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Conserved domains on  [gi|490044503|ref|WP_003946865|]
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MULTISPECIES: gamma carbonic anhydrase family protein [Streptomyces]

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

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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 ...
 6-173 1.63e-78

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 231.07  E-value: 1.63e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   6 TVLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVG 85
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  86 HNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRA 165
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ....*...
gi 490044503 166 LAEAHAKA 173
Cdd:COG0663  162 LARRYLAE 169
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 6-173 1.63e-78

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 231.07  E-value: 1.63e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   6 TVLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVG 85
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  86 HNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRA 165
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ....*...
gi 490044503 166 LAEAHAKA 173
Cdd:COG0663  162 LARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 16-168 1.18e-70

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: 210.35  E-value: 1.18e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  16 EIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVLHGCVI 95
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490044503  96 EDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRALAE 168
Cdd:cd04645   81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 6-173 3.39e-54

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 172.62  E-value: 3.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   6 TVLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPG------FTVTIG 79
Cdd:PLN02296  44 TLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKTnlsgkvLPTIIG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  80 TGVSVGHNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFN 159
Cdd:PLN02296 124 DNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQS 203

                        170
                 ....*....|....
gi 490044503 160 ADGYRALAEAHAKA 173
Cdd:PLN02296 204 ATNYSNLAQVHAAE 217
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 17-142 5.12e-13

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: 64.05  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   17 IDPGAFTAPgSVVIGD--VVMAegsslwyNAVLRADcgpVRLGAGSNIQDNATVhvdpGFTVTIGTGVSVGHNAVLHGCV 94
Cdd:TIGR03570  90 IHPSAIVSP-SASIGEgtVIMA-------GAVINPD---VRIGDNVIINTGAIV----EHDCVIGDFVHIAPGVTLSGGV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490044503   95 -IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPA 142
Cdd:TIGR03570 155 vIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKD--IPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
92-121 7.51e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 7.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490044503   92 GCVIEDDVLVGMGATVLNGAHIGAGSLIAA 121
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 6-173 1.63e-78

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 231.07  E-value: 1.63e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   6 TVLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVG 85
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  86 HNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRA 165
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ....*...
gi 490044503 166 LAEAHAKA 173
Cdd:COG0663  162 LARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 16-168 1.18e-70

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: 210.35  E-value: 1.18e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  16 EIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVLHGCVI 95
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490044503  96 EDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRALAE 168
Cdd:cd04645   81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 6-173 3.39e-54

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 172.62  E-value: 3.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   6 TVLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPG------FTVTIG 79
Cdd:PLN02296  44 TLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKTnlsgkvLPTIIG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  80 TGVSVGHNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFN 159
Cdd:PLN02296 124 DNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQS 203

                        170
                 ....*....|....
gi 490044503 160 ADGYRALAEAHAKA 173
Cdd:PLN02296 204 ATNYSNLAQVHAAE 217
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 15-168 1.81e-42

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: 139.24  E-value: 1.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  15 PEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVLHGCV 94
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490044503  95 IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRALAE 168
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 15-144 9.75e-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: 137.11  E-value: 9.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  15 PEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVLHGCV 94
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490044503  95 IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKV 144
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKV 130
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 9-174 6.55e-28

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 102.96  E-value: 6.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   9 AIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNA 88
Cdd:PRK13627   5 AFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  89 VLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFNADGYRALAE 168
Cdd:PRK13627  85 ILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDLVG 164


                 ....*.
gi 490044503 169 AHAKAV 174
Cdd:PRK13627 165 RCHASL 170
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 13-137 1.90e-27

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: 101.16  E-value: 1.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  13 KEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCG-PVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVLH 91
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGtPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVH 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490044503  92 G-CVIEDDVLVGMGATVLNgAHIGAGSLIAAQALVpQGMRVPPGSLV 137
Cdd:cd00710   81 GpAYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVV-DGVEIPPGRYV 125
PLN02472 PLN02472
uncharacterized protein
 7-170 3.09e-23

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 92.33  E-value: 3.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   7 VLAIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATVHVD-------PGFTVtIG 79
Cdd:PLN02472  52 IIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAwnsptglPAETL-ID 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  80 TGVSVGHNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAKVRRELTEEEREGIRFN 159
Cdd:PLN02472 131 RYVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEIPKL 210

                        170
                 ....*....|.
gi 490044503 160 ADGYRALAEAH 170
Cdd:PLN02472 211 AVAINDLSQSH 221
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
12-144 2.11e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 74.14  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  12 GKEPEIDPGAFTAPGSVVIGD-VVMAEGSSLWynavlraDCGPVRLGAGSNIQDNATVhvdpgFTVTIGTGVSVGHNAVL 90
Cdd:COG0110   12 GDGVVIGPGVRIYGGNITIGDnVYIGPGVTID-------DPGGITIGDNVLIGPGVTI-----LTGNHPIDDPATFPLRT 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490044503  91 HGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQgmRVPPGSLVAGVPAKV 144
Cdd:COG0110   80 GPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTK--DVPPYAIVAGNPARV 131
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 54-144 9.13e-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: 9.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  54 VRLGAGSNIQDNatVHVDPGFTVTIGTGVSVGHNAVLHGC--------------------VIEDDVLVGMGATVLNGAHI 113
Cdd:cd04647    2 ISIGDNVYIGPG--CVISAGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVVILPGVTI 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490044503 114 GAGSLIAAQALVPQgmRVPPGSLVAGVPAKV 144
Cdd:cd04647   80 GDGAVVGAGSVVTK--DVPPNSIVAGNPAKV 108
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 17-142 5.12e-13

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: 64.05  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   17 IDPGAFTAPgSVVIGD--VVMAegsslwyNAVLRADcgpVRLGAGSNIQDNATVhvdpGFTVTIGTGVSVGHNAVLHGCV 94
Cdd:TIGR03570  90 IHPSAIVSP-SASIGEgtVIMA-------GAVINPD---VRIGDNVIINTGAIV----EHDCVIGDFVHIAPGVTLSGGV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490044503   95 -IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPA 142
Cdd:TIGR03570 155 vIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKD--IPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 17-141 3.02e-12

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: 61.73  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  17 IDPGAFTAPgSVVIGD--VVMAegsslwyNAVLRADcgpVRLGAGSNIQDNATVHVDpgftVTIGTGVSVGHNAVLHG-C 93
Cdd:cd03360   87 IHPSAVVSP-SAVIGEgcVIMA-------GAVINPD---ARIGDNVIINTGAVIGHD----CVIGDFVHIAPGVVLSGgV 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490044503  94 VIEDDVLVGMGATVLNGAHIGAGSLIAAQALVpqgMR-VPPGSLVAGVP 141
Cdd:cd03360  152 TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV---TKdVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 68-144 3.92e-12

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: 61.25  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  68 VHVDPGFTVTIGTGVSVGHNAVLHGCV---------------IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVP 132
Cdd:COG1045   78 FFIDHGTGVVIGETAVIGDNVTIYQGVtlggtgkekgkrhptIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD--VP 155

                         90
                 ....*....|..
gi 490044503 133 PGSLVAGVPAKV 144
Cdd:COG1045  156 PGSTVVGVPARI 167
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 94-144 2.42e-11

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: 58.32  E-value: 2.42e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490044503  94 VIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:cd03349   75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKD--VPPYAIVGGNPAKV 123
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 54-144 1.29e-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: 55.97  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  54 VRLGAGSNIQDNatVHVDPGftVTIGTGVSVGHNAV----------------LHGCVIEDDVLVGMGATVLNGAHIGAGS 117
Cdd:cd03358   17 VKIGDNVKIQSN--VSIYEG--VTIEDDVFIGPNVVftndlyprskiyrkweLKGTTVKRGASIGANATILPGVTIGEYA 92

                         90       100
                 ....*....|....*....|....*..
gi 490044503 118 LIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:cd03358   93 LVGAGAVVTKD--VPPYALVVGNPARI 117
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 57-144 1.55e-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: 53.97  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  57 GAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAV-LHGC--------------------------------------VIED 97
Cdd:cd03357   44 SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTiLDVApvtigdnvligpnvqiytaghpldpeernrgleyakpiTIGD 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490044503  98 DVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:cd03357  124 NVWIGGGVIILPGVTIGDNSVIGAGSVVTKD--IPANVVAAGNPARV 168
PLN02739 PLN02739
serine acetyltransferase
 55-144 2.41e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 49.26  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  55 RLGAGSNIQDNATVHVdpGFTVTIGTGVSVGHNAVLHGC---------VIEDDVLVGMGATVLNGAHIGAGSLIAAQALV 125
Cdd:PLN02739 213 RIGKGILLDHGTGVVI--GETAVIGDRVSILHGVTLGGTgketgdrhpKIGDGALLGACVTILGNISIGAGAMVAAGSLV 290

                         90
                 ....*....|....*....
gi 490044503 126 PQGmrVPPGSLVAGVPAKV 144
Cdd:PLN02739 291 LKD--VPSHSMVAGNPAKL 307
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 33-108 2.50e-07

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: 46.09  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  33 VVMAEGSSLWYNAVLRadcGPVRLGAGSNIQDNATVHVDPGFT----VTIGTGVSVGHNAVLHG-CVIEDDVLVGMGATV 107
Cdd:cd00208    1 VFIGEGVKIHPKAVIR---GPVVIGDNVNIGPGAVIGAATGPNeknpTIIGDNVEIGANAVIHGgVKIGDNAVIGAGAVV 77


                 .
gi 490044503 108 L 108
Cdd:cd00208   78 T 78
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 45-144 3.29e-07

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: 47.59  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  45 AVLRADCGPVRLGAGSNIQDNATV--------HVDPGFTVTIGTGVSVGHNAVLHGCVIEDDVLVGMGATVLNGAHIGAG 116
Cdd:cd03359   34 VIIRGDLATVSIGRYCILSEGCVIrppfkkfsKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDC 113

                         90       100
                 ....*....|....*....|....*...
gi 490044503 117 SLIAAQALVPQGMRVPPGSLVAGVPAKV 144
Cdd:cd03359  114 VKILDGTVVPPDTVIPPYSVVSGRPARF 141
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 68-141 1.01e-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: 45.12  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  68 VHVDPGFTVTIGTGVSVGHNAVLHGCV---------------IEDDVLVGMGATVLNGAHIGAGSLIAAQALVpqgMR-V 131
Cdd:cd03354   15 LFIDHGTGIVIGETAVIGDNCTIYQGVtlggkgkgggkrhptIGDNVVIGAGAKILGNITIGDNVKIGANAVV---TKdV 91

                         90
                 ....*....|
gi 490044503 132 PPGSLVAGVP 141
Cdd:cd03354   92 PANSTVVGVP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 9-143 4.02e-06

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: 45.09  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   9 AIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCgpvRLGAGSNIQDNATVHVDP-GFT------------ 75
Cdd:cd03352   14 AVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC---IIGDRVIIHSGAVIGSDGfGFApdgggwvkipql 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  76 ------------------------------------VTIGTGVSVGHNAVLHGCV-------IEDDVLVGMGATVLNGAH 112
Cdd:cd03352   91 ggviigddveiganttidrgalgdtvigdgtkidnlVQIAHNVRIGENCLIAAQVgiagsttIGDNVIIGGQVGIAGHLT 170

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490044503 113 IGAGSLIAAQALVPQgmRVPPGSLVAGVPAK 143
Cdd:cd03352  171 IGDGVVIGAGSGVTS--IVPPGEYVSGTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 66-123 4.50e-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: 45.39  E-value: 4.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490044503  66 ATVHVDPgfTVTIGTGVSVGHNAVLH-GCVIEDDVLVGMGATVLNGAHIGAGSLIAAQA 123
Cdd:COG1044  101 PSAVIDP--SAKIGEGVSIGPFAVIGaGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNV 157
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 14-115 4.99e-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: 45.39  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  14 EPEIDPGAFTAPgSVVIGdvvmaEGSSLWYNAVLRADcgpVRLGAGSNIQDNatvhvdpgftVTIGTGVSVGHNAVLH-G 92
Cdd:COG1044   96 APGIHPSAVIDP-SAKIG-----EGVSIGPFAVIGAG---VVIGDGVVIGPG----------VVIGDGVVIGDDCVLHpN 156

                         90       100
                 ....*....|....*....|...
gi 490044503  93 CVIEDDVLVGMGATVLNGAHIGA 115
Cdd:COG1044  157 VTIYERCVIGDRVIIHSGAVIGA 179
PLN02694 PLN02694
serine O-acetyltransferase
 46-144 8.45e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 44.63  E-value: 8.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  46 VLRADCGPV-RLGAGSnIQDNATvHVDPGFTVTIGTGVSVGHNAVLHGC---------VIEDDVLVGMGATVLNGAHIGA 115
Cdd:PLN02694 158 VFAVDIHPAaKIGKGI-LFDHAT-GVVIGETAVIGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGE 235

                         90       100
                 ....*....|....*....|....*....
gi 490044503 116 GSLIAAQALVPqgMRVPPGSLVAGVPAKV 144
Cdd:PLN02694 236 GAKIGAGSVVL--IDVPPRTTAVGNPARL 262
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 66-125 9.59e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 9.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490044503  66 ATVHVDPgfTVTIGTGVSVGHNAVL-HGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALV 125
Cdd:PRK00892 105 PSAVIDP--SAKIGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 12-144 3.06e-05

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: 42.80  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  12 GKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADC-------GPVRL--GAGSNIQDNATVHV--DPGFTVT-IG 79
Cdd:cd03351   27 GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPqdlkykgEPTRLeiGDNNTIREFVTIHRgtAQGGGVTrIG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  80 ------TGVSVGH------------NAVLHG-CVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGV 140
Cdd:cd03351  107 nnnllmAYVHVAHdcvignnvilanNATLAGhVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQD--VPPYVIAAGN 184


                 ....
gi 490044503 141 PAKV 144
Cdd:cd03351  185 RARL 188
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 17-114 3.42e-05

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: 42.41  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  17 IDPGAFTAPGSVVIG-DVVMAEGSSLWYNAVLRADCgpvRLGAGSNIQDnatvhvdpgftVTIGTGVSVGHNAVLHGCVI 95
Cdd:cd03353    5 IDPETTYIDGDVEIGvDVVIDPGVILEGKTVIGEDC---VIGPNCVIKD-----------STIGDGVVIKASSVIEGAVI 70

                         90       100
                 ....*....|....*....|....*
gi 490044503  96 EDDVLVG------MGATVLNGAHIG 114
Cdd:cd03353   71 GNGATVGpfahlrPGTVLGEGVHIG 95
cysE PRK11132
serine acetyltransferase; Provisional
 95-144 3.85e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 42.76  E-value: 3.85e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490044503  95 IEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:PRK11132 196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQP--VPPHTTAAGVPARI 243
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 17-142 4.09e-05

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: 41.60  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  17 IDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLradcgpvrlGAGSNIQDNATVhvdpGFTVTIGTGVSVGHNAVLHG---- 92
Cdd:cd03350    4 VPPGAIIRDGAFIGPGAVLMMPSYVNIGAYV---------DEGTMVDSWATV----GSCAQIGKNVHLSAGAVIGGvlep 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490044503  93 -----CVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQ-------------GMRVPPGSLV-AGVPA 142
Cdd:cd03350   71 lqatpVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyYGRVPPGSVVvAGSLP 139
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
16-144 4.66e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.39  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  16 EIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLradCGPVRLGAGSNI----------QD--------------------N 65
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVI---DGHTTIGKNNRIfpfasigedpQDlkykgeptrlvigdnntireF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  66 ATVH---VDPGFTVTIG------TGVSVGH------------NAVLHG-CVIEDDVLVGMGATVLNGAHIGAGSLIAAQA 123
Cdd:PRK05289  93 VTINrgtVQGGGVTRIGdnnllmAYVHVAHdcvvgnhvilanNATLAGhVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMS 172

                        170       180
                 ....*....|....*....|.
gi 490044503 124 LVPQGmrVPPGSLVAGVPAKV 144
Cdd:PRK05289 173 GVSQD--VPPYVLAEGNPARL 191
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 40-143 7.76e-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: 42.05  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   40 SLWYNAVLRAdcgpvrLGAgsNIQDNATVHVDPGFT---VTIGTGVSVGHNAVLHG------------CVIEDDVLVGMG 104
Cdd:TIGR02353 101 SPLYSLYLRA------LGA--KIGKGVDIGSLPPVCtdlLTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTR 172

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 490044503  105 ATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPAK 143
Cdd:TIGR02353 173 STLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 56-138 1.27e-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: 38.71  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  56 LGAGSNIQDNATVHvdpgfTVTIGTGVSVGHNAVLHGCVIEDDVLVGMGATVlngahigAGSLIAAQALVPQGMRVPPGS 135
Cdd:cd05787    2 IGRGTSIGEGTTIK-----NSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTI-------HHSIVADGAVIGKGCTIPPGS 69


                 ...
gi 490044503 136 LVA 138
Cdd:cd05787   70 LIS 72
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 54-143 1.46e-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: 39.13  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  54 VRLGAGSNIQDNATVH-VDPgftVTIGTGVSVGHNAVLhgC------------------VIEDDVLVGMGATVLNGAHIG 114
Cdd:cd05825    4 LTIGDNSWIGEGVWIYnLAP---VTIGSDACISQGAYL--CtgshdyrspafplitapiVIGDGAWVAAEAFVGPGVTIG 78

                         90       100
                 ....*....|....*....|....*....
gi 490044503 115 AGSLIAAQALVPQGmrVPPGSLVAGVPAK 143
Cdd:cd05825   79 EGAVVGARSVVVRD--LPAWTVYAGNPAV 105
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 54-125 3.08e-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: 39.70  E-value: 3.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490044503  54 VRLGAGSNIQDNATVhvdpGFTVTIGTGVSVGHNAVL-HGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALV 125
Cdd:cd03352    2 AKIGENVSIGPNAVI----GEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 53-144 6.30e-04

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 38.83  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  53 PVRLGAGSNIQ------DNATVHVDPGFTVTIGTGVSVGHNAVLH-------------------GCVIEDDVLVGMGATV 107
Cdd:PRK09527  67 PVYFSYGSNIHigrnfyANFNLTIVDDYTVTIGDNVLIAPNVTLSvtghpvhhelrkngemysfPITIGNNVWIGSHVVI 146

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 490044503 108 LNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:PRK09527 147 NPGVTIGDNSVIGAGSVVTKD--IPPNVVAAGVPCRV 181
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 17-123 6.40e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 6.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  17 IDPGAFTAPGsVVIGD-VVMAEGSSLWYNAVLRADcgpVRLGAGSNIQDNATVHVDpgftVTIGTGVSVGHNAVLHGC-- 93
Cdd:PRK00892 115 IGEGVSIGPN-AVIGAgVVIGDGVVIGAGAVIGDG---VKIGADCRLHANVTIYHA----VRIGNRVIIHSGAVIGSDgf 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  94 ------------------VIEDDVLVGMGATVLNGA----------------------HIGAGSLIAAQA 123
Cdd:PRK00892 187 gfandrggwvkipqlgrvIIGDDVEIGANTTIDRGAlddtvigegvkidnlvqiahnvVIGRHTAIAAQV 256
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 66-119 6.77e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 39.23  E-value: 6.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490044503  66 ATVHVDPGftVTIGTGVSVGHNAVLH-GCVIEDDVLVGMGATVLNGAHIGAGSLI 119
Cdd:COG1044  113 EGVSIGPF--AVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPNVTIYERCVI 165
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 47-144 7.62e-04

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 38.70  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  47 LRADC-GPVRLGAGSNIQDNATVHVDPGFTVTIGTGVSVGHNAVL----HG------------------------CVIED 97
Cdd:PRK09677  56 LRLDAfGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFItdhnHGsfkhsddfsspnlppdmrtlessaVVIGQ 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490044503  98 DVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSLVAGVPAKV 144
Cdd:PRK09677 136 RVWIGENVTILPGVSIGNGCIVGANSVVTKS--IPENTVIAGNPAKI 180
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 77-136 7.92e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.96  E-value: 7.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490044503  77 TIGTGVSVGHNAVL--------HGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGmrVPPGSL 136
Cdd:PRK14355 374 TIGRNVNIGCGTITcnydgvkkHRTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKD--VPPDSL 439
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 76-142 1.12e-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: 38.58  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490044503   76 VTIGTGVSVGHNAVLHGCVIEDDVL------------VGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAGVPA 142
Cdd:TIGR02353 617 VTIGDDSTLNEGSVIQTHLFEDRVMksdtvtigdgatLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNPA 695
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 76-119 1.15e-03

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: 38.47  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490044503  76 VTIGTGVSVGHNAVLHGCVIEDDVLVGMgaTVLNGAHIGAGSLI 119
Cdd:COG1207  285 TVIGEGVVIGPNCTLKDSTIGDGVVIKY--SVIEDAVVGAGATV 326
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 75-123 2.13e-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: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490044503  75 TVTIGTGVSVGHNAVLH-GCVIEDDVLVGMGATVLNGAHIGAGSLIAAQA 123
Cdd:cd03352    1 SAKIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNV 50
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 1-139 2.21e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 37.31  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503   1 MADGTTVL--AIGGKEPEIDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRAD-------CGPVRLGAGSN--IQDNATVH 69
Cdd:PRK12461  14 LGSGVEIGpfAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEpqdftykGEESRLEIGDRnvIREGVTIH 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490044503  70 --VDPGFTVTIGTG-VSVGHNAVLHGCVIEDDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAG 139
Cdd:PRK12461  94 rgTKGGGVTRIGNDnLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAG 166
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 26-143 4.64e-03

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: 36.53  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  26 GSVVIGDVVmaE-GSSlwyNAVLRADCGPVRLGAGSNIqDNAtVHvdpgftvtIGTGVSVGHNAVLHGCV-------IED 97
Cdd:COG1044  199 GRVVIGDDV--EiGAN---TTIDRGALGDTVIGDGTKI-DNL-VQ--------IAHNVRIGEHTAIAAQVgiagstkIGD 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490044503  98 DVLVGmGATVLNG-AHIGAGSLIAAQALVpqgMR-VPPGSLVAGVPAK 143
Cdd:COG1044  264 NVVIG-GQVGIAGhLTIGDGVIIGAQSGV---TKsIPEGGVYSGSPAQ 307
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 17-139 6.21e-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: 35.76  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  17 IDPGAFTAPGSVVIGDVVMAEGSSLWYNAVLRADCGPVRLGAGSNIQDNATV------HVDPGFTVTIGTgvsvgHNAVL 90
Cdd:cd04646    2 IAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIvnkkpkDPAEPKPMIIGS-----NNVFE 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490044503  91 HGCVIE-----DDVLVGMGATVLNGAHIGAGSLIAAQALVPQGMRVPPGSLVAG 139
Cdd:cd04646   77 VGCKCEalkigNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYG 130
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
92-121 7.51e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 7.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 490044503   92 GCVIEDDVLVGMGATVLNGAHIGAGSLIAA 121
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 45-138 8.31e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 36.11  E-value: 8.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490044503  45 AVLRADCGPVRLGAGSNIQDNATVHVDPgfTVTIGTGVSVGHNAVLHG-------------CVIEDDVL----VGMGATV 107
Cdd:PRK14358 242 ATLRRRINEAHMKAGVTLQDPGTILIED--TVTLGRDVTIEPGVLLRGqtrvadgvtigaySVVTDSVLhegaVIKPHSV 319

                         90       100       110
                 ....*....|....*....|....*....|.
gi 490044503 108 LNGAHIGAGSLIAAQAlvpqgmRVPPGSLVA 138
Cdd:PRK14358 320 LEGAEVGAGSDVGPFA------RLRPGTVLG 344
 
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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