other]


Pssm-ID: 131340 [Multi-domain]  Cd Length: 192  Bit Score: 72.22  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A         26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:TIGR02287   9 PVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFG-RIVLKEGANIQDNCVMH--------GFPGQDTVVEENG--- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1QRG_A        106 avYIGnnvslaHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVL 150
Cdd:TIGR02287  77 --HVG------HGAILHG-CIVGRNALVGMNAVVMdGAVIGENSIV 113
 
Name Accession Description Interval E-value
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
24-211 1.92e-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: 1.92e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       24 SAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETineegepiednivevdgk 103
Cdd:cd00710   1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG------------------ 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A      104 eYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLP 183
Cdd:cd00710  63 -YSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALP 141
                       170       180
                ....*....|....*....|....*...
1QRG_A      184 EVTDDyaYSHTNEAVVYVNVHLAEGYKE 211
Cdd:cd00710 142 DVTDS--AREFNEKVITVNNELAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
15-213 1.86e-47

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


Pssm-ID: 223735 [Multi-domain]  Cd Length: 176  Bit Score: 153.51  E-value: 1.86e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       15 PVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALEtineegepie 94
Cdd:COG0663   1 MMMIYSYEGLSPKIDPTAFVAPSATVIGDVRIGAGVSIWPGAVLRGDVE-PIRIGARTNIQDGVVIHADP---------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       95 dnivevdgkEYAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFK-SKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVV 173
Cdd:COG0663  70 ---------GYPVTIGDDVTIGHGAVVHG-CTIGDNVLIGMGATVLDgAVIGDGSIVGAGALVTPGKEIPGGSLVVGSPA 139
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
1QRG_A      174 TSQAEADKLPevtdDYAYSHTNEAVVYVNVHLAEGYKETS 213
Cdd:COG0663 140 KVVRPLDDEE----LAWLRENAENYVKLADRYLAGLKETQ 175
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
27-207 1.04e-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: 1.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHAletineegepiednivevdGKEYA 106
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVN-PIRIGERTNIQDGSVLHV-------------------DPGYP 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A      107 VYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLEPRSaaigvTIPDGRYIPAGMVVtSQAEADKLPEV 185
Cdd:cd04645  61 TIIGDNVTVGHGAVLHG-CTIGDNCLIGMGAIILdGAVIGKGSIVAAGS-----LVPPGKVIPPGSLV-AGSPAKVVREL 133
                       170       180
                ....*....|....*....|..
1QRG_A      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 1.98e-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: 1.98e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:cd04745   1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFG-RIVIRDGANVQDNCVIH--------GFPGQDTVLEENG--- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A      106 avYIGnnvslaHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVLeprsAAIGVtIPDGRYIPAGMVVTSqAEADKLPE 184
Cdd:cd04745  69 --HIG------HGAILHG-CTIGRNALVGMNAVVMdGAVIGEESIV----GAMAF-VKAGTVIPPRSLIAG-SPAKVIRE 133

                ....
1QRG_A      185 VTDD 188
Cdd:cd04745 134 LSDE 137
PLN02296 PLN02296
carbonate dehydratase
25-210 4.80e-16

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 74.39  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        25 APVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETineegepiednivEVDGKE 104
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       105 YAVYIGNNVSLAHQSQVHGpAAVGDDTFIGMQAFVFKSKVgnncVLEPRSAAIGVTIPDGRYIPAGMvVTSQAEADKLPE 184
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLLDGVV----VEKHAMVAAGALVRQNTRIPSGE-VWAGNPAKFLRK 191
                        170       180
                 ....*....|....*....|....*....
1QRG_A       185 VTDDYAYSHTNEAVVYVN---VHLAEGYK 210
Cdd:PLN02296 192 LTEEEIAFISQSATNYSNlaqVHAAENAK 220
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
26-150 7.09e-16

phenylacetic acid degradation protein PaaY; Members of this family are located next to other genes organized into apparent operons for phenylacetic acid degradation. PaaY is located near the end of these gene clusters and often next to PaaX, a transcriptional regulator. [Energy metabolism, Other]


Pssm-ID: 131340 [Multi-domain]  Cd Length: 192  Bit Score: 72.22  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A         26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:TIGR02287   9 PVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFG-RIVLKEGANIQDNCVMH--------GFPGQDTVVEENG--- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
1QRG_A        106 avYIGnnvslaHQSQVHGpAAVGDDTFIGMQAFVF-KSKVGNNCVL 150
Cdd:TIGR02287  77 --HVG------HGAILHG-CIVGRNALVGMNAVVMdGAVIGENSIV 113
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
26-144 3.41e-15

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 70.61  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIfVGDRSNVQDGVVLHaletineeGEPIEDNIVEVDGkey 105
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLI-VQAGANLQDGCIMH--------GYCDTDTIVGENG--- 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
1QRG_A       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 6.30e-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: 6.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHaletiNEEGEPIEdnivevdgkey 105
Cdd:cd04650   1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDND-SIYIGKYSNVQENVSIH-----TDHGYPTE----------- 63
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1QRG_A      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 2.15e-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: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       44 VTIGANVMVSPMASIRSdegmPIFVGDRSNVQDGVVLHALETINEEGEPIednivevdgkeyavyIGNNVSLAHQSQVHG 123
Cdd:cd00208   1 VFIGEGVKIHPKAVIRG----PVVIGDNVNIGPGAVIGAATGPNEKNPTI---------------IGDNVEIGANAVIHG 61
                        90
                ....*....|....*.
1QRG_A      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 7.02e-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: 7.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVL-HALETINEEGEPI---EDNIVEVDG 102
Cdd:cd04646   1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAG-PIIIGENNIIEEQVTIvNKKPKDPAEPKPMiigSNNVFEVGC 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1QRG_A      103 KEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCV 149
Cdd:cd04646  80 KCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENT 126
PLN02472 PLN02472
uncharacterized protein
26-205 1.81e-07

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 49.96  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        26 PVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGmPIFVGDRSNVQDGVVLHALETiNEEGEPIEDNIvevdgkEY 105
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLN-KITVGFCSNVQERCVLHAAWN-SPTGLPAETLI------DR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       106 AVYIGNNVSLAhqsqvhgPAAVGDDTFIGMQAFVFK-SKVGNNCVLEPrsaaiGVTIPDGRYIPAGMV-----------V 173
Cdd:PLN02472 132 YVTIGAYSLLR-------SCTIEPECIIGQHSILMEgSLVETHSILEA-----GSVLPPGRRIPTGELwagnparfvrtL 199
                        170       180       190
                 ....*....|....*....|....*....|....
1QRG_A       174 TSQA--EADKLPEVTDDYAYSHTNEAVVYVNVHL 205
Cdd:PLN02472 200 TNEEtlEIPKLAVAINDLSQSHFSEFLPYSTAYL 233
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
23-132 5.83e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        23 PSAPVIDPTAYIDPQAsVIGE-VTIGANVMVSPMASIrsDEGMPI----FVGDRSNVQDGVVLHALETINEegepiedni 97
Cdd:PRK00892  98 SPAAGIHPSAVIDPSA-KIGEgVSIGPNAVIGAGVVI--GDGVVIgagaVIGDGVKIGADCRLHANVTIYH--------- 165
                         90       100       110
                 ....*....|....*....|....*....|....*
1QRG_A        98 vevdgkeyAVYIGNNVSlahqsqVHGPAAVGDDTF 132
Cdd:PRK00892 166 --------AVRIGNRVI------IHSGAVIGSDGF 186
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
28-150 1.44e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        28 IDPTAYIDPQASVIGEVTIGANVMVspmasirsdeGMPIFVGDRSNVQDGVVLHALETINEE---------GEPIEDniV 98
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVI----------GANVEIGDGTWIGPHAVILGPTRIGKNnkihqgavvGDEPQD--F 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
1QRG_A        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 2.34e-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: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       27 VIDPTAYIDPQAsVIGE-VTIGANVMVSPMASIRSDegmpIFVGDRSNVQDGVVLHA--LETINEEGEP----------I 93
Cdd:cd03352  21 VIGDGVVIGPGV-VIGDgVVIGDDCVIHPNVTIYEG----CIIGDRVIIHSGAVIGSdgFGFAPDGGGWvkipqlggviI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       94 EDNiVE------VD-GKEYAVYIGNNVSLAHQSQV-HGpAAVGDDTFIGMQAFVFKS-KVGNNCVLEPRSAAIG-VTIPD 163
Cdd:cd03352  96 GDD-VEiganttIDrGALGDTVIGDGTKIDNLVQIaHN-VRIGENCLIAAQVGIAGStTIGDNVIIGGQVGIAGhLTIGD 173
                       170
                ....*....|..
1QRG_A      164 GRYIPAGMVVTS 175
Cdd:cd03352 174 GVVIGAGSGVTS 185
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
20-134 3.17e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 223974 [Multi-domain]  Cd Length: 338  Bit Score: 40.36  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       20 NPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIrsDEGMPI----FVGDRSNVQDGVVLHALETINEEgepied 95
Cdd:COG1044  94 RPFNPAAGIHPTAVIDPTATIGKNVSIGPNVVIGAGVVI--GENVVIgagaVIGENVKIGDGTVIHPNVTIYHN------ 165
                        90       100       110
                ....*....|....*....|....*....|....*....
1QRG_A       96 nivevdgkeyaVYIGNNVSlahqsqVHGPAAVGDDTFIG 134
Cdd:COG1044 166 -----------VVIGNNVI------IHSGAVIGADGFGY 187
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
21-181 3.68e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 40.35  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A         21 PEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIrsDEGMPI----FVGDRSNVQDGVVLHALETINEEGEpIEDN 96
Cdd:TIGR01853  87 PPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEI--GENVIIgpgvVIGDDVVIGDGSRIHPNVVIYERVQ-LGKN 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A         97 -------IVEVDGKEYA---------------VYIGNNVSLA----------------------HQSQVHGPAAVGDDTF 132
Cdd:TIGR01853 164 viihsgaVIGSDGFGYAhtangghvkipqigrVIIEDDVEIGanttidrgafddtiigegtkidNLVQIAHNCRIGENCI 243
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
1QRG_A        133 IGMQAFVFKS-KVGNNCVLEPRSAAIG-VTIPDGRYIPAGMVVTSQAEADK 181
Cdd:TIGR01853 244 IVAQVGIAGStKIGRNVIIGGQVGVAGhLEIGDNVTIGAKSGVTKSIPPPG 294
glmU PRK14354
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
37-182 7.57e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.43  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        37 QASVIGEVTIGANVMVSPMASIRSDegmpifvgdrSNVQDGVVLhaletineegepieDNIVEVDGKEyavyIGNNVSLA 116
Cdd:PRK14354 310 TNSVIEESKVGDNVTVGPFAHLRPG----------SVIGEEVKI--------------GNFVEIKKST----IGEGTKVS 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       117 HQSQVhGPAAVGDDTFIGMQAFV--------FKSKVGNNcvleprsAAIG--------VTIPDGRYIPAGMVVTSQAEAD 180
Cdd:PRK14354 362 HLTYI-GDAEVGENVNIGCGTITvnydgknkFKTIIGDN-------AFIGcnsnlvapVTVGDNAYIAAGSTITKDVPED 433

                 ..
1QRG_A       181 KL 182
Cdd:PRK14354 434 AL 435
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
34-182 8.53e-04

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224128 [Multi-domain]  Cd Length: 460  Bit Score: 39.47  E-value: 8.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       34 IDPQASVIGEVTIGANVMVSPMASIRSdegmpifvgdrSNVQDGVVLHALETIneEGEPIED------------------ 95
Cdd:COG1207 277 IEPNVILEGNTVIGDNVVIGPGSVIKD-----------SVIGDNAVIKAYSVI--EGSTVGEgatvgpfarlrpgavlga 343
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       96 -----NIVEVDGKEyavyIGNNVSLAHQSQVhGPAAVGDDTFIGMQAFV--------FKSKVGNNcvleprsAAIG---- 158
Cdd:COG1207 344 dvhigNFVEVKKAT----IGKGSKAGHLTYL-GDAEIGENVNIGAGTITcnydgknkFKTIIGDN-------VFIGsnsq 411
                       170       180
                ....*....|....*....|....*...
1QRG_A      159 ----VTIPDGRYIPAGMVVTSQAEADKL 182
Cdd:COG1207 412 lvapVTIGDGATIAAGSTITKDVPEGAL 439
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
25-175 2.04e-03

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 37.47  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A         25 APVIDPTAYIDPQASvIGE-VTIGANVMVSPMASIrsdegmpifvGDRSNVQDGVvlhaletineegepiednIVEVDgk 103
Cdd:TIGR03570  87 ATLIHPSAIVSPSAS-IGEgTVIMAGAVINPDVRI----------GDNVIINTGA------------------IVEHD-- 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1QRG_A        104 eyaVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAfvfkskvgnnCVLEprsaaiGVTIPDGRYIPAGMVVTS 175
Cdd:TIGR03570 136 ---CVIGDFVHIAPGVTLSGGVVIGEGVFIGAGA----------TIIQ------GVTIGAGAIVGAGAVVTK 188
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
28-86 3.69e-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: 3.69e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       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 3.97e-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: 3.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A        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 5.51e-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: 5.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       66 IFVGDRSNVQDGVVLHALETINeegepIEDNivevdgkeyaVYIGNNVSL-------------AHQSQVHGPAAVGDDTF 132
Cdd:cd04647   2 ISIGDNVYIGPGCVISAGGGIT-----IGDN----------VLIGPNVTIydhnhdiddperpIEQGVTSAPIVIGDDVW 66
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1QRG_A      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 6.25e-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: 6.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       27 VIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEgmpifVGDRSNVQDGVVLHAlETINEE-----------GEPIED 95
Cdd:cd03353  17 EIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDST-----IGDGVVIKASSVIEG-AVIGNGatvgpfahlrpGTVLGE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       96 -----NIVEVdgKEyaVYIGNNVSLAHQSQVhGPAAVGDDTFIGmqAFV----------FKSKVGNNCVleprsaaIG-- 158
Cdd:cd03353  91 gvhigNFVEI--KK--STIGEGSKANHLSYL-GDAEIGEGVNIG--AGTitcnydgvnkHRTVIGDNVF-------IGsn 156
                       170       180       190
                ....*....|....*....|....*....|
1QRG_A      159 ------VTIPDGRYIPAGMVVTSQAEADKL 182
Cdd:cd03353 157 sqlvapVTIGDGATIAAGSTITKDVPPGAL 186
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
44-149 9.80e-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: 34.35  E-value: 9.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QRG_A       44 VTIGANVMVSPMASIRSDEGmpIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGkeyaVYIGNNVSLAHQSQVHG 123
Cdd:cd04647   2 ISIGDNVYIGPGCVISAGGG--ITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAP----IVIGDDVWIGANVVILP 75
                        90       100
                ....*....|....*....|....*.
1QRG_A      124 PAAVGDDTFIGMQAFVFKSkVGNNCV 149
Cdd:cd04647  76 GVTIGDGAVVGAGSVVTKD-VPPNSI 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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