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Conserved domains on  [gi|2125505770|ref|WP_227293495|]
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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 ...
 10-173 4.99e-90

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 259.96  E-value: 4.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  10 IGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAV 89
Cdd:COG0663     6 FDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  90 LHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAKA 169
Cdd:COG0663    86 LHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARR 165


                  ....
gi 2125505770 170 HRAA 173
Cdd:COG0663   166 YLAE 169
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 10-173 4.99e-90

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 259.96  E-value: 4.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  10 IGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAV 89
Cdd:COG0663     6 FDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  90 LHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAKA 169
Cdd:COG0663    86 LHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARR 165


                  ....
gi 2125505770 170 HRAA 173
Cdd:COG0663   166 YLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 16-168 1.43e-84

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: 245.78  E-value: 1.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  16 VLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLHGCTV 95
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2125505770  96 EDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAK 168
Cdd:cd04645    81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 7-175 3.25e-64

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 198.43  E-value: 3.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770   7 ITGIGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPG------FPVTVGE 80
Cdd:PLN02296   45 LMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKTnlsgkvLPTIIGD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  81 RVSVGHNAVLHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNG 160
Cdd:PLN02296  125 NVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSA 204

                         170
                  ....*....|....*
gi 2125505770 161 TLYVELAKAHRAAHS 175
Cdd:PLN02296  205 TNYSNLAQVHAAENA 219
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 25-142 2.18e-11

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: 59.81  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  25 PTSVVIGEVTLHAGASVWYGAVLRADCgpiVLGADSNIQDNCTVhvdpGFPVTVGERVSVGHNAVLHG-CTVEDDCLVGM 103
Cdd:TIGR03570  92 PSAIVSPSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAIV----EHDCVIGDFVHIAPGVTLSGgVVIGEGVFIGA 164

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2125505770 104 GATVLNGAVIGAGSLVAAQALVPQGmqVPPGSLVAGVPA 142
Cdd:TIGR03570 165 GATIIQGVTIGAGAIVGAGAVVTKD--IPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 10-173 4.99e-90

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 259.96  E-value: 4.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  10 IGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAV 89
Cdd:COG0663     6 FDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTIGHGAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  90 LHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAKA 169
Cdd:COG0663    86 LHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARR 165


                  ....
gi 2125505770 170 HRAA 173
Cdd:COG0663   166 YLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 16-168 1.43e-84

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: 245.78  E-value: 1.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  16 VLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLHGCTV 95
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2125505770  96 EDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAK 168
Cdd:cd04645    81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 7-175 3.25e-64

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 198.43  E-value: 3.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770   7 ITGIGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPG------FPVTVGE 80
Cdd:PLN02296   45 LMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKTnlsgkvLPTIIGD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  81 RVSVGHNAVLHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNG 160
Cdd:PLN02296  125 NVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSA 204

                         170
                  ....*....|....*
gi 2125505770 161 TLYVELAKAHRAAHS 175
Cdd:PLN02296  205 TNYSNLAQVHAAENA 219
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 15-167 4.08e-53

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: 166.00  E-value: 4.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  15 PVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLHGCT 94
Cdd:cd04745     1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2125505770  95 VEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELA 167
Cdd:cd04745    81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQLA 153
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 15-168 4.94e-49

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: 155.81  E-value: 4.94e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  15 PVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLHGCT 94
Cdd:cd04650     1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2125505770  95 VEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAK 168
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 12-173 4.09e-36

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 124.15  E-value: 4.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  12 GKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLH 91
Cdd:PRK13627    8 GLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENGHIGHGAILH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  92 GCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAGITLNGTLYVELAKAHR 171
Cdd:PRK13627   88 GCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDLVGRCH 167


                  ..
gi 2125505770 172 AA 173
Cdd:PRK13627  168 AS 169
PLN02472 PLN02472
uncharacterized protein
 2-170 8.30e-34

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 119.68  E-value: 8.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770   2 GQQALITgIGGKDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCTVHVDPGFPV----- 76
Cdd:PLN02472   48 GQRQIIP-LGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTglpae 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  77 -TVGERVSVGHNAVLHGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPLTDEERAG 155
Cdd:PLN02472  127 tLIDRYVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLE 206

                         170
                  ....*....|....*
gi 2125505770 156 ITLNGTLYVELAKAH 170
Cdd:PLN02472  207 IPKLAVAINDLSQSH 221
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 13-137 3.24e-31

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 110.79  E-value: 3.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  13 KDPVLDQEAFAAPTSVVIGEVTLHAGASVWYGAVLRADCG-PIVLGADSNIQDNCTVHVDPGFPVTVGERVSVGHNAVLH 91
Cdd:cd00710     1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGtPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2125505770  92 G-CTVEDDCLVGMGATVLNgAVIGAGSLVAAQALVpQGMQVPPGSLV 137
Cdd:cd00710    81 GpAYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVV-DGVEIPPGRYV 125
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
38-153 1.16e-19

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 80.30  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  38 GASVWYGAVLRADCGPIVLGADSNIQDNCtvHVDPGFPVTVGERVSVGHNAVL-----------------HGCTVEDDCL 100
Cdd:COG0110    12 GDGVVIGPGVRIYGGNITIGDNVYIGPGV--TIDDPGGITIGDNVLIGPGVTIltgnhpiddpatfplrtGPVTIGDDVW 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2125505770 101 VGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAKVKRPLTDEER 153
Cdd:COG0110    90 IGAGATILPGVTIGDGAVVGAGSVVTK--DVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 54-144 7.53e-15

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 66.71  E-value: 7.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  54 IVLGADSNIQDNCtvHVDPGFPVTVGERVSVGHNAVLHGC--------------------TVEDDCLVGMGATVLNGAVI 113
Cdd:cd04647     2 ISIGDNVYIGPGC--VISAGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVVILPGVTI 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2125505770 114 GAGSLVAAQALVPQgmQVPPGSLVAGVPAKV 144
Cdd:cd04647    80 GDGAVVGAGSVVTK--DVPPNSIVAGNPAKV 108
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 55-146 7.39e-12

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 59.05  E-value: 7.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  55 VLGADSNIQDNctVHVDPGfpVTVGERVSVGHNAV----------------LHGCTVEDDCLVGMGATVLNGAVIGAGSL 118
Cdd:cd03358    18 KIGDNVKIQSN--VSIYEG--VTIEDDVFIGPNVVftndlyprskiyrkweLKGTTVKRGASIGANATILPGVTIGEYAL 93

                          90       100
                  ....*....|....*....|....*...
gi 2125505770 119 VAAQALVPQgmQVPPGSLVAGVPAKVKR 146
Cdd:cd03358    94 VGAGAVVTK--DVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 25-142 2.18e-11

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: 59.81  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  25 PTSVVIGEVTLHAGASVWYGAVLRADCgpiVLGADSNIQDNCTVhvdpGFPVTVGERVSVGHNAVLHG-CTVEDDCLVGM 103
Cdd:TIGR03570  92 PSAIVSPSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAIV----EHDCVIGDFVHIAPGVTLSGgVVIGEGVFIGA 164

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2125505770 104 GATVLNGAVIGAGSLVAAQALVPQGmqVPPGSLVAGVPA 142
Cdd:TIGR03570 165 GATIIQGVTIGAGAIVGAGAVVTKD--IPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 54-147 2.52e-11

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: 58.94  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  54 IVLGADSNIQDNCTVHVDpgfpVTVGER-VSVGHNAVlhgcTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVP 132
Cdd:COG1045    86 VVIGETAVIGDNVTIYQG----VTLGGTgKEKGKRHP----TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLK--DVP 155

                          90
                  ....*....|....*
gi 2125505770 133 PGSLVAGVPAKVKRP 147
Cdd:COG1045   156 PGSTVVGVPARIVKR 170
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 50-144 4.21e-11

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: 58.20  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  50 DCGPIVLGADSNIQDNCTVHVdPGFPVTVGERVSVGHNAvlHGCTVEDDCLVGMGATVL------NGAVIGAGSLVAAQa 123
Cdd:cd03357    79 DVAPVTIGDNVLIGPNVQIYT-AGHPLDPEERNRGLEYA--KPITIGDNVWIGGGVIILpgvtigDNSVIGAGSVVTKD- 154

                          90       100
                  ....*....|....*....|.
gi 2125505770 124 lvpqgmqVPPGSLVAGVPAKV 144
Cdd:cd03357   155 -------IPANVVAAGNPARV 168
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 24-141 7.90e-11

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: 57.88  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  24 APTSVVIGEVTLHAGASVWYGAVLRADCgpiVLGADSNIQDNCTVHVDpgfpVTVGERVSVGHNAVLHG-CTVEDDCLVG 102
Cdd:cd03360    88 HPSAVVSPSAVIGEGCVIMAGAVINPDA---RIGDNVIINTGAVIGHD----CVIGDFVHIAPGVVLSGgVTIGEGAFIG 160

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2125505770 103 MGATVLNGAVIGAGSLVAAQALVPQGmqVPPGSLVAGVP 141
Cdd:cd03360   161 AGATIIQGVTIGAGAIIGAGAVVTKD--VPDGSVVVGNP 197
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 94-152 4.33e-10

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: 55.24  E-value: 4.33e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2125505770  94 TVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAKVKRPLTDEE 152
Cdd:cd03349    75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTK--DVPPYAIVGGNPAKVIRYRFDEE 131
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 33-108 1.54e-09

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: 51.87  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  33 VTLHAGASVWYGAVLRadcGPIVLGADSNIQDNCTVHVDPG----FPVTVGERVSVGHNAVLHG-CTVEDDCLVGMGATV 107
Cdd:cd00208     1 VFIGEGVKIHPKAVIR---GPVVIGDNVNIGPGAVIGAATGpnekNPTIIGDNVEIGANAVIHGgVKIGDNAVIGAGAVV 77


                  .
gi 2125505770 108 L 108
Cdd:cd00208    78 T 78
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 24-115 1.65e-08

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: 52.71  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  24 APTSVVIGEVTLHAGASVWYGAVLRADCgpiVLGADSNIQDNCTVhvdpgfpvtvGERVSVGHNAVLH-GCTVEDDCLVG 102
Cdd:COG1044   100 HPSAVIDPSAKIGEGVSIGPFAVIGAGV---VIGDGVVIGPGVVI----------GDGVVIGDDCVLHpNVTIYERCVIG 166

                          90
                  ....*....|...
gi 2125505770 103 MGATVLNGAVIGA 115
Cdd:COG1044   167 DRVIIHSGAVIGA 179
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 44-148 2.65e-08

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: 50.68  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  44 GAVLRADCGPIVLGADSNIQDNCTV--------HVDPGFPVTVGERVSVGHNAVLHGCTVEDDCLVGMGATVLNGAVIGA 115
Cdd:cd03359    33 DVIIRGDLATVSIGRYCILSEGCVIrppfkkfsKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIKD 112

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2125505770 116 GSLVAAQALVPQGMQVPPGSLVAGVPAKVKRPL 148
Cdd:cd03359   113 CVKILDGTVVPPDTVIPPYSVVSGRPARFIGEL 145
PLN02739 PLN02739
serine acetyltransferase
 70-176 4.20e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 51.58  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  70 VDPGFPVTVGERVSVGHN-AVLHGCT--------------VEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPG 134
Cdd:PLN02739  220 LDHGTGVVIGETAVIGDRvSILHGVTlggtgketgdrhpkIGDGALLGACVTILGNISIGAGAMVAAGSLVLK--DVPSH 297

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2125505770 135 SLVAGVPAKVKRpLTDEERAGITL----NGTLYVELAKAHRAAHSD 176
Cdd:PLN02739  298 SMVAGNPAKLIG-FVDEQDPSLTMeydaTREFFQNVAVAYRETIPN 342
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 74-153 1.22e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 49.62  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  74 FPVTVGERVSVGHNAVLHGctveddclvgmGATVLNGAVIGAGSLVAAQalvpqgmqVPPGSLVAGVPAKVKRPLTDEER 153
Cdd:PRK09527  130 FPITIGNNVWIGSHVVINP-----------GVTIGDNSVIGAGSVVTKD--------IPPNVVAAGVPCRVIREINDRDK 190
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 54-141 1.97e-07

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 47.05  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  54 IVLGADSNIQDNCTVHvdPGfpVTVGERVSVGHNAVLhgcTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPP 133
Cdd:cd03354    23 IVIGETAVIGDNCTIY--QG--VTLGGKGKGGGKRHP---TIGDNVVIGAGAKILGNITIGDNVKIGANAVVTK--DVPA 93


                  ....*...
gi 2125505770 134 GSLVAGVP 141
Cdd:cd03354    94 NSTVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 53-164 5.76e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.10  E-value: 5.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  53 PIVLGADSNIQDNCTVHVDPGFP------------VTVGERVSVGHN-AVLHGCT--------------VEDDCLVGMGA 105
Cdd:PLN02694  146 PLALALHSRISDVFAVDIHPAAKigkgilfdhatgVVIGETAVIGNNvSILHHVTlggtgkacgdrhpkIGDGVLIGAGA 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2125505770 106 TVLNGAVIGAGSLVAAQALVPqgMQVPPGSLVAGVPAKV----KRPLTDEERAGITLNGTLYV 164
Cdd:PLN02694  226 TILGNVKIGEGAKIGAGSVVL--IDVPPRTTAVGNPARLvggkEKPAKHEECPGESMDHTSFI 286
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 13-115 2.41e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  13 KDPVLdqeAFAA------PTSVVIGEVTLHAGASVWYGAVLRADC--GP-IVLGADSNIQDNCTVHvdPGfpVTVGERVS 83
Cdd:PRK00892   78 KNPYL---AFARlaqlfdPPATPSPAAGIHPSAVIDPSAKIGEGVsiGPnAVIGAGVVIGDGVVIG--AG--AVIGDGVK 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2125505770  84 VGHNAVLH-GCTVEDDCLVGMGATVLNGAVIGA 115
Cdd:PRK00892  151 IGADCRLHaNVTIYHAVRIGNRVIIHSGAVIGS 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 33-115 2.94e-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: 45.48  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  33 VTLHAGASVWYGAVLradcgpivlGADSNIQDNCTVHvdPGfpVTVGERVSVGHNAVLH-GCTVEDDCLVGMGATVLNGA 111
Cdd:cd03352     2 AKIGENVSIGPNAVI---------GEGVVIGDGVVIG--PG--VVIGDGVVIGDDCVIHpNVTIYEGCIIGDRVIIHSGA 68


                  ....
gi 2125505770 112 VIGA 115
Cdd:cd03352    69 VIGS 72
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 25-144 3.79e-06

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: 45.50  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  25 PTSVVIGE-------VTLHAGAsvwygavlRADCGPIVLGADSNIQDNCtvHVdpGFPVTVGERVSVGHNAVLHG-CTVE 96
Cdd:cd03351    75 PTRLEIGDnntirefVTIHRGT--------AQGGGVTRIGNNNLLMAYV--HV--AHDCVIGNNVILANNATLAGhVEIG 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2125505770  97 DDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAKV 144
Cdd:cd03351   143 DYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQ--DVPPYVIAAGNRARL 188
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 35-143 5.43e-06

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: 43.36  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  35 LHAGASVWYGAVLRADC-GPIVLGADSNIQDNCTV------HVDPGFPVTVGErvsvghnavlhgCTVEDDCLVGMGATV 107
Cdd:cd05825     4 LTIGDNSWIGEGVWIYNlAPVTIGSDACISQGAYLctgshdYRSPAFPLITAP------------IVIGDGAWVAAEAFV 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2125505770 108 LNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAK 143
Cdd:cd05825    72 GPGVTIGEGAVVGARSVVVR--DLPAWTVYAGNPAV 105
PRK10502 PRK10502
putative acyl transferase; Provisional
 35-147 2.00e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 43.01  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  35 LHAGASVWYG--AVLRaDCGPIVLGADSNIQDNCTV------HVDPGF-----PVTVGErvsvghnavlhGCTVEDDCLV 101
Cdd:PRK10502   72 LTIGDYAWIGddVWLY-NLGEITIGAHCVISQKSYLctgshdYSDPHFdlntaPIVIGE-----------GCWLAADVFV 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2125505770 102 GMGATVLNGAVIGAGSLVAAqalvpqgmQVPPGSLVAGVPAKVKRP 147
Cdd:PRK10502  140 APGVTIGSGAVVGARSSVFK--------SLPANTICRGNPAVPIRP 177
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 23-158 4.03e-05

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: 41.93  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  23 AAPTSVVI------GEVTLHAGASVWYGAVLRADCGPIVLGADSNIQDNCT-VHVDPGFPVtVGERVSVGHNAVLH-GCT 94
Cdd:cd04646     2 IAPGAVVCqeseirGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTiVNKKPKDPA-EPKPMIIGSNNVFEvGCK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2125505770  95 V-----------EDDCLVGMGATVLNGAVIGAGSlvaaqaLVPQGMQVPPGSLVAGvpAKVKRPLTDEERAGITL 158
Cdd:cd04646    81 CealkignnnvfESKSFVGKNVIITDGCIIGAGC------KLPSSEILPENTVIYG--ADCLRRTQTDRPKPQTL 147
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 55-138 9.16e-05

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: 39.10  E-value: 9.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  55 VLGADSNIQDNCTVHvdpgfPVTVGERVSVGHNAVLHGCTVEDDCLVGMGATVlngavigAGSLVAAQALVPQGMQVPPG 134
Cdd:cd05787     1 VIGRGTSIGEGTTIK-----NSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTI-------HHSIVADGAVIGKGCTIPPG 68


                  ....
gi 2125505770 135 SLVA 138
Cdd:cd05787    69 SLIS 72
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 76-142 1.51e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 41.27  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2125505770  76 VTVGERVSVGHNAVLH------------GCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPA 142
Cdd:TIGR02353 617 VTIGDDSTLNEGSVIQthlfedrvmksdTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNPA 695
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 33-119 1.69e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 41.17  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  33 VTLHAGASVWygavLRADcgpIVLGADSNIQDNCTVHVDpgfpVTVGERVSVGHNAVLHGCTVEDDCLVGMgaTVLNGAV 112
Cdd:COG1207   253 VTIIDPATTY----IDGD---VEIGRDVVIDPNVILEGK----TVIGEGVVIGPNCTLKDSTIGDGVVIKY--SVIEDAV 319


                  ....*..
gi 2125505770 113 IGAGSLV 119
Cdd:COG1207   320 VGAGATV 326
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 97-146 1.90e-04

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 40.24  E-value: 1.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2125505770  97 DDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAKVKR 146
Cdd:PRK09677  135 QRVWIGENVTILPGVSIGNGCIVGANSVVTK--SIPENTVIAGNPAKIIK 182
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 28-143 2.02e-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: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  28 VVIGE-VTLHAGASVWYGAVLRADC----------------------------GPIVLGADSNIQDNCTVhvDPG-FPVT 77
Cdd:cd03352    38 VVIGDdCVIHPNVTIYEGCIIGDRViihsgavigsdgfgfapdgggwvkipqlGGVIIGDDVEIGANTTI--DRGaLGDT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  78 V-GER------VSVGHNAVL--H-----------GCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLV 137
Cdd:cd03352   116 ViGDGtkidnlVQIAHNVRIgeNcliaaqvgiagSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTS--IVPPGEYV 193


                  ....*.
gi 2125505770 138 AGVPAK 143
Cdd:cd03352   194 SGTPAQ 199
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 76-143 2.03e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 40.89  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  76 VTVGERVSVGHNAVLHG------------CTVEDDCLVGMGATVLNGAVIGAGSLVAAQALVPQGMQVPPGSLVAGVPAK 143
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
cysE PRK11132
serine acetyltransferase; Provisional
 100-150 3.16e-04

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 40.07  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2125505770 100 LVGMGATVLN------GAVIGAGSLVaaqaLVPqgmqVPPGSLVAGVPAK-VKRPLTD 150
Cdd:PRK11132  201 MIGAGAKILGnievgrGAKIGAGSVV----LQP----VPPHTTAAGVPARiVGKPESD 250
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 55-125 4.43e-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: 39.31  E-value: 4.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2125505770  55 VLGADSNIQDNCTVhvdpGFPVTVGERVSVGHNAVL-HGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALV 125
Cdd:cd03352     3 KIGENVSIGPNAVI----GEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 67-125 4.74e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 4.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  67 TVHVDPGfpVTVGERVSVGHNAVL-HGCTVEDDCLVGMGATVLNGAVIGAGSLVAAQALV 125
Cdd:PRK00892  106 SAVIDPS--AKIGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
24-144 5.23e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  24 APTSVVIGE-------VTLHAGASvwygavlrADCGPIVLGADSNIQDNCtvHVdpGFPVTVGERVSVGHNAVLHG-CTV 95
Cdd:PRK05289   77 EPTRLVIGDnntirefVTINRGTV--------QGGGVTRIGDNNLLMAYV--HV--AHDCVVGNHVILANNATLAGhVEV 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2125505770  96 EDDCLVGMGATVLNGAVIGAGSLVAAQALVPQgmQVPPGSLVAGVPAKV 144
Cdd:PRK05289  145 GDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQ--DVPPYVLAEGNPARL 191
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 55-142 7.36e-04

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: 38.13  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  55 VLGADSNIQDNCTVhvdpGFPVTVGERVSVGHNAVLHG---------CTVEDDCLVGMGATVLNGAVIGAGSLVAAQALV 125
Cdd:cd03350    33 YVDEGTMVDSWATV----GSCAQIGKNVHLSAGAVIGGvleplqatpVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVL 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2125505770 126 PQGMQ-------------VPPGSLV-AGVPA 142
Cdd:cd03350   109 TQSTPiydretgeiyygrVPPGSVVvAGSLP 139
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 27-123 7.79e-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: 38.85  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  27 SVVIGE-VTLHAGASVWYGAVLRADC--GP-IVLGADSNIQDNCTVHvdPGfpVTVGERVSVGHNAVLHGCTV------- 95
Cdd:COG1044   108 SAKIGEgVSIGPFAVIGAGVVIGDGVviGPgVVIGDGVVIGDDCVLH--PN--VTIYERCVIGDRVIIHSGAVigadgfg 183

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  96 --------------------EDDCLVG---------MGATVL-NGA------------VIGAGSLVAAQA 123
Cdd:COG1044   184 fapdedggwvkipqlgrvviGDDVEIGanttidrgaLGDTVIgDGTkidnlvqiahnvRIGEHTAIAAQV 253
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 61-148 3.13e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 36.71  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125505770  61 NIQDNCT----VHV-------DP---------GFPVTVGERVSVGHNAVLH-GCTVEDDCLVGMGATVLNgavigagslv 119
Cdd:PRK10092   95 RIGDNCMlapgVHIytathplDPvarnsgaelGKPVTIGNNVWIGGRAVINpGVTIGDNVVVASGAVVTK---------- 164

                          90       100
                  ....*....|....*....|....*....
gi 2125505770 120 aaqalvpqgmQVPPGSLVAGVPAKVKRPL 148
Cdd:PRK10092  165 ----------DVPDNVVVGGNPARIIKKL 183
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 55-116 9.70e-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: 33.71  E-value: 9.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2125505770  55 VLGADSNIQDNctVHVDPGFpvtVGERVSVGHNAVLHGCTVEDDCLVGMGATVLNGAVIGAG 116
Cdd:cd05787    18 VIGRNCKIGKN--VVIDNSY---IWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFG 74
 
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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