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Conserved domains on  [gi|15598948|ref|NP_252442|]
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hypothetical protein PA3753 [Pseudomonas aeruginosa PAO1]

Protein Classification

gamma carbonic anhydrase family protein( domain architecture ID 11429531)

gamma carbonic anhydrase family protein is a hexapeptide repeat protein similar to carnitine operon protein CaiE and phenylacetic acid degradation protein PaaY, which are involved in amine/polyamine and aromatic compound metabolism, respectively

CATH:  2.160.10.10
EC:  4.2.1.-
Gene Ontology:  GO:0046872
PubMed:  15500694|11747907|11696553|10611359
SCOP:  4002848

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-169 1.08e-95

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 274.21  E-value: 1.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   1 MKYRLGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVG 80
Cdd:COG0663   2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  81 HNAMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVH 160
Cdd:COG0663  82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                ....*....
gi 15598948 161 NARRYARDL 169
Cdd:COG0663 162 LARRYLAEL 170
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-169 1.08e-95

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 274.21  E-value: 1.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   1 MKYRLGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVG 80
Cdd:COG0663   2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  81 HNAMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVH 160
Cdd:COG0663  82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                ....*....
gi 15598948 161 NARRYARDL 169
Cdd:COG0663 162 LARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 11-163 5.31e-88

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: 254.26  E-value: 5.31e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  11 ETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHGCSV 90
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598948  91 GDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNAR 163
Cdd:cd04645  81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 13-166 6.34e-42

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 141.03  E-value: 6.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMH---TDMG---YPLTLGKGVTVGHNAMLH 86
Cdd:PLN02296  56 DKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvakTNLSgkvLPTIIGDNVTIGHSAVLH 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   87 GCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNARRYA 166
Cdd:PLN02296 136 GCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHA 215
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
 3-173 5.57e-37

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: 126.15  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948     3 YRLGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHN 82
Cdd:TIGR02287   2 YQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDTVVEENGHVGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    83 AMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNA 162
Cdd:TIGR02287  82 AILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIRELSEQELAWKKQGTHEYQVLA 161

                         170
                  ....*....|.
gi 15598948   163 RRYARDLVEDP 173
Cdd:TIGR02287 162 TRCKQTLHQCE 172
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
87-116 1.72e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 15598948    87 GCSVGDYSLVGINAVILNGAKIGKYCIIGA 116
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-169 1.08e-95

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 274.21  E-value: 1.08e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   1 MKYRLGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVG 80
Cdd:COG0663   2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  81 HNAMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVH 160
Cdd:COG0663  82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                ....*....
gi 15598948 161 NARRYARDL 169
Cdd:COG0663 162 LARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 11-163 5.31e-88

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: 254.26  E-value: 5.31e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  11 ETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHGCSV 90
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598948  91 GDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNAR 163
Cdd:cd04645  81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 13-163 3.17e-55

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: 171.21  E-value: 3.17e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHGCSVGD 92
Cdd:cd04650   4 SPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAKVGN 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948  93 YSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNAR 163
Cdd:cd04650  84 YVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 13-145 4.77e-42

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: 137.88  E-value: 4.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHGCSVGD 92
Cdd:cd04745   4 DPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCTIGR 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598948  93 YSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSE 145
Cdd:cd04745  84 NALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSD 136
PLN02296 PLN02296
carbonate dehydratase
 13-166 6.34e-42

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 141.03  E-value: 6.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMH---TDMG---YPLTLGKGVTVGHNAMLH 86
Cdd:PLN02296  56 DKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvakTNLSgkvLPTIIGDNVTIGHSAVLH 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   87 GCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNARRYA 166
Cdd:PLN02296 136 GCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHA 215
PaaY TIGR02287
phenylacetic acid degradation protein PaaY; Members of this family are located next to other ...
 3-173 5.57e-37

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: 126.15  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948     3 YRLGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHN 82
Cdd:TIGR02287   2 YQIDGLTPVVHPEAYVHPTAVLIGDVILGKRCYVGPLASLRGDFGRIVLKEGANIQDNCVMHGFPGQDTVVEENGHVGHG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    83 AMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNA 162
Cdd:TIGR02287  82 AILHGCIVGRNALVGMNAVVMDGAVIGENSIVAASAFVKAGAEMPAQYLVVGSPAKVIRELSEQELAWKKQGTHEYQVLA 161

                         170
                  ....*....|.
gi 15598948   163 RRYARDLVEDP 173
Cdd:TIGR02287 162 TRCKQTLHQCE 172
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 13-152 2.97e-29

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: 105.40  E-value: 2.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNEL-IHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHG-CSV 90
Cdd:cd00710   6 DPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTpIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVHGpAYI 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598948  91 GDYSLVGINAVILNgAKIGKYCIIGANAL-----IPEGKEIPDGSLVmgSPGKVVRELSEPQKKMLE 152
Cdd:cd00710  86 GDNCFIGFRSVVFN-AKVGDNCVIGHNAVvdgveIPPGRYVPAGAVI--TSQTQADALPDVTDSARE 149
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 13-171 5.98e-29

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 105.66  E-value: 5.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   13 HPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLHGCSVGD 92
Cdd:PRK13627  14 HPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGAILHGCVIGR 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598948   93 YSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEASAAHYVHNARRYARDLVE 171
Cdd:PRK13627  94 DALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDLVGRCHASLHE 172
PLN02472 PLN02472
uncharacterized protein
 5-144 7.32e-27

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 101.58  E-value: 7.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    5 LGDARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTL------GKGVT 78
Cdd:PLN02472  55 LGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTGLpaetliDRYVT 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598948   79 VGHNAMLHGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSLVMGSPGKVVRELS 144
Cdd:PLN02472 135 IGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLT 200
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
33-148 7.81e-18

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 75.29  E-value: 7.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  33 GASVWFGAVLRGDNELIHIGEHSNVQDGSVMhtDMGYPLTLGKGVTVGHNAMLHGCS-----------------VGDYSL 95
Cdd:COG0110  12 GDGVVIGPGVRIYGGNITIGDNVYIGPGVTI--DDPGGITIGDNVLIGPGVTILTGNhpiddpatfplrtgpvtIGDDVW 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598948  96 VGINAVILNGAKIGKYCIIGANALIpeGKEIPDGSLVMGSPGKVVRELSEPQK 148
Cdd:COG0110  90 IGAGATILPGVTIGDGAVVGAGSVV--TKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 18-136 5.36e-15

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: 69.05  E-value: 5.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  18 IAPSAAVIGKVRLDAGASVWFGAVLrgdNELIHIGEHSNVQDGSVMHTDmgypLTLGKGVTVGHNAMLHG-CSVGDYSLV 96
Cdd:cd03360  87 IHPSAVVSPSAVIGEGCVIMAGAVI---NPDARIGDNVIINTGAVIGHD----CVIGDFVHIAPGVVLSGgVTIGEGAFI 159

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598948  97 GINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSP 136
Cdd:cd03360 160 GAGATIIQGVTIGAGAIIGAGAVVT--KDVPDGSVVVGNP 197
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 39-153 1.50e-14

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: 67.24  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  39 GAVLRGDNELIHIGEHSNVQDGSVM--------HTDMGYPLTLGKGVTVGHNAMLHGCSVGDYSLVGINAVILNGAKIGK 110
Cdd:cd03359  33 DVIIRGDLATVSIGRYCILSEGCVIrppfkkfsKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIKD 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598948 111 YCIIGANALIPEGKEIPDGSLVMGSPGKVVRELSEPQKKMLEA 153
Cdd:cd03359 113 CVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMEE 155
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 18-136 5.72e-14

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: 66.36  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    18 IAPSAAVIGKVRLDAGASVWFGAVLrgdNELIHIGEHSNVQDGSVMHTDMgyplTLGKGVTVGHNAMLHG-CSVGDYSLV 96
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVI---NPDVRIGDNVIINTGAIVEHDC----VIGDFVHIAPGVTLSGgVVIGEGVFI 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 15598948    97 GINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSP 136
Cdd:TIGR03570 163 GAGATIIQGVTIGAGAIVGAGAVVT--KDIPDGGVVVGVP 200
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 49-140 8.97e-14

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: 64.01  E-value: 8.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  49 IHIGEHSNVQDGSVMhtDMGYPLTLGKGVTVGHNAMLHGCS--------------------VGDYSLVGINAVILNGAKI 108
Cdd:cd04647   2 ISIGDNVYIGPGCVI--SAGGGITIGDNVLIGPNVTIYDHNhdiddperpieqgvtsapivIGDDVWIGANVVILPGVTI 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598948 109 GKYCIIGANALIPegKEIPDGSLVMGSPGKVV 140
Cdd:cd04647  80 GDGAVVGAGSVVT--KDVPPNSIVAGNPAKVI 109
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 28-103 5.68e-11

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: 55.72  E-value: 5.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  28 VRLDAGASVWFGAVLRGDnelIHIGEHSNVQDGSVMHTD----MGYPLTLGKGVTVGHNAMLHG-CSVGDYSLVGINAVI 102
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGP---VVIGDNVNIGPGAVIGAAtgpnEKNPTIIGDNVEIGANAVIHGgVKIGDNAVIGAGAVV 77


                .
gi 15598948 103 L 103
Cdd:cd00208  78 T 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 51-141 2.53e-10

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: 55.20  E-value: 2.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  51 IGEHSNVQDGSVMHTDMgyplTLGKGVTVGHNAM----------------LHGCSVGDYSLVGINAVILNGAKIGKYCII 114
Cdd:cd03358  19 IGDNVKIQSNVSIYEGV----TIEDDVFIGPNVVftndlyprskiyrkweLKGTTVKRGASIGANATILPGVTIGEYALV 94

                        90       100
                ....*....|....*....|....*..
gi 15598948 115 GANALIPegKEIPDGSLVMGSPGKVVR 141
Cdd:cd03358  95 GAGAVVT--KDVPPYALVVGNPARIIG 119
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 45-140 2.08e-08

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: 50.88  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  45 DNELIHIGEH----SNVQDGSVMH----TDMGYPLTLGKGVTVGHNAMLhgcsvgdyslvGINAVILNGAKIGKYCIIGA 116
Cdd:cd03357  79 DVAPVTIGDNvligPNVQIYTAGHpldpEERNRGLEYAKPITIGDNVWI-----------GGGVIILPGVTIGDNSVIGA 147

                        90       100
                ....*....|....*....|....
gi 15598948 117 NALIPegKEIPDGSLVMGSPGKVV 140
Cdd:cd03357 148 GSVVT--KDIPANVVAAGNPARVI 169
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 7-140 8.52e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 50.02  E-value: 8.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    7 DARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVL---------RGDNELIHIGEHSNVQDGSVMHTDmgyplTLGKGV 77
Cdd:PRK12461  27 GANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHRG-----TKGGGV 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948   78 T-VGHNAML-------HGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIpdGSLVMGSPGKVV 140
Cdd:PRK12461 102 TrIGNDNLLmayshvaHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRI--GALAMMAGGSRI 170
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 90-141 1.27e-07

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 49.10  E-value: 1.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15598948   90 VGDYSLVGINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSPGKVVR 141
Cdd:PRK09677 133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVT--KSIPENTVIAGNPAKIIK 182
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 72-126 1.35e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 1.35e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598948   72 TLGKGVTVGHNAML-HGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEI 126
Cdd:PRK00892 114 KIGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRI 169
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-120 4.71e-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: 48.48  E-value: 4.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  13 HPDSWIAPSAavigkvRLDAGASVWFGAVlrgdnelihIGEHSNVQDGSVmhtdmgypltLGKGVTVGHNamlhgCSVGD 92
Cdd:COG1044 100 HPSAVIDPSA------KIGEGVSIGPFAV---------IGAGVVIGDGVV----------IGPGVVIGDG-----VVIGD 149

                        90       100
                ....*....|....*....|....*...
gi 15598948  93 YSLVGINAVILNGAKIGKYCIIGANALI 120
Cdd:COG1044 150 DCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 72-137 5.37e-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: 47.40  E-value: 5.37e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598948  72 TLGKGVTVGHNAMLH-GCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEIPDGSL-----VMGSPG 137
Cdd:cd03352   3 KIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIihsgaVIGSDG 74
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 72-126 1.14e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 47.32  E-value: 1.14e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598948  72 TLGKGVTVGHNAMLH-GCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEI 126
Cdd:COG1044 110 KIGEGVSIGPFAVIGaGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVI 165
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 72-136 2.04e-06

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: 43.97  E-value: 2.04e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598948  72 TLGKGVTVGHNAMLHGC---SVGDYSLVGINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSP 136
Cdd:cd03354  36 TIYQGVTLGGKGKGGGKrhpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT--KDVPANSTVVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 10-150 6.55e-06

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 45.03  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   10 VETHPdswiapsAAVIGK-VRLDAGASVWfgavlrgdnelihIGEHSNVQDG-SVMHtdmgypltlgkGVTVGHNAMLHG 87
Cdd:PLN02739 206 IDIHP-------AARIGKgILLDHGTGVV-------------IGETAVIGDRvSILH-----------GVTLGGTGKETG 254

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598948   88 ---CSVGDYSLVGINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSPGKVVRELSEPQKKM 150
Cdd:PLN02739 255 drhPKIGDGALLGACVTILGNISIGAGAMVAAGSLVL--KDVPSHSMVAGNPAKLIGFVDEQDPSL 318
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 7-120 1.18e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.36  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    7 DARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVlrgdnelihIGEHSNVQDGSVmhtdmgypltLGKGVTVGHNamlh 86
Cdd:PRK00892  92 DPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAV---------IGAGVVIGDGVV----------IGAGAVIGDG---- 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598948   87 gCSVGDYSLVGINAVILNGAKIGKYCIIGANALI 120
Cdd:PRK00892 149 -VKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 96-155 1.35e-05

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: 42.92  E-value: 1.35e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948  96 VGINAVILNGAKIGKYCIIGANALIpeGKEIPDGSLVMGSPGKVVRE-LSEPQKKMLEASA 155
Cdd:cd03349  82 IGHGATILPGVTIGDGAVIAAGAVV--TKDVPPYAIVGGNPAKVIRYrFDEETIERLLALK 140
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 78-140 1.44e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.09  E-value: 1.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598948   78 TVGHNAMLHGCSVGDYSLVgINAVILNGAKIGKYCIIgANALIPEGKEIPDGSLVMGSPGKVV 140
Cdd:PRK05293 305 TVEHSVLFQGVQVGEGSVV-KDSVIMPGAKIGENVVI-ERAIIGENAVIGDGVIIGGGKEVIT 365
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 51-140 2.16e-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: 43.59  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    51 IGEHSNVQDGSVMHTDMgypLTLGKGVTVGHNAMLHGCS------------VGDYSLVGINAVILNGAKIGKYCIIGANA 118
Cdd:TIGR02353 115 IGKGVDIGSLPPVCTDL---LTIGAGTIVRKEVMLLGYRaergrlhtgpvtLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|..
gi 15598948   119 LIPEGKEIPDGSLVMGSPGKVV 140
Cdd:TIGR02353 192 ALQGGQSIPDGERWHGSPAQKT 213
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 10-142 5.97e-05

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: 41.22  E-value: 5.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  10 VETHPdswiapsAAVIGK-VRLDAGASVWFG--AVLrGDNELIH----IGEHSnvqdgsvMHTDMGYPlTLGKGVTVGHN 82
Cdd:COG1045  66 IDIHP-------GATIGRgFFIDHGTGVVIGetAVI-GDNVTIYqgvtLGGTG-------KEKGKRHP-TIGDNVVIGAG 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948  83 AM-LHGCSVGDYSLVGINAVILngakigkyciiganalipegKEIPDGSLVMGSPGKVVRE 142
Cdd:COG1045 130 AKiLGPITIGDNAKIGANSVVL--------------------KDVPPGSTVVGVPARIVKR 170
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
87-116 1.72e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 15598948    87 GCSVGDYSLVGINAVILNGAKIGKYCIIGA 116
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 13-134 2.03e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.08  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  13 HPDSWIAPSA-----AVIGK-VRLDAGASVWFGAVLrGDNELIH----------IGEHSNVQDGSVMHTD---------- 66
Cdd:cd03352   5 GENVSIGPNAvigegVVIGDgVVIGPGVVIGDGVVI-GDDCVIHpnvtiyegciIGDRVIIHSGAVIGSDgfgfapdggg 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  67 ------MGYpLTLGKGVTVGHN-----AML------------------HGCSVGDYSLVGINAVILNGAKIGKYCIIGAN 117
Cdd:cd03352  84 wvkipqLGG-VIIGDDVEIGANttidrGALgdtvigdgtkidnlvqiaHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQ 162

                       170
                ....*....|....*..
gi 15598948 118 ALIPEGKEIPDGSLVMG 134
Cdd:cd03352 163 VGIAGHLTIGDGVVIGA 179
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 49-143 2.18e-04

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 39.80  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   49 IHIGEHSNVQDGSVMHTDMgYPL---------TLGKGVTVGHNAMLHGcsvgdyslvgiNAVILNGAKIGKYCIIGANAL 119
Cdd:PRK10092  94 IRIGDNCMLAPGVHIYTAT-HPLdpvarnsgaELGKPVTIGNNVWIGG-----------RAVINPGVTIGDNVVVASGAV 161

                         90       100
                 ....*....|....*....|....
gi 15598948  120 IPegKEIPDGSLVMGSPGKVVREL 143
Cdd:PRK10092 162 VT--KDVPDNVVVGGNPARIIKKL 183
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-120 3.42e-04

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: 39.72  E-value: 3.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   7 DARVETHPDSWIAPSAAVIGKVRLDAGASVWFGAVL---------RGDNELIHIGEHSNVQDGSVMH--TDmgypltLGK 75
Cdd:cd03351  27 GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkyKGEPTRLEIGDNNTIREFVTIHrgTA------QGG 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598948  76 GVT-VGHNAML-------HGCSVGDyslvgiNAVILNGAKIGKYCIIGANALI 120
Cdd:cd03351 101 GVTrIGNNNLLmayvhvaHDCVIGN------NVILANNATLAGHVEIGDYAII 147
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 29-140 3.84e-04

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: 37.97  E-value: 3.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  29 RLDAGASVWFGAVLRGDN-ELIHIGEHSNV-QD-----GSVMHTDMGYPLTLGKGVtvghnamlhgcsVGDYSLVGINAV 101
Cdd:cd05825   3 NLTIGDNSWIGEGVWIYNlAPVTIGSDACIsQGaylctGSHDYRSPAFPLITAPIV------------IGDGAWVAAEAF 70

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598948 102 ILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSPGKVV 140
Cdd:cd05825  71 VGPGVTIGEGAVVGARSVVV--RDLPAWTVYAGNPAVPV 107
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 76-134 3.96e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.82  E-value: 3.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598948   76 GVTVGHNAMLHGCSVGDYSLVgINAVILNGAKIGKYCIIgANALIPEGKEIPDGsLVMG 134
Cdd:PRK00725 338 GAVVRRSVLFSRVRVNSFSNV-EDSVLLPDVNVGRSCRL-RRCVIDRGCVIPEG-MVIG 393
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 51-120 4.37e-04

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: 38.72  E-value: 4.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598948  51 IGEHSNVQDGSVM----HTDMGYPLTL-GKGVTVGHNAMlhGCSVGDYSLVGINAVILNGAKIGKYCIIGANALI 120
Cdd:cd05636  90 LGENVNLGAGTITanlrFDDKPVKVRLkGERVDTGRRKL--GAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 7-126 6.65e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.08  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    7 DARVEthpDSWIAPSAAVIGKVRldagASVWFGAVlrgdneliHIGEHSNVQDGSVMHtdmgypltlgkGVTVGHNAMLH 86
Cdd:PRK05293 288 NAKVK---NSLVVEGCVVYGTVE----HSVLFQGV--------QVGEGSVVKDSVIMP-----------GAKIGENVVIE 341

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15598948   87 GCSVGDyslvgiNAVILNGAKIG----KYCIIGANALIPEGKEI 126
Cdd:PRK05293 342 RAIIGE------NAVIGDGVIIGggkeVITVIGENEVIGVGTVI 379
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 49-133 6.75e-04

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: 36.84  E-value: 6.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  49 IHIGEHSNVQDGSVMhtdmGYPLTLGKGVTVGHNAMLHGCSVGDYSlvginavilNGAKIGKYCIIGANALIPEGKEIPD 128
Cdd:cd00208   1 VFIGEGVKIHPKAVI----RGPVVIGDNVNIGPGAVIGAATGPNEK---------NPTIIGDNVEIGANAVIHGGVKIGD 67


                ....*
gi 15598948 129 GSLVM 133
Cdd:cd00208  68 NAVIG 72
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 87-142 1.01e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 36.67  E-value: 1.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948  87 GCSVGDYSLVgINAVILNGAKIG-----KYCIIGANALIPEGKEIPDGSLVMGSPGKVVRE 142
Cdd:cd04651  34 GVRVGSGSVV-EDSVIMPNVGIGrnaviRRAIIDKNVVIPDGVVIGGDPEEDRARFYVTED 93
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 89-149 1.22e-03

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 38.06  E-value: 1.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598948   89 SVGDYSLVGINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSPGKVVRELSEPQKK 149
Cdd:PRK09527 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVT--KDIPPNVVAAGVPCRVIREINDRDKQ 191
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 51-128 2.63e-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: 35.25  E-value: 2.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598948  51 IGEHSNVQDGS-VMHTDMGYPLTLGKGVTVGHNAMLHGCSVGDYSLVGiNAVILNGAKIGKYCIIGANALIPEGKEIPD 128
Cdd:cd05787   2 IGRGTSIGEGTtIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 33-136 2.78e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.42  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    33 GASVWFGAVLRGDNELIHIGEHSNVQDGSVMHTDMGYPLTLG-KGVTVGHnamlhGCSVGDYSLVginaviLNGAKIGKY 111
Cdd:TIGR02353 601 GRGVYIDGTDLTERDLVTIGDDSTLNEGSVIQTHLFEDRVMKsDTVTIGD-----GATLGPGAIV------LYGVVMGEG 669

                          90       100
                  ....*....|....*....|....*
gi 15598948   112 CIIGANALIPEGKEIPDGSLVMGSP 136
Cdd:TIGR02353 670 SVLGPDSLVMKGEEVPAHTRWRGNP 694
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 76-125 2.91e-03

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 35.25  E-value: 2.91e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15598948  76 GVTVGHNAMLHGCSVGDyslvgiNAVILNGAKIgKYCIIGANALIPEGKE 125
Cdd:cd04652  39 NVTIEDGCTLENCIIGN------GAVIGEKCKL-KDCLVGSGYRVEAGTE 81
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
10-139 5.28e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.23  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   10 VETHPDSWIAPSAAVIGKVRLDAGASVWFGAVLRGDN----------ELIhIGEHSNVQDGSVMH--TDMGYPLT----- 72
Cdd:PRK05289  33 VVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPqdlkykgeptRLV-IGDNNTIREFVTINrgTVQGGGVTrigdn 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948   73 --------------LGKGVTVGHNAMLHG-CSVGDYSLVGINAVILNGAKIGKYCIIGANALIpeGKEIPDGSLVMGSPG 137
Cdd:PRK05289 112 nllmayvhvahdcvVGNHVILANNATLAGhVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGV--SQDVPPYVLAEGNPA 189


                 ..
gi 15598948  138 KV 139
Cdd:PRK05289 190 RL 191
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 48-171 5.64e-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: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948    48 LIHIGEHSNVQDGSVMhtdmgYPLTLGKG-VTVGHNamlhgcSVGDYSLVGINAVILNGAKIGKYCIIGANALIPEGKEI 126
Cdd:TIGR02353 372 LTDIGEETFIADGLLM-----GNARLSGGwFRLGRT------RIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKV 440

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15598948   127 PDGSLVMGSPG----KVVRELSEPQKKMLEASAahyvhnARRYARDLVE 171
Cdd:TIGR02353 441 REGVGWLGSPPfelpRRVNRDDELEALTFEPDP------RRRLARKNVE 483
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 72-142 6.35e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.44  E-value: 6.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598948   72 TLGKGVTVGHNAML--------HGCSVGDYSLVGINAVILNGAKIGKYCIIGANALIPegKEIPDGSLVMGSPGKVVRE 142
Cdd:PRK14360 367 TLGEQVNIGAGTITanydgvkkHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTIT--KDVPDNSLAIARSRQVIKE 443
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 49-153 9.32e-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: 34.99  E-value: 9.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598948  49 IHIGEHSNVQDGSVMHTDMGYPLTLGKGVTVGHNAMLH-GC-----SVGDYSLVGINAVILNGAKIGKYCIIGANALIPE 122
Cdd:cd04646  39 IIIGENNIIEEQVTIVNKKPKDPAEPKPMIIGSNNVFEvGCkcealKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPS 118

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598948 123 GKEIPDGSLVMGspGKVVREL----SEPQKKMLEA 153
Cdd:cd04646 119 SEILPENTVIYG--ADCLRRTqtdrPKPQTLQLDF 151
 
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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