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Conserved domains on  [gi|499779248|ref|WP_011459982|]
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MULTISPECIES: transferase [Desulfitobacterium]

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 ...
 16-182 2.75e-84

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: 246.00  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGLTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVH 95
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  96 GPAVIGRETFVGFRAIVHNATLGKNSFISHGAMVLNVELPDDSSVPVGKIIQSEAEVRELPAIVVQEISFKHDVQQINRE 175
Cdd:cd00710   81 GPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPDVTDSAREFNEKVITVNNE 160


                 ....*..
gi 499779248 176 LGRGYRE 182
Cdd:cd00710  161 LAEGYKA 167
 
Name Accession Description Interval E-value
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 16-182 2.75e-84

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: 246.00  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGLTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVH 95
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  96 GPAVIGRETFVGFRAIVHNATLGKNSFISHGAMVLNVELPDDSSVPVGKIIQSEAEVRELPAIVVQEISFKHDVQQINRE 175
Cdd:cd00710   81 GPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPDVTDSAREFNEKVITVNNE 160


                 ....*..
gi 499779248 176 LGRGYRE 182
Cdd:cd00710  161 LAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 16-182 8.09e-51

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 160.96  E-value: 8.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVH 95
Cdd:COG0663    9 KTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAILH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  96 GpAVIGRETFVGFRAIVHN-ATLGKNSFISHGAMVlnvelPDDSSVPVGKII-QSEAE-VRELPAivvQEISFKHDVQQI 172
Cdd:COG0663   88 G-CTIGDNVLIGMGAIVLDgAVIGDGSIVGAGALV-----TEGKVVPPGSLVvGSPAKvVRELTE---EEIAFLRESAEN 158

                        170
                 ....*....|
gi 499779248 173 NRELGRGYRE 182
Cdd:COG0663  159 YVELARRYLA 168
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 18-128 2.81e-24

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 94.10  E-value: 2.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVHGp 97
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYG-RLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGAILHG- 88

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499779248  98 AVIGRETFVGFRAIVHN-ATLGKNSFIshGAM 128
Cdd:PRK13627  89 CVIGRDALVGMNSVIMDgAVIGEESIV--AAM 118
 
Name Accession Description Interval E-value
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 16-182 2.75e-84

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: 246.00  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGLTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVH 95
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  96 GPAVIGRETFVGFRAIVHNATLGKNSFISHGAMVLNVELPDDSSVPVGKIIQSEAEVRELPAIVVQEISFKHDVQQINRE 175
Cdd:cd00710   81 GPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPDVTDSAREFNEKVITVNNE 160


                 ....*..
gi 499779248 176 LGRGYRE 182
Cdd:cd00710  161 LAEGYKA 167
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 16-182 8.09e-51

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 160.96  E-value: 8.09e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVH 95
Cdd:COG0663    9 KTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAILH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  96 GpAVIGRETFVGFRAIVHN-ATLGKNSFISHGAMVlnvelPDDSSVPVGKII-QSEAE-VRELPAivvQEISFKHDVQQI 172
Cdd:COG0663   88 G-CTIGDNVLIGMGAIVLDgAVIGDGSIVGAGALV-----TEGKVVPPGSLVvGSPAKvVRELTE---EEIAFLRESAEN 158

                        170
                 ....*....|
gi 499779248 173 NRELGRGYRE 182
Cdd:COG0663  159 YVELARRYLA 168
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 19-138 1.47e-34

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: 119.05  E-value: 1.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  19 KVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVHGpA 98
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVN-PIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHG-C 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 499779248  99 VIGRETFVGFRAIV-HNATLGKNSFISHGAMVL-NVELPDDS 138
Cdd:cd04645   79 TIGDNCLIGMGAIIlDGAVIGKGSIVAAGSLVPpGKVIPPGS 120
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 18-164 1.28e-27

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: 101.29  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVHGp 97
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFG-RIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHG- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499779248  98 AVIGRETFVGFRAIVHN-ATLGKNSFIshGAMvlnvelpddSSVPVGKIIQSEAEVRELPAIVVQEIS 164
Cdd:cd04745   79 CTIGRNALVGMNAVVMDgAVIGEESIV--GAM---------AFVKAGTVIPPRSLIAGSPAKVIRELS 135
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 18-128 2.81e-24

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 94.10  E-value: 2.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVHGp 97
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYG-RLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGAILHG- 88

                         90       100       110
                 ....*....|....*....|....*....|..
gi 499779248  98 AVIGRETFVGFRAIVHN-ATLGKNSFIshGAM 128
Cdd:PRK13627  89 CVIGRDALVGMNSVIMDgAVIGEESIV--AAM 118
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 18-140 3.92e-21

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: 84.54  E-value: 3.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVHGp 97
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDND-SIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHG- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499779248  98 AVIGRETFVGFRAIVHN-ATLGKNSFISHGAMVL-NVELPDDSSV 140
Cdd:cd04650   79 AKVGNYVIVGMGAILLNgAKIGDHVIIGAGAVVTpGKEIPDYSLV 123
PLN02296 PLN02296
carbonate dehydratase
 8-145 2.57e-16

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 74.39  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248   8 KTSWNRTSKHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLK---GGSIE--- 81
Cdd:PLN02296  43 RTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKtnlSGKVLpti 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499779248  82 IGQDCSIAHCALVHGPAViGRETFVGFRA-IVHNATLGKNSFISHGAMVLnvelpDDSSVPVGKI 145
Cdd:PLN02296 122 IGDNVTIGHSAVLHGCTV-EDEAFVGMGAtLLDGVVVEKHAMVAAGALVR-----QNTRIPSGEV 180
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 18-118 7.72e-09

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: 53.87  E-value: 7.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVlradegltiiIGAGVNIQDGVImhclkggsieIGQDCSI-AHCALVHG 96
Cdd:COG1044   97 PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVV----------IGDGVVIGPGVV----------IGDGVVIgDDCVLHPN 156

                         90       100
                 ....*....|....*....|...
gi 499779248  97 pAVIGRETFVGFRAIVH-NATLG 118
Cdd:COG1044  157 -VTIYERCVIGDRVIIHsGAVIG 178
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 18-108 2.22e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.45  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADegltIIIGAGVNIQDGVIM--HCLKGGSIEIGQDCSIAHCALVH 95
Cdd:PRK00892 101 AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDG----VVIGAGAVIGDGVKIgaDCRLHANVTIYHAVRIGNRVIIH 176

                         90
                 ....*....|...
gi 499779248  96 GPAVIGRETFvGF 108
Cdd:PRK00892 177 SGAVIGSDGF-GF 188
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 25-143 1.52e-07

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 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. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 49.02  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  25 YVHPTAVLIGDVRVCENVMICPNVVlradegltiiIGAGVNIQDGVIMHClkgGSIeIGQDCSI-AHC-----ALVHGPA 98
Cdd:cd03360   86 LIHPSAVVSPSAVIGEGCVIMAGAV----------INPDARIGDNVIINT---GAV-IGHDCVIgDFVhiapgVVLSGGV 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499779248  99 VIGRETFVGFRAIV-HNATLGKNSFISHGAMVL-NVElpdDSSVPVG 143
Cdd:cd03360  152 TIGEGAFIGAGATIiQGVTIGAGAIIGAGAVVTkDVP---DGSVVVG 195
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 16-118 5.26e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.60  E-value: 5.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDVRVCENVMICPNVVlradegltiiIGAGVNIQDGVIM--HCLKGGSIEIGQDCSIahcal 93
Cdd:PRK00892  93 PPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAV----------IGAGVVIGDGVVIgaGAVIGDGVKIGADCRL----- 157

                         90       100
                 ....*....|....*....|....*.
gi 499779248  94 vHGPAVIGRETFVGFRAIVH-NATLG 118
Cdd:PRK00892 158 -HANVTIYHAVRIGNRVIIHsGAVIG 182
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
16-112 1.14e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.02  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  16 KHPKVHHTAYVHPTAVLIGDvrvceNVMICPNVVLRADEGLTI----IIGAGVNIQDG------VIMHCLKGGSIEIGQD 85
Cdd:COG0110   13 DGVVIGPGVRIYGGNITIGD-----NVYIGPGVTIDDPGGITIgdnvLIGPGVTILTGnhpiddPATFPLRTGPVTIGDD 87

                         90       100
                 ....*....|....*....|....*..
gi 499779248  86 CSIAHCALVHGPAVIGRETFVGFRAIV 112
Cdd:COG0110   88 VWIGAGATILPGVTIGDGAVVGAGSVV 114
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
29-130 7.65e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 43.71  E-value: 7.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  29 TAVLIGDVRVCENVMICPNVVLRadeGLTIIIGAGVNIQDGVIMHClkGGSIEIGQDCSIAHCALVHGpAVIGRETFVGF 108
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIDD--PGGITIGDNVLIGPGVTILT-GNHPIDDPATF 75

                         90       100
                 ....*....|....*....|..
gi 499779248 109 RAIVHNATLGKNSFISHGAMVL 130
Cdd:COG0110   76 PLRTGPVTIGDDVWIGAGATIL 97
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 19-112 2.76e-05

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: 40.70  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  19 KVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGLTiiigagvniqdgvimhclKGGSIEIGQDCSIAHCALVHGPA 98
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN------------------EKNPTIIGDNVEIGANAVIHGGV 63

                         90
                 ....*....|....
gi 499779248  99 VIGRETFVGFRAIV 112
Cdd:cd00208   64 KIGDNAVIGAGAVV 77
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 58-129 2.81e-05

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: 41.29  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  58 IIIGAGVNIQDGVIMHClkGGSIEIGQDCSIAHCA-------------------LVHGPAVIGRETFVGFRAIVH-NATL 117
Cdd:cd04647    2 ISIGDNVYIGPGCVISA--GGGITIGDNVLIGPNVtiydhnhdiddperpieqgVTSAPIVIGDDVWIGANVVILpGVTI 79

                         90
                 ....*....|..
gi 499779248 118 GKNSFISHGAMV 129
Cdd:cd04647   80 GDGAVVGAGSVV 91
PLN02472 PLN02472
uncharacterized protein
 18-145 5.68e-05

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 42.26  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADEGlTIIIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCALVhGP 97
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLN-KITVGFCSNVQERCVLHAAWNSPTGLPAETLIDRYVTI-GA 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499779248  98 ------AVIGRETFVGFRAIVHNATLGK-NSFISHGAMvlnveLPDDSSVPVGKI 145
Cdd:PLN02472 138 ysllrsCTIEPECIIGQHSILMEGSLVEtHSILEAGSV-----LPPGRRIPTGEL 187
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 26-125 1.26e-04

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: 40.87  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  26 VHPTAVLIGDVRVCENVMICPNVVLRADegltiIIGAGVNIQDGVIMHclkggSIEIGQDCSIAHCALVHGPAVIGRETF 105
Cdd:cd03353   24 IDPGVILEGKTVIGEDCVIGPNCVIKDS-----TIGDGVVIKASSVIE-----GAVIGNGATVGPFAHLRPGTVLGEGVH 93

                         90       100
                 ....*....|....*....|
gi 499779248 106 VGFRAIVHNATLGKNSFISH 125
Cdd:cd03353   94 IGNFVEIKKSTIGEGSKANH 113
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 26-125 2.52e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.78  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  26 VHPTAVLIGDVRVCENVMICPNVVLRAdegltIIIGAGVNIQDGVIMHClkggsiEIGQDCSIahcalvhGP-------A 98
Cdd:COG1207  275 IDPNVILEGKTVIGEGVVIGPNCTLKD-----STIGDGVVIKYSVIEDA------VVGAGATV-------GPfarlrpgT 336

                         90       100
                 ....*....|....*....|....*...
gi 499779248  99 VIGRETFVG-FrAIVHNATLGKNSFISH 125
Cdd:COG1207  337 VLGEGVKIGnF-VEVKNSTIGEGSKVNH 363
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 66-129 8.63e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.94  E-value: 8.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499779248  66 IQDGVIMHclKGGSIEIGQDCSIAHCALVHGPAVIGRETFVGFRAIVHNATLGKNSFISHGAMV 129
Cdd:PRK14356 252 LESGVLIH--APESVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWLRDAVVSSGATI 313
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 49-129 1.83e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.88  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  49 VLRADEGLTI----IIGAGVNIQDGVIMHCLKGGSIEIGQDCSIAHCaLVHGPAVIGRetfvgfRAIVHNATLGKNSFIS 124
Cdd:PRK00844 303 FVDGGGRVGSaqdsLVSAGSIISGATVRNSVLSPNVVVESGAEVEDS-VLMDGVRIGR------GAVVRRAILDKNVVVP 375


                 ....*
gi 499779248 125 HGAMV 129
Cdd:PRK00844 376 PGATI 380
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 36-130 2.24e-03

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: 35.30  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  36 VRVCENVMICPNVVLRAdeglTIIIGAGVNIQDGVIMH----CLKGGSIEIGQDCSIAHCALVHGpavigretfvgfrai 111
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG----PVVIGDNVNIGPGAVIGaatgPNEKNPTIIGDNVEIGANAVIHG--------------- 61

                         90
                 ....*....|....*....
gi 499779248 112 vhNATLGKNSFISHGAMVL 130
Cdd:cd00208   62 --GVKIGDNAVIGAGAVVT 78
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 19-101 4.09e-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: 36.64  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  19 KVHHTAYVHPTAVlIGdvrvcENVMICPNVVlradegltiiIGAGVNIQDGVIM--HCLKGGSIEIGQDCSIahcalvHG 96
Cdd:cd03351    1 MIHPTAIVDPGAK-IG-----ENVEIGPFCV----------IGPNVEIGDGTVIgsHVVIDGPTTIGKNNRI------FP 58


                 ....*
gi 499779248  97 PAVIG 101
Cdd:cd03351   59 FASIG 63
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 19-108 4.31e-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: 36.62  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  19 KVHHTAYVHPTAVLIGDVRVCENVMICPNVVLRADegltIIIGAGVNIQDGVImhclkggsieIGQDCSIAHCALVHGPA 98
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDG----VVIGDDCVIHPNVT----------IYEGCIIGDRVIIHSGA 68

                         90
                 ....*....|
gi 499779248  99 VIGRETFvGF 108
Cdd:cd03352   69 VIGSDGF-GF 77
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 18-118 4.71e-03

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 36.53  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  18 PKVHHTAYVHPTAVlIGDvrvceNVMICPNVVlradegltiiIGAGVniqdgvimhclkggsiEIGQDCSIAHCALVHGP 97
Cdd:COG1043    2 AMIHPTAIVDPGAK-LGE-----NVEIGPFCV----------IGPDV----------------EIGDGTVIGSHVVIEGP 49

                         90       100
                 ....*....|....*....|.
gi 499779248  98 AVIGRETFVGfraivHNATLG 118
Cdd:COG1043   50 TTIGKNNRIF-----PFASIG 65
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 58-164 6.49e-03

Dynactin 5 (or subunit p25); 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 p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain 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: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 35.65  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  58 IIIGAGVNIQDGVImhcLKG--GSIEIGQDCSIAHCALV------------HGPAVIGRETFVGFRAIVHNATLG----- 118
Cdd:cd03359   22 IVLNGKTIIQSDVI---IRGdlATVSIGRYCILSEGCVIrppfkkfskgvaFFPLHIGDYVFIGENCVVNAAQIGsyvhi 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499779248 119 -KNSFISHGAMVL-NVELPDDSSVPVGKIIQSEAEVRELPAIVVQEIS 164
Cdd:cd03359   99 gKNCVIGRRCIIKdCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELP 146
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 35-118 9.25e-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: 35.46  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499779248  35 DVRVCENVMICPNVVLRADegltIIIGAGVNIQDGVImhclkggsieIGQDCSIAHCALVHGPAVIGRETFVGFRAIVH- 113
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEG----VVIGDGVVIGPGVV----------IGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHs 66


                 ....*
gi 499779248 114 NATLG 118
Cdd:cd03352   67 GAVIG 71
 
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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