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Conserved domains on  [gi|145334925|ref|NP_001078808|]
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gamma carbonic anhydrase 3 [Arabidopsis thaliana]

Protein Classification

gamma carbonic anhydrase family protein( domain architecture ID 11476605)

uncharacterized member of the gamma carbonic anhydrase family, a supgroup of left handed beta helix proteins with diverse functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02296 PLN02296
carbonate dehydratase
 1-269 0e+00

carbonate dehydratase


:

Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 507.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925   1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  81 YGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSA 160
Cdd:PLN02296  81 YGCVLR-----------GDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 161 TVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKK 240
Cdd:PLN02296 150 TLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEK 229

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 145334925 241 LLNKKNA-RDTEYDSVLD-------DLTLPENVPKAA 269
Cdd:PLN02296 230 VLRKKFArRDEEYDSMLGvvretppELILPDNILPDK 266
 
Name Accession Description Interval E-value
PLN02296 PLN02296
carbonate dehydratase
 1-269 0e+00

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 507.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925   1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  81 YGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSA 160
Cdd:PLN02296  81 YGCVLR-----------GDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 161 TVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKK 240
Cdd:PLN02296 150 TLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEK 229

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 145334925 241 LLNKKNA-RDTEYDSVLD-------DLTLPENVPKAA 269
Cdd:PLN02296 230 VLRKKFArRDEEYDSMLGvvretppELILPDNILPDK 266
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 54-223 4.11e-78

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: 233.07  E-value: 4.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  54 NVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVI 133
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLR-----------GDVNPIRIGERTNIQDGSVLHVDPGY------PTII 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 134 GDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSS 213
Cdd:cd04645   64 GDNVTVGHGAVLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRE 143

                        170
                 ....*....|
gi 145334925 214 SAVEYSNLAQ 223
Cdd:cd04645  144 SAEHYVELAK 153
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 50-228 1.03e-77

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 232.61  E-value: 1.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  50 DKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNlsgkvl 129
Cdd:COG0663    8 GKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLR-----------GDVGPIRIGEGSNIQDGVVLHVDPGY------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 130 PTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERV 209
Cdd:COG0663   71 PLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIA 150

                        170
                 ....*....|....*....
gi 145334925 210 FFSSSAVEYSNLAQAHATE 228
Cdd:COG0663  151 FLRESAENYVELARRYLAE 169
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 133-198 7.62e-06

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: 46.67  E-value: 7.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334925  133 IGDNVTIGHSAVLHG------------CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAK 198
Cdd:TIGR02353 134 IGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
130-157 1.36e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 145334925  130 PTVIGDNVTIGHSAVL-HGCTVEDEAYIG 157
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIgGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
PLN02296 PLN02296
carbonate dehydratase
 1-269 0e+00

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 507.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925   1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  81 YGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSA 160
Cdd:PLN02296  81 YGCVLR-----------GDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 161 TVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKK 240
Cdd:PLN02296 150 TLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEK 229

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 145334925 241 LLNKKNA-RDTEYDSVLD-------DLTLPENVPKAA 269
Cdd:PLN02296 230 VLRKKFArRDEEYDSMLGvvretppELILPDNILPDK 266
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 54-223 4.11e-78

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: 233.07  E-value: 4.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  54 NVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVI 133
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLR-----------GDVNPIRIGERTNIQDGSVLHVDPGY------PTII 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 134 GDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSS 213
Cdd:cd04645   64 GDNVTVGHGAVLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRE 143

                        170
                 ....*....|
gi 145334925 214 SAVEYSNLAQ 223
Cdd:cd04645  144 SAEHYVELAK 153
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 50-228 1.03e-77

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 232.61  E-value: 1.03e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  50 DKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNlsgkvl 129
Cdd:COG0663    8 GKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLR-----------GDVGPIRIGEGSNIQDGVVLHVDPGY------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 130 PTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERV 209
Cdd:COG0663   71 PLTIGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIA 150

                        170
                 ....*....|....*....
gi 145334925 210 FFSSSAVEYSNLAQAHATE 228
Cdd:COG0663  151 FLRESAENYVELARRYLAE 169
PLN02472 PLN02472
uncharacterized protein
 43-228 2.38e-46

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 155.51  E-value: 2.38e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  43 RTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKT 122
Cdd:PLN02472  50 RQIIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLR-----------GDLNKITVGFCSNVQERCVLHAAWN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 123 NLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRK 202
Cdd:PLN02472 119 SPTGLPAETLIDRYVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRT 198

                        170       180
                 ....*....|....*....|....*.
gi 145334925 203 VTEEERVFFSSSAVEYSNLAQAHATE 228
Cdd:PLN02472 199 LTNEETLEIPKLAVAINDLSQSHFSE 224
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 53-223 5.03e-36

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: 125.76  E-value: 5.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTnlsgkvLPTV 132
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIR-----------GDNDSIYIGKYSNVQENVSIHTDHG------YPTE 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 133 IGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFS 212
Cdd:cd04650   64 IGDYVTIGHNAVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIK 143

                        170
                 ....*....|.
gi 145334925 213 SSAVEYSNLAQ 223
Cdd:cd04650  144 KNAEEYVELAE 154
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 53-223 3.54e-34

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: 120.94  E-value: 3.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHvaktnlSGKVLPTV 132
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLR-----------GDFGRIVIRDGANVQDNCVIH------GFPGQDTV 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 133 IGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFS 212
Cdd:cd04745   64 LEENGHIGHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKT 143

                        170
                 ....*....|.
gi 145334925 213 SSAVEYSNLAQ 223
Cdd:cd04745  144 RGTKEYQQLAA 154
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 52-223 6.93e-24

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 95.26  E-value: 6.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  52 TPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVH-VAKTNlsgkvlp 130
Cdd:PRK13627  10 IPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLR-----------GDYGRLIVQAGANLQDGCIMHgYCDTD------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 131 TVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVF 210
Cdd:PRK13627  72 TIVGENGHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHW 151

                        170
                 ....*....|...
gi 145334925 211 FSSSAVEYSNLAQ 223
Cdd:PRK13627 152 KRLNTKEYQDLVG 164
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
64-208 2.92e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 86.85  E-value: 2.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  64 NASLSGDVHVGRGSSIWYGCVLRDipfdlmtdsagdaNSISVGAGTNIQDNALVHVAKtnlsgkvlPTVIGDNVTIGHSA 143
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYG-------------GNITIGDNVYIGPGVTIDDPG--------GITIGDNVLIGPGV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 144 VL-----------------HGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFLRKVTEE 206
Cdd:COG0110   61 TIltgnhpiddpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD--VPPYAIVAGNPARVIRKRDEE 138


                 ..
gi 145334925 207 ER 208
Cdd:COG0110  139 ER 140
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 53-189 4.68e-19

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: 81.52  E-value: 4.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRdipfdlmtdsAGDANSISVGAGTNIQDNALVHVAKTnlsGKVLptv 132
Cdd:cd00710    3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIR----------ADEGTPIIIGANVNIQDGVVIHALEG---YSVW--- 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145334925 133 IGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDgAHVEKHAMVASGALVrQNTRIPSG 189
Cdd:cd00710   67 IGKNVSIAHGAIVHGpAYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVV-DGVEIPPG 122
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 57-196 3.25e-15

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 72.13  E-value: 3.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  57 KGAFVAPNASLSGDVHVGRGSSIWYGCVlrdipfdlmtdsagdansisVGAGTniqdnalvhvaktnlsgkvlptVIGDN 136
Cdd:cd03360  101 EGCVIMAGAVINPDARIGDNVIINTGAV--------------------IGHDC----------------------VIGDF 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145334925 137 VTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 196
Cdd:cd03360  139 VHIAPGVVLSGgVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKD--VPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 101-201 5.69e-14

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: 66.76  E-value: 5.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 101 NSISVGAGTNIQDNalVHVAKtnlsgkvlPTVIGDNVTIGHSAV----------------LHGCTVEDEAYIGTSATVLD 164
Cdd:cd03358   15 NDVKIGDNVKIQSN--VSIYE--------GVTIEDDVFIGPNVVftndlyprskiyrkweLKGTTVKRGASIGANATILP 84

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145334925 165 GAHVEKHAMVASGALVrqnTR-IPSGEVWGGNPAKFLR 201
Cdd:cd03358   85 GVTIGEYALVGAGAVV---TKdVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 102-200 2.17e-13

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: 64.79  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 102 SISVGAGTNIQDNALVhvaktNLSGKVlptVIGDNVTIGHSAVLHGC--------------------TVEDEAYIGTSAT 161
Cdd:cd04647    1 NISIGDNVYIGPGCVI-----SAGGGI---TIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVV 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145334925 162 VLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFL 200
Cdd:cd04647   73 ILPGVTIGDGAVVGAGSVVTKD--VPPNSIVAGNPAKVI 109
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 53-198 1.99e-09

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: 56.67  E-value: 1.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVLRDIPFDLM---TDSA---GDANSI---------SVGAG--TNIQD 113
Cdd:cd03351   28 PNVeiGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKykgEPTRleiGDNNTIrefvtihrgTAQGGgvTRIGN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 114 NAL----VHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 188
Cdd:cd03351  108 NNLlmayVHVAHD--------CVIGNNVILANNATLAGhVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDV-PPY 178

                        170
                 ....*....|
gi 145334925 189 GEVwGGNPAK 198
Cdd:cd03351  179 VIA-AGNRAR 187
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 71-163 4.26e-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: 52.25  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  71 VHVGRGSSIWYGCVLRDipfdlmtdsagdanSISVGAGTNIQDNALVHVAKTNLSGKvlPTVIGDNVTIGHSAVLHG-CT 149
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG--------------PVVIGDNVNIGPGAVIGAATGPNEKN--PTIIGDNVEIGANAVIHGgVK 64

                         90
                 ....*....|....
gi 145334925 150 VEDEAYIGTSATVL 163
Cdd:cd00208   65 IGDNAVIGAGAVVT 78
PLN02739 PLN02739
serine acetyltransferase
 132-218 4.86e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 56.20  E-value: 4.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 132 VIGDNVTIGHSAVLHGCTVE---------DEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFLRK 202
Cdd:PLN02739 233 VIGDRVSILHGVTLGGTGKEtgdrhpkigDGALLGACVTILGNISIGAGAMVAAGSLVLKD--VPSHSMVAGNPAKLIGF 310

                         90       100
                 ....*....|....*....|....*.
gi 145334925 203 VTEEE----------RVFFSSSAVEY 218
Cdd:PLN02739 311 VDEQDpsltmeydatREFFQNVAVAY 336
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 103-200 7.04e-09

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: 52.22  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 103 ISVGAGTNIQDNALVHvaktNLSgkvlPTVIGDNVTIGHSAVLhgCT------------------VEDEAYIGTSATVLD 164
Cdd:cd05825    4 LTIGDNSWIGEGVWIY----NLA----PVTIGSDACISQGAYL--CTgshdyrspafplitapivIGDGAWVAAEAFVGP 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145334925 165 GAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFL 200
Cdd:cd05825   74 GVTIGEGAVVGARSVVVRD--LPAWTVYAGNPAVPV 107
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
53-198 7.12e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 55.10  E-value: 7.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVLRDIPFDLMTDSA------GDANSI---------SVGAG--TNIQD 113
Cdd:PRK05289  31 PNVviGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEptrlviGDNNTIrefvtinrgTVQGGgvTRIGD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 114 NAL----VHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 188
Cdd:PRK05289 111 NNLlmayVHVAHD--------CVVGNHVILANNATLAGhVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDV-PPY 181

                        170
                 ....*....|
gi 145334925 189 GEVWgGNPAK 198
Cdd:PRK05289 182 VLAE-GNPAR 190
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 105-186 3.44e-08

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: 51.23  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 105 VGAGTNIQDNALVHVAKTnlsgkvlptvIGDNVTIGHSAVLHG---------CTVEDEAYIGTSATVLDGAHVEKHAMVA 175
Cdd:cd03350   34 VDEGTMVDSWATVGSCAQ----------IGKNVHLSAGAVIGGvleplqatpVIIEDDVFIGANCEVVEGVIVGKGAVLA 103

                         90
                 ....*....|.
gi 145334925 176 SGALVRQNTRI 186
Cdd:cd03350  104 AGVVLTQSTPI 114
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 55-180 5.38e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 52.33  E-value: 5.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  55 VDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRDIPFDLmtDSAGDANSISVGAGTNIQDNALVH---------------- 118
Cdd:PRK12461  32 IGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDF--TYKGEESRLEIGDRNVIREGVTIHrgtkgggvtrigndnl 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334925 119 -VAKTNLSGKVlptVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALV 180
Cdd:PRK12461 110 lMAYSHVAHDC---QIGNNVILVNGALLAGhVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRI 170
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 53-198 1.85e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 50.79  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVLRDIPFDLM---TDSA---GDANSI---------SVGAG--TNIQD 113
Cdd:COG1043   30 PDVeiGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKykgEPTRleiGDNNTIrefvtihrgTVQGGgvTRIGD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 114 N----ALVHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 188
Cdd:COG1043  110 DnllmAYVHVAHD--------CVVGNNVILANNATLAGhVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDV-PPY 180

                        170
                 ....*....|
gi 145334925 189 GEVwGGNPAK 198
Cdd:COG1043  181 VLA-AGNPAR 189
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 68-205 2.83e-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: 49.14  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  68 SGDVHVGRGSSIWYGCVLRdipfdlmtdsaGDANSISVGAGTNIQDNALVHVAKTNLSGKV--LPTVIGDNVTIGHSAVL 145
Cdd:cd03359   19 SQNIVLNGKTIIQSDVIIR-----------GDLATVSIGRYCILSEGCVIRPPFKKFSKGVafFPLHIGDYVFIGENCVV 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 146 HGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTE 205
Cdd:cd03359   88 NAAQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPE 147
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 130-202 2.86e-07

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: 48.69  E-value: 2.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145334925 130 PTVIGDNVTIGHSA-VLHGCTvedeayIGtsatvlDGAhvekhaMVASGALVRQNtrIPSGEVWGGNPAKFLRK 202
Cdd:cd03349   73 DVIIGNDVWIGHGAtILPGVT------IG------DGA------VIAAGAVVTKD--VPPYAIVGGNPAKVIRY 126
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 105-191 4.29e-07

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: 46.42  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 105 VGAGTNIQDNALVhvakTNlsgkvlpTVIGDNVTIGHSAVLHGctvedeAYIGTSATVLDGAHVEkHAMVASGALVRQNT 184
Cdd:cd05787    2 IGRGTSIGEGTTI----KN-------SVIGRNCKIGKNVVIDN------SYIWDDVTIEDGCTIH-HSIVADGAVIGKGC 63


                 ....*..
gi 145334925 185 RIPSGEV 191
Cdd:cd05787   64 TIPPGSL 70
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 131-198 1.56e-06

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: 47.00  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 131 TVIGDNVTIghsavLHGCT--------------VEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 196
Cdd:COG1045   92 AVIGDNVTI-----YQGVTlggtgkekgkrhptIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD--VPPGSTVVGVP 164


                 ..
gi 145334925 197 AK 198
Cdd:COG1045  165 AR 166
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-198 2.69e-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: 47.02  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 105 VGAGTNIqDNaLVHVA-------------KTNLSGKvlpTVIGDNVTIGhsavlhGctvedeayigtSATVLDGAHVEKH 171
Cdd:cd03352  117 IGDGTKI-DN-LVQIAhnvrigencliaaQVGIAGS---TTIGDNVIIG------G-----------QVGIAGHLTIGDG 174

                         90       100
                 ....*....|....*....|....*..
gi 145334925 172 AMVASGALVRQNtrIPSGEVWGGNPAK 198
Cdd:cd03352  175 VVIGAGSGVTSI--VPPGEYVSGTPAQ 199
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 110-203 4.10e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 45.96  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 110 NIQDNAL----VHV--------AKTNLSGKVL--PTVIGDNVTIGHSAVLH-GCTVEDeayigtsatvldgahvekHAMV 174
Cdd:PRK10092  95 RIGDNCMlapgVHIytathpldPVARNSGAELgkPVTIGNNVWIGGRAVINpGVTIGD------------------NVVV 156

                         90       100
                 ....*....|....*....|....*....
gi 145334925 175 ASGALVRQNtrIPSGEVWGGNPAKFLRKV 203
Cdd:PRK10092 157 ASGAVVTKD--VPDNVVVGGNPARIIKKL 183
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 133-198 7.62e-06

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: 46.67  E-value: 7.62e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145334925  133 IGDNVTIGHSAVLHG------------CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAK 198
Cdd:TIGR02353 134 IGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 45-157 9.59e-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: 46.16  E-value: 9.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  45 LMNVFDKTPNVDKG----AFVAPNASLSGDVHVGRGSSIWYGCVlrdipfdlmtdsagdansisVGAGTNIQDNAlvhva 120
Cdd:COG1044   85 LLQLFYPPPAPAPGihpsAVIDPSAKIGEGVSIGPFAVIGAGVV--------------------IGDGVVIGPGV----- 139

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145334925 121 ktnlsgkvlptVIGDNVTIGHSAVLH-GCTVEDEAYIG 157
Cdd:COG1044  140 -----------VIGDGVVIGDDCVLHpNVTIYERCVIG 166
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 131-196 9.64e-06

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 43.20  E-value: 9.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145334925 131 TVIGDNVTIGHSAVL--------HGC-TVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 196
Cdd:cd03354   29 AVIGDNCTIYQGVTLggkgkgggKRHpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD--VPANSTVVGVP 101
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 105-187 1.44e-05

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 42.23  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 105 VGAGTNIQDNAlvhvaktnlsgKVLPTVIGDNVTIG------HSAVLHGCTVEDEAYIgTSATVLDGAHVEKHAMVASGA 178
Cdd:cd03356    2 IGESTVIGENA-----------IIKNSVIGDNVRIGdgvtitNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLC 69


                 ....*....
gi 145334925 179 LVRQNTRIP 187
Cdd:cd03356   70 IIGDDVVVE 78
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 31-197 1.92e-05

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: 44.41  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925   31 GKNHFREQL-----SRHRTLMNVFDKTPNVDK------GAFVAPNASLSGDVHVGRGSSIWYGCVlrdIPFDlmtDSAGD 99
Cdd:TIGR03570  67 GDNKLRRRLveklkAKGYRFATLIHPSAIVSPsasigeGTVIMAGAVINPDVRIGDNVIINTGAI---VEHD---CVIGD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  100 ANSISVGA----GTNIQDNALVHVAKTnlsgkVLPTV-IGDNVTIGhsavlhgctvedeayigtsatvldgahvekhamv 174
Cdd:TIGR03570 141 FVHIAPGVtlsgGVVIGEGVFIGAGAT-----IIQGVtIGAGAIVG---------------------------------- 181

                         170       180
                  ....*....|....*....|...
gi 145334925  175 aSGALVRQNtrIPSGEVWGGNPA 197
Cdd:TIGR03570 182 -AGAVVTKD--IPDGGVVVGVPA 201
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 71-197 3.24e-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: 44.74  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925   71 VHVGRGSSIwYGCvlrDIP-FDLMTdsAGDANSISVGAGTN---IQDNALvhvaktnlsgKVLPTVIGDNVTIG-HSAVL 145
Cdd:TIGR02353 598 VKIGRGVYI-DGT---DLTeRDLVT--IGDDSTLNEGSVIQthlFEDRVM----------KSDTVTIGDGATLGpGAIVL 661

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145334925  146 HGCTVEDEAYIGTSATVLDGAHVEKHamvasgalvrqnTRipsgevWGGNPA 197
Cdd:TIGR02353 662 YGVVMGEGSVLGPDSLVMKGEEVPAH------------TR------WRGNPA 695
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 41-198 7.23e-05

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: 42.41  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  41 RHRTLMNVFdktPNVDKGAFVAPNASLS-GD-VHVGRGSSIWYGCVLRDIpfdlmtdsagdaNSISVGAGTNIQDNalVH 118
Cdd:cd03357   34 RRELLKELF---GSVGENVYIEPPFHCDyGYnIHIGDNFYANFNCTILDV------------APVTIGDNVLIGPN--VQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 119 V--------AKTNLSGKV--LPTVIGDNVtighsavlhgctvedeaYIGTSATVLDGAHVEKHAMVASGALVrqnTR-IP 187
Cdd:cd03357   97 IytaghpldPEERNRGLEyaKPITIGDNV-----------------WIGGGVIILPGVTIGDNSVIGAGSVV---TKdIP 156

                        170
                 ....*....|.
gi 145334925 188 SGEVWGGNPAK 198
Cdd:cd03357  157 ANVVAAGNPAR 167
PRK10502 PRK10502
putative acyl transferase; Provisional
 133-201 5.47e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.93  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 133 IGDNVTIGHSAVLhgCT------------------VEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGG 194
Cdd:PRK10502  94 IGAHCVISQKSYL--CTgshdysdphfdlntapivIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS--LPANTICRG 169


                 ....*..
gi 145334925 195 NPAKFLR 201
Cdd:PRK10502 170 NPAVPIR 176
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 105-198 6.72e-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: 40.39  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925 105 VGAGTNIqDNaLVHVAKtNlsgkvlpTVIGDNVTI-GHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQN 183
Cdd:COG1044  225 IGDGTKI-DN-LVQIAH-N-------VRIGEHTAIaAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKS 294

                         90
                 ....*....|....*
gi 145334925 184 trIPSGEVWGGNPAK 198
Cdd:COG1044  295 --IPEGGVYSGSPAQ 307
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 53-168 7.24e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 7.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  53 PNVDKGAFVAPNASLSGDVHVGRGSSIwygcvlrdipfdlmtdsagdansisvGAGTNIQDNALVHvaktnlSGkvlpTV 132
Cdd:PRK00892 101 AGIHPSAVIDPSAKIGEGVSIGPNAVI--------------------------GAGVVIGDGVVIG------AG----AV 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145334925 133 IGDNVTIGHSAVLH-GCTVEDEAYIGTSATVLDGAHV 168
Cdd:PRK00892 145 IGDGVKIGADCRLHaNVTIYHAVRIGNRVIIHSGAVI 181
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 67-168 1.08e-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: 40.01  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  67 LSGDVHVGRGSSIWYGCVLRdipfdlmtdsaGD---ANSISVGAGTNIQDnalvhvaktnlsgkvlpTVIGDNVTIGHSa 143
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILE-----------GKtviGEGVVIGPNCTLKD-----------------STIGDGVVIKYS- 313

                         90       100       110
                 ....*....|....*....|....*....|.
gi 145334925 144 VLHGCTVEDEAYIGTSA-----TVL-DGAHV 168
Cdd:COG1207  314 VIEDAVVGAGATVGPFArlrpgTVLgEGVKI 344
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 63-172 1.23e-03

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: 38.94  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  63 PNASLSGDVHVGRGSSIWYGCVLRDipfdlmtdsagdansisvgagtniqdnalvhvaktnlsgkvlpTVIGDNVTIGHS 142
Cdd:cd03353   26 PGVILEGKTVIGEDCVIGPNCVIKD-------------------------------------------STIGDGVVIKAS 62

                         90       100       110
                 ....*....|....*....|....*....|
gi 145334925 143 AVLHGCTVEDEAYIGTSATVLDGAHVEKHA 172
Cdd:cd03353   63 SVIEGAVIGNGATVGPFAHLRPGTVLGEGV 92
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 131-174 1.31e-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: 39.62  E-value: 1.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 145334925 131 TVIGDNVTIGHSAVLHGCTVEDEAYIgtSATVLDGAHVEKHAMV 174
Cdd:COG1207  285 TVIGEGVVIGPNCTLKDSTIGDGVVI--KYSVIEDAVVGAGATV 326
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
130-157 1.36e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 1.36e-03
                          10        20
                  ....*....|....*....|....*....
gi 145334925  130 PTVIGDNVTIGHSAVL-HGCTVEDEAYIG 157
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIgGGVIIGDNVIIG 29
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 48-145 2.95e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  48 VFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLrdipfdlmtdsaGDanSISVGAGTNIQDNALVHVAktnlsgk 127
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI------------GD--GVKIGADCRLHANVTIYHA------- 166

                         90
                 ....*....|....*....
gi 145334925 128 vlpTVIGDNVTIgHS-AVL 145
Cdd:PRK00892 167 ---VRIGNRVII-HSgAVI 181
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 73-166 5.58e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.86  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145334925  73 VGRGSSIWYGCVLRdipfdlmtdsagdaNSIsVGAGTNIQDNALVHVAktnlsgkvlptVIGDNVTIGHSAVLHGCTVED 152
Cdd:cd05787    2 IGRGTSIGEGTTIK--------------NSV-IGRNCKIGKNVVIDNS-----------YIWDDVTIEDGCTIHHSIVAD 55

                         90
                 ....*....|....
gi 145334925 153 EAYIGTSATVLDGA 166
Cdd:cd05787   56 GAVIGKGCTIPPGS 69
 
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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