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Conserved domains on  [gi|695764928|ref|WP_032687964|]
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MULTISPECIES: phenylacetic acid degradation protein PaaY [Raoultella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaY super family cl31188
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
 3-195 8.16e-122

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]


The actual alignment was detected with superfamily member TIGR02287:

Pssm-ID: 131340 [Multi-domain]  Cd Length: 192  Bit Score: 342.25  E-value: 8.16e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928    3 IYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGH 82
Cdd:TIGR02287   1 CYQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDTVVEENGHVGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   83 GAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVL 162
Cdd:TIGR02287  81 GAILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIRELSEQELAWKKQGTHEYQVL 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 695764928  163 VERCKQSLHQVEPLKEAEPERKRLEfDENLRPK 195
Cdd:TIGR02287 161 ATRCKQTLHQCEPLREAEPGRPRMV-DENVRPK 192
 
Name Accession Description Interval E-value
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
 3-195 8.16e-122

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: 342.25  E-value: 8.16e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928    3 IYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGH 82
Cdd:TIGR02287   1 CYQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDTVVEENGHVGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   83 GAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVL 162
Cdd:TIGR02287  81 GAILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIRELSEQELAWKKQGTHEYQVL 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 695764928  163 VERCKQSLHQVEPLKEAEPERKRLEfDENLRPK 195
Cdd:TIGR02287 161 ATRCKQTLHQCEPLREAEPGRPRMV-DENVRPK 192
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-165 9.11e-101

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: 287.73  E-value: 9.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  11 PVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGHGAILHGCV 90
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695764928  91 IGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVLVER 165
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQLAAR 155
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 1-196 3.01e-99

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 285.55  E-value: 3.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   1 MPIYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHI 80
Cdd:PRK13627   1 MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  81 GHGAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQ 160
Cdd:PRK13627  81 GHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 695764928 161 VLVERCKQSLHQVEPLKEAEPERKRLEFDENLRPKS 196
Cdd:PRK13627 161 DLVGRCHASLHETQPLRQMEENRPRLQGTTDVTPKR 196
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-170 4.80e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.41  E-value: 4.80e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   1 MPIYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHI 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  81 GHGAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQ 160
Cdd:COG0663   81 GHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYV 160

                        170
                 ....*....|
gi 695764928 161 VLVERCKQSL 170
Cdd:COG0663  161 ELARRYLAEL 170
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
88-117 2.41e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.63  E-value: 2.41e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 695764928   88 GCVIGRNALVGMSAVIIDGATIGENSIVGA 117
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
 3-195 8.16e-122

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: 342.25  E-value: 8.16e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928    3 IYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGH 82
Cdd:TIGR02287   1 CYQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDTVVEENGHVGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   83 GAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVL 162
Cdd:TIGR02287  81 GAILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIRELSEQELAWKKQGTHEYQVL 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 695764928  163 VERCKQSLHQVEPLKEAEPERKRLEfDENLRPK 195
Cdd:TIGR02287 161 ATRCKQTLHQCEPLREAEPGRPRMV-DENVRPK 192
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-165 9.11e-101

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: 287.73  E-value: 9.11e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  11 PVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGHGAILHGCV 90
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695764928  91 IGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVLVER 165
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQLAAR 155
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 1-196 3.01e-99

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 285.55  E-value: 3.01e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   1 MPIYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHI 80
Cdd:PRK13627   1 MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  81 GHGAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQ 160
Cdd:PRK13627  81 GHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQ 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 695764928 161 VLVERCKQSLHQVEPLKEAEPERKRLEFDENLRPKS 196
Cdd:PRK13627 161 DLVGRCHASLHETQPLRQMEENRPRLQGTTDVTPKR 196
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-170 4.80e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.41  E-value: 4.80e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   1 MPIYQIDGMTPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHI 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  81 GHGAILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQ 160
Cdd:COG0663   81 GHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYV 160

                        170
                 ....*....|
gi 695764928 161 VLVERCKQSL 170
Cdd:COG0663  161 ELARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-162 1.53e-62

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: 190.70  E-value: 1.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  12 VVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGHGAILHGCVI 91
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695764928  92 GRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVL 162
Cdd:cd04645   81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVEL 151
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 11-159 6.61e-39

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: 130.77  E-value: 6.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  11 PVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGHGAILHGCV 90
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695764928  91 IGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREY 159
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEY 149
PLN02296 PLN02296
carbonate dehydratase
 10-195 1.56e-36

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 128.32  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  10 TPVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMH----GFPGQ--DTVVEEDGHIGHG 83
Cdd:PLN02296  52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvaktNLSGKvlPTIIGDNVTIGHS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  84 AILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQVLV 163
Cdd:PLN02296 132 AVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLA 211

                        170       180       190
                 ....*....|....*....|....*....|..
gi 695764928 164 ErckqsLHQVEPLKEAEperkRLEFDENLRPK 195
Cdd:PLN02296 212 Q-----VHAAENAKSFD----EIEFEKVLRKK 234
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 11-122 6.94e-31

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: 110.41  E-value: 6.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  11 PVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGR-IVVKDGANIQDNCVMHGFPGQDTVVEEDGHIGHGAILHG- 88
Cdd:cd00710    3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTpIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVHGp 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 695764928  89 CVIGRNALVGMSAVIIDgATIGENSIVGASAFVK 122
Cdd:cd00710   83 AYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVVD 115
PLN02472 PLN02472
uncharacterized protein
 11-149 3.11e-23

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 92.72  E-value: 3.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  11 PVVPDESYVHPTAVLIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVMH-------GFPGqDTVVEEDGHIGHG 83
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHaawnsptGLPA-ETLIDRYVTIGAY 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695764928  84 AILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEI 149
Cdd:PLN02472 139 SLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEET 204
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
15-149 9.81e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 83.38  E-value: 9.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  15 DESYVHPTAVL-IGDVILGKGVYVGPNASLrGDFGRIVVKDGANIQDNCVM----HGFPGQDTVVEEDGHIghgailhgc 89
Cdd:COG0110   13 DGVVIGPGVRIyGGNITIGDNVYIGPGVTI-DDPGGITIGDNVLIGPGVTIltgnHPIDDPATFPLRTGPV--------- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  90 VIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIRTLSEQEI 149
Cdd:COG0110   83 TIGDDVWIGAGATILPGVTIGDGAVVGAGSVV--TKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 17-138 2.91e-19

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: 81.39  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   17 SYVHPTAVLIGDVILGKGVYVGPNASLRGDfgrIVVKDGANIQDNCVMhgfpGQDTVVEEDGHIGHGAILHGCV-IGRNA 95
Cdd:TIGR03570  88 TLIHPSAIVSPSASIGEGTVIMAGAVINPD---VRIGDNVIINTGAIV----EHDCVIGDFVHIAPGVTLSGGVvIGEGV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 695764928   96 LVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPA 138
Cdd:TIGR03570 161 FIGAGATIIQGVTIGAGAIVGAGAVV--TKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 17-137 3.11e-18

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: 78.30  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  17 SYVHPTAVLIGDVILGKGVYVGPNASLRGDfgrIVVKDGANIQDNC-VMHgfpgqDTVVEEDGHIGHGAILHG-CVIGRN 94
Cdd:cd03360   85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPD---ARIGDNVIINTGAvIGH-----DCVIGDFVHIAPGVVLSGgVTIGEG 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 695764928  95 ALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSP 137
Cdd:cd03360  157 AFIGAGATIIQGVTIGAGAIIGAGAVV--TKDVPDGSVVVGNP 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 28-141 1.27e-15

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: 69.41  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  28 DVILGKGVYVGPNASLrGDFGRIVVKDGANIQDNCVM--HGFPGQDTVVEEDGHIGHGAIlhgcVIGRNALVGMSAVIID 105
Cdd:cd04647    1 NISIGDNVYIGPGCVI-SAGGGITIGDNVLIGPNVTIydHNHDIDDPERPIEQGVTSAPI----VIGDDVWIGANVVILP 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 695764928 106 GATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAI 141
Cdd:cd04647   76 GVTIGDGAVVGAGSVV--TKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 26-142 1.48e-11

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 59.05  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  26 IGD-VILGKGVYVGPNAslrgdfgriVVKDGANIQDNCvmhgFPGQDTVVEEDGHIGHGAI----------------LHG 88
Cdd:cd03358    1 IGDnCIIGTNVFIENDV---------KIGDNVKIQSNV----SIYEGVTIEDDVFIGPNVVftndlyprskiyrkweLKG 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695764928  89 CVIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIR 142
Cdd:cd03358   68 TTVKRGASIGANATILPGVTIGEYALVGAGAVV--TKDVPPYALVVGNPARIIG 119
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 29-121 2.43e-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: 54.56  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  29 VILGKGVYVGPNASLRGdfgRIVVKDGANIQDNCVMHGFPG----QDTVVEEDGHIGHGAILHGCVigrnalvgmsavii 104
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG---PVVIGDNVNIGPGAVIGAATGpnekNPTIIGDNVEIGANAVIHGGV-------------- 63

                         90
                 ....*....|....*..
gi 695764928 105 dgaTIGENSIVGASAFV 121
Cdd:cd00208   64 ---KIGDNAVIGAGAVV 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 19-103 3.17e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 58.23  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVMHG--FPGQDTVVEEDGHIGHGA-ILHGCVIGRNA 95
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNA---------VIGAGVVIGDGVVIGAgaVIGDGVKIGADCRLHANVtIYHAVRIGNRV 173


                 ....*...
gi 695764928  96 LVGMSAVI 103
Cdd:PRK00892 174 IIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 19-119 1.99e-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: 55.79  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVmhgfpgqdtvveedghIGHGA-ILHGCVIGRNALV 97
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFA---------VIGAGVVIGDGVV----------------IGPGVvIGDGVVIGDDCVL 153

                         90       100
                 ....*....|....*....|..
gi 695764928  98 GMSAVIIDGATIGENSIVGASA 119
Cdd:COG1044  154 HPNVTIYERCVIGDRVIIHSGA 175
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 90-141 3.38e-09

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 53.58  E-value: 3.38e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695764928  90 VIGRNALVGMSAVIIDGATIGENSIVGASAFVkAKaEMPANHLIVGSPAKAI 141
Cdd:cd03357  120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVV-TK-DIPANVVAAGNPARVI 169
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 17-103 1.06e-08

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: 50.33  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  17 SYVHPTAVLIGDVILGKGVYVGPNASLRGdfgrivvkdganiqdncVMHGFPGQDTVVEEDGHIGHGA-ILHGCVIGRNA 95
Cdd:cd00208    7 VKIHPKAVIRGPVVIGDNVNIGPGAVIGA-----------------ATGPNEKNPTIIGDNVEIGANAvIHGGVKIGDNA 69


                 ....*...
gi 695764928  96 LVGMSAVI 103
Cdd:cd00208   70 VIGAGAVV 77
PLN02739 PLN02739
serine acetyltransferase
 19-159 1.15e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 53.89  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAvLIGDVIL---GKGVYVGPNAslrgdfgriVVKDGANIQDNCVMHGfPGQDTvveEDGH--IGHGAILHGCVigr 93
Cdd:PLN02739 208 IHPAA-RIGKGILldhGTGVVIGETA---------VIGDRVSILHGVTLGG-TGKET---GDRHpkIGDGALLGACV--- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695764928  94 nalvgmsaVIIDGATIGENSIVGASAFVKAkaEMPANHLIVGSPAKAIRTLSEQE--IAWKKQGTREY 159
Cdd:PLN02739 271 --------TILGNISIGAGAMVAAGSLVLK--DVPSHSMVAGNPAKLIGFVDEQDpsLTMEYDATREF 328
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 17-103 1.06e-07

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: 50.79  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  17 SYVHPTAVLIGDVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVMhgfpGQDTVVEEDGHIGHGA-ILHGCVIGRNA 95
Cdd:COG1044  103 AVIDPSAKIGEGVSIGPFAVIGAGV---------VIGDGVVIGPGVVI----GDGVVIGDDCVLHPNVtIYERCVIGDRV 169


                 ....*...
gi 695764928  96 LVGMSAVI 103
Cdd:COG1044  170 IIHSGAVI 177
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 32-148 1.42e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 49.62  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  32 GKGVYVGPNasLRGDFGRIVVKD-GANIQDNCVMhgfpGQDTVVEEDGHIGHGAI-LHG------CVIGRNALVGMSAVI 103
Cdd:PRK09527  73 GSNIHIGRN--FYANFNLTIVDDyTVTIGDNVLI----APNVTLSVTGHPVHHELrKNGemysfpITIGNNVWIGSHVVI 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695764928 104 IDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIRTLSEQE 148
Cdd:PRK09527 147 NPGVTIGDNSVIGAGSVV--TKDIPPNVVAAGVPCRVIREINDRD 189
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 18-92 2.42e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  18 YVHPTAVLIGDVILGKGVYVGPNASLrGDFGRI----VVKDGANIQDNCVMHgfPGqdTVVEEDGHIGHGAILH-GCVIG 92
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVI-GDGVVIgagaVIGDGVKIGADCRLH--AN--VTIYHAVRIGNRVIIHsGAVIG 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 15-142 3.05e-07

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: 48.56  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  15 DESYVHPTAVLIGDVILGKGVYVGPNASLRGD----------------FGRIVVKDGANIQDNCVMHGFPGQDTVVEEDG 78
Cdd:cd03352   42 DDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDgfgfapdgggwvkipqLGGVIIGDDVEIGANTTIDRGALGDTVIGDGT 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  79 ------HIGHGA------ILHGCV-------IGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAK 139
Cdd:cd03352  122 kidnlvQIAHNVrigencLIAAQVgiagsttIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGV--TSIVPPGEYVSGTPAQ 199


                 ...
gi 695764928 140 AIR 142
Cdd:cd03352  200 PHR 202
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 69-143 3.65e-07

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 48.16  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  69 GQDTVVEEDGHIGHGAILHGC---------VIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAK 139
Cdd:COG1045   89 GETAVIGDNVTIYQGVTLGGTgkekgkrhpTIGDNVVIGAGAKILGPITIGDNAKIGANSVV--LKDVPPGSTVVGVPAR 166


                 ....
gi 695764928 140 AIRT 143
Cdd:COG1045  167 IVKR 170
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 28-119 6.16e-07

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: 47.79  E-value: 6.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  28 DVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVmhgfpgqdtvveedghIGHGA-ILHGCVIGRNALVGMSAVIIDG 106
Cdd:cd03352    1 SAKIGENVSIGPNA---------VIGEGVVIGDGVV----------------IGPGVvIGDGVVIGDDCVIHPNVTIYEG 55

                         90
                 ....*....|...
gi 695764928 107 ATIGENSIVGASA 119
Cdd:cd03352   56 CIIGDRVIIHSGA 68
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 19-116 6.51e-07

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: 47.41  E-value: 6.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNASLRGDfgriVVKDGANIQDNCVMHGfpgqdTVVEEDGHIGHGAILH-GCVIGRNALV 97
Cdd:cd03353   24 IDPGVILEGKTVIGEDCVIGPNCVIKDS----TIGDGVVIKASSVIEG-----AVIGNGATVGPFAHLRpGTVLGEGVHI 94

                         90
                 ....*....|....*....
gi 695764928  98 GmSAVIIDGATIGENSIVG 116
Cdd:cd03353   95 G-NFVEIKKSTIGEGSKAN 112
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 91-144 7.70e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 47.50  E-value: 7.70e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695764928  91 IGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIRTL 144
Cdd:PRK10092 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVV--TKDVPDNVVVGGNPARIIKKL 183
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 90-152 7.78e-07

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 47.56  E-value: 7.78e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695764928  90 VIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIRTLSEQEIAWK 152
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVV--TKSIPENTVIAGNPAKIIKKYNHETKLWE 192
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 69-137 8.12e-07

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 45.51  E-value: 8.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  69 GQDTVVEEDGHIGHGA-ILHGC--------------VIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLI 133
Cdd:cd03354   20 GTGIVIGETAVIGDNCtIYQGVtlggkgkgggkrhpTIGDNVVIGAGAKILGNITIGDNVKIGANAVV--TKDVPANSTV 97


                 ....
gi 695764928 134 VGSP 137
Cdd:cd03354   98 VGVP 101
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 21-132 1.57e-06

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: 46.64  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  21 PTAVLI-GDVILGKGVYVGPNASLRgdfGRIVVKDGANIQDNCVMhgfpgQDTVVEEDGHIGHGAILHGCVIGRNALVGM 99
Cdd:cd03353    7 PETTYIdGDVEIGVDVVIDPGVILE---GKTVIGEDCVIGPNCVI-----KDSTIGDGVVIKASSVIEGAVIGNGATVGP 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695764928 100 SAVIIDGATIGENSIVGasAFVKAK-----AEMPANHL 132
Cdd:cd03353   79 FAHLRPGTVLGEGVHIG--NFVEIKkstigEGSKANHL 114
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 27-116 8.12e-06

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: 45.40  E-value: 8.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  27 GDVILGKGVYVGPNASLRGdfgrivvkdganiqdncvmhgfpgqDTVVEEDGHIGHGAILHGCVIGRNALVGMSavIIDG 106
Cdd:COG1207  265 GDVEIGRDVVIDPNVILEG-------------------------KTVIGEGVVIGPNCTLKDSTIGDGVVIKYS--VIED 317

                         90
                 ....*....|
gi 695764928 107 ATIGENSIVG 116
Cdd:COG1207  318 AVVGAGATVG 327
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 12-92 1.31e-05

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: 43.94  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  12 VVPDESYVHPTAVLIGDVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVMHgfPGqdTVVEEDGHIGHGAILH-GCV 90
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGV---------VIGDGVVIGDDCVIH--PN--VTIYEGCIIGDRVIIHsGAV 69


                 ..
gi 695764928  91 IG 92
Cdd:cd03352   70 IG 71
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 10-154 1.32e-05

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: 44.62  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  10 TPVVPDESYVHPTAVL-----IGD-VILGKGVYVGPNASLrGDFGRI----VVKDGANIQDNCVMH--------GF---P 68
Cdd:COG1044  108 SAKIGEGVSIGPFAVIgagvvIGDgVVIGPGVVIGDGVVI-GDDCVLhpnvTIYERCVIGDRVIIHsgavigadGFgfaP 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  69 GQD----------TVVEEDG-----------------HIGHGAIL-------HGCVIGRN----ALVGMS---------- 100
Cdd:COG1044  187 DEDggwvkipqlgRVVIGDDveiganttidrgalgdtVIGDGTKIdnlvqiaHNVRIGEHtaiaAQVGIAgstkigdnvv 266

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695764928 101 ----AVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAIRTlseqeiaWKKQ 154
Cdd:COG1044  267 iggqVGIAGHLTIGDGVIIGAQSGV--TKSIPEGGVYSGSPAQPHRE-------WLRN 315
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-132 1.74e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.47  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   7 DGMTPVVPDesyvhpTAVLIGDVILGKGVYVGPNaslrgdfgrIVVKDGANIQDNCVMHGFpgqdtvveedghiGHgaiL 86
Cdd:PRK14353 253 AGVTLIAPE------TVFFSYDTVIGRDVVIEPN---------VVFGPGVTVASGAVIHAF-------------SH---L 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 695764928  87 HGCVIGRNALVGMSAVIIDGATIGENSIVGasAFVKAK-AEM----PANHL 132
Cdd:PRK14353 302 EGAHVGEGAEVGPYARLRPGAELGEGAKVG--NFVEVKnAKLgegaKVNHL 350
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
88-117 2.41e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.63  E-value: 2.41e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 695764928   88 GCVIGRNALVGMSAVIIDGATIGENSIVGA 117
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 19-117 2.75e-05

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: 43.86  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNASLRGdfgrIVVKDGANIQdNCVMHgfpgqDTVVEEDGHIGHGAILH-GCVIGRNALV 97
Cdd:COG1207  275 IDPNVILEGKTVIGEGVVIGPNCTLKD----STIGDGVVIK-YSVIE-----DAVVGAGATVGPFARLRpGTVLGEGVKI 344

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 695764928  98 G-----MSAVIIDG-----------ATIGENSIVGA 117
Cdd:COG1207  345 GnfvevKNSTIGEGskvnhlsyigdAEIGEGVNIGA 380
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 90-141 5.66e-05

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 40.67  E-value: 5.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695764928  90 VIGRNALVGMSAVIIDGATIGENSIVGASAFVkaKAEMPANHLIVGSPAKAI 141
Cdd:cd05825   58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVV--VRDLPAWTVYAGNPAVPV 107
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 19-122 5.97e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.80  E-value: 5.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNASLRGDfgrIVVKDGANIQDNC------VMHG-------FPGqDTVVEEDGHIGHGAI 85
Cdd:cd05636   26 VRSGAYIEGPVIIGKGCEIGPNAYIRGY---TVLGDGCVVGNSVevknsiIMDGtkvphlnYVG-DSVLGENVNLGAGTI 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695764928  86 LH-------------------------GCVIGRNALVGMSAVIIDGATIGENSIVGASAFVK 122
Cdd:cd05636  102 TAnlrfddkpvkvrlkgervdtgrrklGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 71-142 6.96e-05

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: 42.82  E-value: 6.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695764928   71 DTVVEEDGHIGHGAILHG-CVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIR 142
Cdd:TIGR02353 383 DGLLMGNARLSGGWFRLGrTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKVREGVGWLGSPPFELP 455
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 29-160 7.32e-05

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: 41.43  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  29 VILGKGVyVGPNASLRGDFGRI------VVKDGANIQDNCVM--HGFPGQDTVVEEDGHIGHGAILHGCVIGRNALVGMS 100
Cdd:cd03359   23 VLNGKTI-IQSDVIIRGDLATVsigrycILSEGCVIRPPFKKfsKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKN 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928 101 AVIIDGATIGENSIVGASAFVKAKAEMPANHLIVGSPAKAIRTLSEQEIAWKKQGTREYQ 160
Cdd:cd03359  102 CVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEEETKEYY 161
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 17-142 2.30e-04

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 39.83  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  17 SYVHP--TAVLIGDVILGKGVYVGPNAslrgdfgRIVVkdGANIQDNCV-MHGFPGQDTVVEEDGHIGHGAILHGCVIGR 93
Cdd:cd03349    8 SYGSGpdCDVGGDKLSIGKFCSIAPGV-------KIGL--GGNHPTDWVsTYPFYIFGGEWEDDAKFDDWPSKGDVIIGN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 695764928  94 NALVGMSAVIIDGATIGENSIVGASAFVkAKaEMPANHLIVGSPAKAIR 142
Cdd:cd03349   79 DVWIGHGATILPGVTIGDGAVIAAGAVV-TK-DVPPYAIVGGNPAKVIR 125
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 55-141 2.34e-04

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: 41.27  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   55 GANIQDNCVMHGFP---------GQDTVVEED----GHIGHGAILH-GCV-IGRNALVGMSAVIIDGATIGENSIVGASA 119
Cdd:TIGR02353 112 GAKIGKGVDIGSLPpvctdlltiGAGTIVRKEvmllGYRAERGRLHtGPVtLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|..
gi 695764928  120 FVKAKAEMPANHLIVGSPAKAI 141
Cdd:TIGR02353 192 ALQGGQSIPDGERWHGSPAQKT 213
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 26-142 3.54e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  26 IGDVILGKGVYVGPNASL-RGDFGRIVVKDGANIqDNCVM--HGfpgqdtvVeedgHIGHGAILHGCV-------IGRNA 95
Cdd:PRK00892 201 LGRVIIGDDVEIGANTTIdRGALDDTVIGEGVKI-DNLVQiaHN-------V----VIGRHTAIAAQVgiagstkIGRYC 268

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 695764928  96 LVGMSAVIIDGATIGENSIVGASAFVKAKAEmPANHLIVGSPAKAIR 142
Cdd:PRK00892 269 MIGGQVGIAGHLEIGDGVTITAMSGVTKSIP-EPGEYSSGIPAQPNK 314
PRK10502 PRK10502
putative acyl transferase; Provisional
 90-148 3.94e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.55  E-value: 3.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695764928  90 VIGRNALVGMSAVIIDGATIGENSIVGA--SAFvkakAEMPANHLIVGSPAKAIRTLSEQE 148
Cdd:PRK10502 126 VIGEGCWLAADVFVAPGVTIGSGAVVGArsSVF----KSLPANTICRGNPAVPIRPRVETE 182
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 15-121 6.78e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.24  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  15 DESYVHPTAVLIGDVILGKGVYVGPNASL---------RGDFGRIVVKDGANIQDNCVMH--GFPGQDTvveedgHIGHG 83
Cdd:PRK12461  34 DGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHrgTKGGGVT------RIGND 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 695764928  84 AIL-------HGCVIGRNALVGMSAVIIDGATIGENSIVGASAFV 121
Cdd:PRK12461 108 NLLmayshvaHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLV 152
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 30-111 8.47e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.79  E-value: 8.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  30 ILGKGVYVGPNASLRGDfgriVVKDGANIQDNCVMHG-FPGQDTVVEEDGHIGHGAILHGCVIGRNALVGMSAVIIDGAT 108
Cdd:cd05787    1 VIGRGTSIGEGTTIKNS----VIGRNCKIGKNVVIDNsYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVV 76


                 ...
gi 695764928 109 IGE 111
Cdd:cd05787   77 IGD 79
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
15-121 8.88e-04

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.93  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  15 DESYVHPTAVLIGDVILGKGVYVGPNASL---------RGDFGRIVVKDGANIQDNCVMHGFPGQD---TVVEEDG---- 78
Cdd:PRK05289  37 DGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkyKGEPTRLVIGDNNTIREFVTINRGTVQGggvTRIGDNNllma 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695764928  79 --HIGHGAILH-GCVIGRNALVGMSAVIIDGATIGENS------IVGASAFV 121
Cdd:PRK05289 117 yvHVAHDCVVGnHVILANNATLAGHVEVGDYAIIGGLTavhqfvRIGAHAMV 168
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 36-118 1.47e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 38.70  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  36 YVGPNASlrgdfgrivVKDgANIQDNCVMHG-------FPG---------QDTVVEEDGHIGHGAILHGCVIGRNALVGM 99
Cdd:PRK05293 284 YIAENAK---------VKN-SLVVEGCVVYGtvehsvlFQGvqvgegsvvKDSVIMPGAKIGENVVIERAIIGENAVIGD 353

                         90       100
                 ....*....|....*....|...
gi 695764928 100 SAVIIDG----ATIGENSIVGAS 118
Cdd:PRK05293 354 GVIIGGGkeviTVIGENEVIGVG 376
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 21-132 1.70e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 38.42  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  21 PTAVLIGD-VILGKGVYVGPNASLRGdfgRIVVKDGANIQDNCVMhgfpgQDTVVEEDGHIGHGAILHGCVIGRNALVGM 99
Cdd:PRK14358 262 PGTILIEDtVTLGRDVTIEPGVLLRG---QTRVADGVTIGAYSVV-----TDSVLHEGAVIKPHSVLEGAEVGAGSDVGP 333

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 695764928 100 SAVIIDGATIGENSIVGasAFVKAK-----AEMPANHL 132
Cdd:PRK14358 334 FARLRPGTVLGEGVHIG--NFVETKnarldAGVKAGHL 369
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 73-125 1.75e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 1.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 695764928  73 VVEEDGHIGHGA-ILHGCVIGRNALVGMSAVIIDGATIGENSIVGASAFVKAKA 125
Cdd:PRK00892 108 VIDPSAKIGEGVsIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANV 161
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 15-121 2.27e-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: 37.80  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  15 DESYVHPTAVLIGDVILGKGVYVGPNASL---------RGDFGRIVVKDGANIQDNCVMHGFPGQD---TVVEEDG---- 78
Cdd:cd03351   34 DGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkyKGEPTRLEIGDNNTIREFVTIHRGTAQGggvTRIGNNNllma 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 695764928  79 --HIGHGAIL-HGCVIGRNALVGMSAVIIDGATIGENS------IVGASAFV 121
Cdd:cd03351  114 yvHVAHDCVIgNNVILANNATLAGHVEIGDYAIIGGLSavhqfcRIGRHAMV 165
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 73-121 2.77e-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: 37.39  E-value: 2.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 695764928  73 VVEEDGHIGHGAILH-GCVIGRNALVGMSAVIIDGATIGENSIVGASAFV 121
Cdd:cd03352    3 KIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 20-112 3.36e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 37.50  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  20 HPTAVLIGDVILGKGVYVGpNASLRGDF--GRIVVKDGANIQDNCVMhgfpgqdtvveEDGHIGHGAILHGCVIGRNalv 97
Cdd:PRK00844 307 GGRVGSAQDSLVSAGSIIS-GATVRNSVlsPNVVVESGAEVEDSVLM-----------DGVRIGRGAVVRRAILDKN--- 371

                         90
                 ....*....|....*
gi 695764928  98 gmsAVIIDGATIGEN 112
Cdd:PRK00844 372 ---VVVPPGATIGVD 383
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 79-133 3.78e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.86  E-value: 3.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695764928  79 HIGHGAILHGCVIGRNALVG-----MSAVIIDGATIGEN-----SIVGASAFVKAKAEMPANHLI 133
Cdd:cd05787    7 SIGEGTTIKNSVIGRNCKIGknvviDNSYIWDDVTIEDGctihhSIVADGAVIGKGCTIPPGSLI 71
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-124 4.50e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.22  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  28 DVILGKGVYVGPNASLRGdfgRIVVKDGANIQDNCVMhgfpgQDTVVEEDGHI--GHGAilhGCVIGRNALVGMSAVIID 105
Cdd:PRK14352 271 DVTIGRDVVIHPGTQLLG---RTTIGEDAVVGPDTTL-----TDVTVGEGASVvrTHGS---ESEIGAGATVGPFTYLRP 339

                         90
                 ....*....|....*....
gi 695764928 106 GATIGENSIVGasAFVKAK 124
Cdd:PRK14352 340 GTVLGEEGKLG--AFVETK 356
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 19-117 4.85e-03

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: 36.15  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAV------LIGDVILGKGVYVGPNASLRGDFGRIVVKDGANIQDNCVM-HGFPgQDTVVEEDGHIGHGAILH-GCV 90
Cdd:cd04646    2 IAPGAVvcqeseIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIvNKKP-KDPAEPKPMIIGSNNVFEvGCK 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 695764928  91 -----IGRNALVGMSAVIIDGATIGENSIVGA 117
Cdd:cd04646   81 cealkIGNNNVFESKSFVGKNVIITDGCIIGA 112
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-135 6.11e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   6 IDGMTPVVPDESYVHPtavligDVILGKGVYVGPNASLRGDfgrivvkdgANIQDNCVmhgfpgqdtvveedghIGHGAI 85
Cdd:PRK14355 252 LAGVTLIDPETTYIDR------GVVIGRDTTIYPGVCISGD---------TRIGEGCT----------------IEQGVV 300

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 695764928  86 LHGCVIGRNALVGMSAVIIDgATIGENSIVGASAFVKAKAEMPAnHLIVG 135
Cdd:PRK14355 301 IKGCRIGDDVTVKAGSVLED-SVVGDDVAIGPMAHLRPGTELSA-HVKIG 348
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 80-117 7.01e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 36.76  E-value: 7.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 695764928  80 IGHGAILHGCVIgRNALVGMSAVIIDGATIGENSIVGA 117
Cdd:PLN02241 318 ISHGCFLRECKI-EHSVVGLRSRIGEGVEIEDTVMMGA 354
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 31-138 7.20e-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: 36.65  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928   31 LGKGVYVGPNASLRGDFGRIvvKDGANIQDNCVM--HGFpgQDTVVEEDGhighgailhgCVIGRNALVGMSAVIIDGAT 108
Cdd:TIGR02353 600 IGRGVYIDGTDLTERDLVTI--GDDSTLNEGSVIqtHLF--EDRVMKSDT----------VTIGDGATLGPGAIVLYGVV 665

                          90       100       110
                  ....*....|....*....|....*....|
gi 695764928  109 IGENSIVGASAFVKAKAEMPANHLIVGSPA 138
Cdd:TIGR02353 666 MGEGSVLGPDSLVMKGEEVPAHTRWRGNPA 695
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 19-103 7.79e-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: 36.26  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  19 VHPTAVLIGDVILGKGVYVGPNAslrgdfgriVVKDGANIQDNCVmhgfpgqdtvveedghIGHGAILHGC-VIGRNALV 97
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFC---------VIGPNVEIGDGTV----------------IGSHVVIDGPtTIGKNNRI 56


                 ....*.
gi 695764928  98 GMSAVI 103
Cdd:cd03351   57 FPFASI 62
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 69-136 7.93e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.14  E-value: 7.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695764928  69 GQDTVVEEDGHIGHGAILHGCVIGRNALVGMSaVIIDGATIGEN-----SIVGASAFVKAKAEMpANHLIVGS 136
Cdd:cd03356    3 GESTVIGENAIIKNSVIGDNVRIGDGVTITNS-ILMDNVTIGANsvivdSIIGDNAVIGENVRV-VNLCIIGD 73
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 30-121 8.83e-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: 35.05  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695764928  30 ILGKGVYVGPNASL-RGDFGRI--VVKDGANIqDNCVMHGFPGQdtvVEEDGHIGHGAILHG---------CVIGRNALV 97
Cdd:cd03350    9 IIRDGAFIGPGAVLmMPSYVNIgaYVDEGTMV-DSWATVGSCAQ---IGKNVHLSAGAVIGGvleplqatpVIIEDDVFI 84

                         90       100
                 ....*....|....*....|....
gi 695764928  98 GMSAVIIDGATIGENSIVGASAFV 121
Cdd:cd03350   85 GANCEVVEGVIVGKGAVLAAGVVL 108
 
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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