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Conserved domains on  [gi|75165017|sp|Q94AU7|]
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RecName: Full=Gamma carbonic anhydrase 3, mitochondrial; Short=AtCA3; Short=GAMMA CA3; Flags: Precursor

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
 1-258 0e+00

carbonate dehydratase


:

Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 514.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   81 YGCVLRGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKH 160
Cdd:PLN02296  81 YGCVLRGDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  161 AMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKKLLNKKNA-RDT 239
Cdd:PLN02296 161 AMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEKVLRKKFArRDE 240

                        250       260
                 ....*....|....*....|....*.
gi 75165017  240 EYDSVLD-------DLTLPENVPKAA 258
Cdd:PLN02296 241 EYDSMLGvvretppELILPDNILPDK 266
 
Name Accession Description Interval E-value
PLN02296 PLN02296
carbonate dehydratase
 1-258 0e+00

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 514.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   81 YGCVLRGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKH 160
Cdd:PLN02296  81 YGCVLRGDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  161 AMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKKLLNKKNA-RDT 239
Cdd:PLN02296 161 AMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEKVLRKKFArRDE 240

                        250       260
                 ....*....|....*....|....*.
gi 75165017  240 EYDSVLD-------DLTLPENVPKAA 258
Cdd:PLN02296 241 EYDSMLGvvretppELILPDNILPDK 266
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 54-212 3.66e-81

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: 240.39  E-value: 3.66e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  54 NVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVIGDNVTIGHSAV 133
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGY------PTIIGDNVTVGHGAV 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75165017 134 LHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQ 212
Cdd:cd04645  75 LHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 50-217 5.61e-81

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 240.70  E-value: 5.61e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  50 DKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVIGDNVTIG 129
Cdd:COG0663   8 GKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGY------PLTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 130 HSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSN 209
Cdd:COG0663  82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                ....*...
gi 75165017 210 LAQAHATE 217
Cdd:COG0663 162 LARRYLAE 169
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 31-186 1.80e-06

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: 47.10  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    31 GKNHFREQL-----SRHRTLMNVFDKTPNVDK------GAFVAPNASLSGDVHVGRGSSIWYGCVLR-----GDANSISV 94
Cdd:TIGR03570  67 GDNKLRRRLveklkAKGYRFATLIHPSAIVSPsasigeGTVIMAGAVINPDVRIGDNVIINTGAIVEhdcviGDFVHIAP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    95 GA----GTNIQDNALVHVAKTnlsgkVLPTV-IGDNVTIGhsavlhgctvedeayigtsatvldgahvekhamvaSGALV 169
Cdd:TIGR03570 147 GVtlsgGVVIGEGVFIGAGAT-----IIQGVtIGAGAIVG-----------------------------------AGAVV 186

                         170
                  ....*....|....*..
gi 75165017   170 RQNtrIPSGEVWGGNPA 186
Cdd:TIGR03570 187 TKD--IPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
119-146 1.69e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|....*....
gi 75165017   119 PTVIGDNVTIGHSAVL-HGCTVEDEAYIG 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIgGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
PLN02296 PLN02296
carbonate dehydratase
 1-258 0e+00

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 514.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    1 MGTMGKAFYSVGFWIRETGQALDRLGCRLQGKNHFREQLSRHRTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIW 80
Cdd:PLN02296   1 MGTLGRAIYTVGFWIRETGQALDRLGCRLQGNYYFREQLSRHRTLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   81 YGCVLRGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKH 160
Cdd:PLN02296  81 YGCVLRGDVNSISVGSGTNIQDNSLVHVAKTNLSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  161 AMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQAHATENAKNLDEAEFKKLLNKKNA-RDT 239
Cdd:PLN02296 161 AMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSNLAQVHAAENAKSFDEIEFEKVLRKKFArRDE 240

                        250       260
                 ....*....|....*....|....*.
gi 75165017  240 EYDSVLD-------DLTLPENVPKAA 258
Cdd:PLN02296 241 EYDSMLGvvretppELILPDNILPDK 266
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 54-212 3.66e-81

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: 240.39  E-value: 3.66e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  54 NVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVIGDNVTIGHSAV 133
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGY------PTIIGDNVTVGHGAV 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75165017 134 LHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQ 212
Cdd:cd04645  75 LHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 50-217 5.61e-81

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 240.70  E-value: 5.61e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  50 DKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNlsgkvlPTVIGDNVTIG 129
Cdd:COG0663   8 GKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGY------PLTIGDDVTIG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 130 HSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSN 209
Cdd:COG0663  82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                ....*...
gi 75165017 210 LAQAHATE 217
Cdd:COG0663 162 LARRYLAE 169
PLN02472 PLN02472
uncharacterized protein
 43-217 8.61e-50

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 163.98  E-value: 8.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   43 RTLMNVFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNLSGKVLPTVI 122
Cdd:PLN02472  50 RQIIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPAETLI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  123 GDNVTIGHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSS 202
Cdd:PLN02472 130 DRYVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEIPK 209

                        170
                 ....*....|....*
gi 75165017  203 SAVEYSNLAQAHATE 217
Cdd:PLN02472 210 LAVAINDLSQSHFSE 224
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 53-212 3.69e-39

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 133.46  E-value: 3.69e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTnlsgkvLPTVIGDNVTIGHSA 132
Cdd:cd04650   1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHG------YPTEIGDYVTIGHNA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 133 VLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQ 212
Cdd:cd04650  75 VVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 53-212 1.86e-37

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: 129.03  E-value: 1.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHvaktnlSGKVLPTVIGDNVTIGHSA 132
Cdd:cd04745   1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIH------GFPGQDTVLEENGHIGHGA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 133 VLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNLAQ 212
Cdd:cd04745  75 ILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEYQQLAA 154
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 52-212 4.61e-27

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 103.35  E-value: 4.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   52 TPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVH-VAKTNlsgkvlpTVIGDNVTIGH 130
Cdd:PRK13627  10 IPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHgYCDTD-------TIVGENGHIGH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  131 SAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTEEERVFFSSSAVEYSNL 210
Cdd:PRK13627  83 GAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKEYQDL 162


                 ..
gi 75165017  211 AQ 212
Cdd:PRK13627 163 VG 164
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
64-197 2.41e-23

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 91.86  E-value: 2.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  64 NASLSGDVHVGRGSSIWYGCVLRGdaNSISVGAGTNIQDNALVHVAKtnlsgkvlPTVIGDNVTIGHSAVL--------- 134
Cdd:COG0110   2 KLLLLFGARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIDDPG--------GITIGDNVLIGPGVTIltgnhpidd 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75165017 135 --------HGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFLRKVTEEER 197
Cdd:COG0110  72 patfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD--VPPYAIVAGNPARVIRKRDEEER 140
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 53-178 1.55e-21

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: 88.07  E-value: 1.55e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  53 PNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGD-ANSISVGAGTNIQDNALVHVAKTnlsGKVLptvIGDNVTIGHS 131
Cdd:cd00710   3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADeGTPIIIGANVNIQDGVVIHALEG---YSVW---IGKNVSIAHG 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 75165017 132 AVLHG-CTVEDEAYIGTSATVLDgAHVEKHAMVASGALVrQNTRIPSG 178
Cdd:cd00710  77 AIVHGpAYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVV-DGVEIPPG 122
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 57-185 7.37e-17

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: 76.37  E-value: 7.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  57 KGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDansisvgagtniqdnalvhvaktnlsgkvlpTVIGDNVTIGHSAVLHG 136
Cdd:cd03360 101 EGCVIMAGAVINPDARIGDNVIINTGAVIGHD-------------------------------CVIGDFVHIAPGVVLSG 149

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75165017 137 -CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 185
Cdd:cd03360 150 gVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKD--VPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 70-190 5.57e-15

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: 69.07  E-value: 5.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  70 DVHVGRGSSIWYGCVlrgdansisVGAGTNIQDNalVHVAKtnlsgkvlPTVIGDNVTIGHSAV---------------- 133
Cdd:cd03358   4 NCIIGTNVFIENDVK---------IGDNVKIQSN--VSIYE--------GVTIEDDVFIGPNVVftndlyprskiyrkwe 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75165017 134 LHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVrqnTR-IPSGEVWGGNPAKFLR 190
Cdd:cd03358  65 LKGTTVKRGASIGANATILPGVTIGEYALVGAGAVV---TKdVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 70-189 5.43e-14

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 66.33  E-value: 5.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  70 DVHVGRGSSIWYGCVLrGDANSISVGAGTNIQDNALVHVA---------KTNLSGKVLPTVIGDNVtighsavlhgctve 140
Cdd:cd04647   1 NISIGDNVYIGPGCVI-SAGGGITIGDNVLIGPNVTIYDHnhdiddperPIEQGVTSAPIVIGDDV-------------- 65

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 75165017 141 deaYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFL 189
Cdd:cd04647  66 ---WIGANVVILPGVTIGDGAVVGAGSVVTKD--VPPNSIVAGNPAKVI 109
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 71-152 2.18e-10

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 55.72  E-value: 2.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  71 VHVGRGSSIWYGCVLRGDansISVGAGTNIQDNALVHVAKTNLSGKvlPTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSA 149
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGP---VVIGDNVNIGPGAVIGAATGPNEKN--PTIIGDNVEIGANAVIHGgVKIGDNAVIGAGA 75


                ...
gi 75165017 150 TVL 152
Cdd:cd00208  76 VVT 78
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 68-194 2.56e-10

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: 57.61  E-value: 2.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  68 SGDVHVGRGSSIWYGCVLRGDANSISVGAGTNIQDNALVHVAKTNLSGKV--LPTVIGDNVTIGHSAVLHGCTVEDEAYI 145
Cdd:cd03359  19 SQNIVLNGKTIIQSDVIIRGDLATVSIGRYCILSEGCVIRPPFKKFSKGVafFPLHIGDYVFIGENCVVNAAQIGSYVHI 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 75165017 146 GTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAKFLRKVTE 194
Cdd:cd03359  99 GKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPE 147
PLN02739 PLN02739
serine acetyltransferase
 121-207 4.26e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 56.20  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  121 VIGDNVTIGHSAVLHGCTVE---------DEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFLRK 191
Cdd:PLN02739 233 VIGDRVSILHGVTLGGTGKEtgdrhpkigDGALLGACVTILGNISIGAGAMVAAGSLVLKD--VPSHSMVAGNPAKLIGF 310

                         90       100
                 ....*....|....*....|....*.
gi 75165017  192 VTEEE----------RVFFSSSAVEY 207
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 ...
 92-189 7.55e-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: 7.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  92 ISVGAGTNIQDNALVHvaktNLSgkvlPTVIGDNVTIGHSAVLhgCT------------------VEDEAYIGTSATVLD 153
Cdd:cd05825   4 LTIGDNSWIGEGVWIY----NLA----PVTIGSDACISQGAYL--CTgshdyrspafplitapivIGDGAWVAAEAFVGP 73

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 75165017 154 GAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAKFL 189
Cdd:cd05825  74 GVTIGEGAVVGARSVVVRD--LPAWTVYAGNPAVPV 107
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 58-175 7.96e-09

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: 52.77  E-value: 7.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  58 GAFVAPNASLSGDVHVGRGSSIWYGCVLRGDAnsiSVGAGTNIQDNALVHVAKTnlsgkvlptvIGDNVTIGHSAVLHG- 136
Cdd:cd03350   1 GRRVPPGAIIRDGAFIGPGAVLMMPSYVNIGA---YVDEGTMVDSWATVGSCAQ----------IGKNVHLSAGAVIGGv 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 75165017 137 --------CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRI 175
Cdd:cd03350  68 leplqatpVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPI 114
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 55-187 1.24e-08

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: 53.57  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  55 VDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDA----NSI-----SVGAGTNIQDNALVH------------------ 107
Cdd:cd03352   4 IGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVvigdDCVihpnvTIYEGCIIGDRVIIHsgavigsdgfgfapdggg 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 108 VAKTNLSGKVL-------------------PTVIGD------------NVTIGHSAVLHGC-------TVEDEAYIGTSA 149
Cdd:cd03352  84 WVKIPQLGGVIigddveiganttidrgalgDTVIGDgtkidnlvqiahNVRIGENCLIAAQvgiagstTIGDNVIIGGQV 163

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75165017 150 TVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNPAK 187
Cdd:cd03352 164 GIAGHLTIGDGVVIGAGSGVTSI--VPPGEYVSGTPAQ 199
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 53-187 9.71e-08

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: 51.66  E-value: 9.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVLR-----------------GDANSI---------SVGAG--TNIQD 102
Cdd:cd03351  28 PNVeiGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGeapqdlkykgeptrleiGDNNTIrefvtihrgTAQGGgvTRIGN 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 103 NAL----VHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 177
Cdd:cd03351 108 NNLlmayVHVAHD--------CVIGNNVILANNATLAGhVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDV-PPY 178

                       170
                ....*....|
gi 75165017 178 GEVwGGNPAK 187
Cdd:cd03351 179 VIA-AGNRAR 187
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 119-191 2.64e-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: 2.64e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75165017 119 PTVIGDNVTIGHSA-VLHGCTvedeayIGtsatvlDGAhvekhaMVASGALVRQNtrIPSGEVWGGNPAKFLRK 191
Cdd:cd03349  73 DVIIGNDVWIGHGAtILPGVT------IG------DGA------VIAAGAVVTKD--VPPYAIVGGNPAKVIRY 126
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
53-187 3.57e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 50.10  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVLR-----------------GDANSI---------SVGAG--TNIQD 102
Cdd:PRK05289  31 PNVviGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGedpqdlkykgeptrlviGDNNTIrefvtinrgTVQGGgvTRIGD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  103 NAL----VHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 177
Cdd:PRK05289 111 NNLlmayVHVAHD--------CVVGNHVILANNATLAGhVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDV-PPY 181

                        170
                 ....*....|
gi 75165017  178 GEVWgGNPAK 187
Cdd:PRK05289 182 VLAE-GNPAR 190
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 45-146 4.25e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 50.02  E-value: 4.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  45 LMNVFDKTPNVDKG----AFVAPNASLSGDVHVGRGSSIWYGCVlrgdansisVGAGTNIQDNAlvhvaktnlsgkvlpt 120
Cdd:COG1044  85 LLQLFYPPPAPAPGihpsAVIDPSAKIGEGVSIGPFAVIGAGVV---------IGDGVVIGPGV---------------- 139

                        90       100
                ....*....|....*....|....*..
gi 75165017 121 VIGDNVTIGHSAVLH-GCTVEDEAYIG 146
Cdd:COG1044 140 VIGDGVVIGDDCVLHpNVTIYERCVIG 166
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 94-180 5.62e-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: 46.03  E-value: 5.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  94 VGAGTNIQDNALVhvakTNlsgkvlpTVIGDNVTIGHSAVLHGctvedeAYIGTSATVLDGAHVEkHAMVASGALVRQNT 173
Cdd:cd05787   2 IGRGTSIGEGTTI----KN-------SVIGRNCKIGKNVVIDN------SYIWDDVTIEDGCTIH-HSIVADGAVIGKGC 63


                ....*..
gi 75165017 174 RIPSGEV 180
Cdd:cd05787  64 TIPPGSL 70
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 55-169 8.82e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.87  E-value: 8.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   55 VDKGAFVAPNASLSGDVHVGRGSSIWYGCVL---------RGDANSISVGAGTNIQDNALVH-----------------V 108
Cdd:PRK12461  32 IGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHrgtkgggvtrigndnllM 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75165017  109 AKTNLSGKVlptVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALV 169
Cdd:PRK12461 112 AYSHVAHDC---QIGNNVILVNGALLAGhVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRI 170
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 31-186 1.80e-06

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: 47.10  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    31 GKNHFREQL-----SRHRTLMNVFDKTPNVDK------GAFVAPNASLSGDVHVGRGSSIWYGCVLR-----GDANSISV 94
Cdd:TIGR03570  67 GDNKLRRRLveklkAKGYRFATLIHPSAIVSPsasigeGTVIMAGAVINPDVRIGDNVIINTGAIVEhdcviGDFVHIAP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017    95 GA----GTNIQDNALVHVAKTnlsgkVLPTV-IGDNVTIGhsavlhgctvedeayigtsatvldgahvekhamvaSGALV 169
Cdd:TIGR03570 147 GVtlsgGVVIGEGVFIGAGAT-----IIQGVtIGAGAIVG-----------------------------------AGAVV 186

                         170
                  ....*....|....*..
gi 75165017   170 RQNtrIPSGEVWGGNPA 186
Cdd:TIGR03570 187 TKD--IPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 120-187 1.81e-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: 1.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 120 TVIGDNVTIghsavLHGCT--------------VEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 185
Cdd:COG1045  92 AVIGDNVTI-----YQGVTlggtgkekgkrhptIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD--VPPGSTVVGVP 164


                ..
gi 75165017 186 AK 187
Cdd:COG1045 165 AR 166
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 67-157 2.15e-06

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 48.10  E-value: 2.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  67 LSGDVHVGRGSSIWYGCVLRGD---ANSISVGAGTNIQDnalvhvaktnlsgkvlpTVIGDNVTIGHSaVLHGCTVEDEA 143
Cdd:COG1207 263 IDGDVEIGRDVVIDPNVILEGKtviGEGVVIGPNCTLKD-----------------STIGDGVVIKYS-VIEDAVVGAGA 324

                        90       100
                ....*....|....*....|
gi 75165017 144 YIGTSA-----TVL-DGAHV 157
Cdd:COG1207 325 TVGPFArlrpgTVLgEGVKI 344
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 60-161 2.86e-06

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 46.64  E-value: 2.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  60 FVAPNA-SLSGDVHVGRGSSIWYGCVLRGD---ANSISVGAGTNIQDnalvhvaktnlsgkvlpTVIGDNVTIGHSAVLH 135
Cdd:cd03353   4 LIDPETtYIDGDVEIGVDVVIDPGVILEGKtviGEDCVIGPNCVIKD-----------------STIGDGVVIKASSVIE 66

                        90       100
                ....*....|....*....|....*.
gi 75165017 136 GCTVEDEAYIGTSATVLDGAHVEKHA 161
Cdd:cd03353  67 GAVIGNGATVGPFAHLRPGTVLGEGV 92
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 53-187 3.72e-06

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: 46.94  E-value: 3.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  53 PNV--DKGAFVAPNASLSGDVHVGRGSSIWYGCVL--------------R---GDANSI---------SVGAG--TNIQD 102
Cdd:COG1043  30 PDVeiGDGTVIGSHVVIEGPTTIGKNNRIFPFASIgeepqdlkykgeptRleiGDNNTIrefvtihrgTVQGGgvTRIGD 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 103 N----ALVHVAKTnlsgkvlpTVIGDNVTIGHSAVLHG-CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTrIPS 177
Cdd:COG1043 110 DnllmAYVHVAHD--------CVVGNNVILANNATLAGhVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDV-PPY 180

                       170
                ....*....|
gi 75165017 178 GEVwGGNPAK 187
Cdd:COG1043 181 VLA-AGNPAR 189
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 99-192 4.05e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 45.96  E-value: 4.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   99 NIQDNAL----VHV--------AKTNLSGKVL--PTVIGDNVTIGHSAVLH-GCTVEDeayigtsatvldgahvekHAMV 163
Cdd:PRK10092  95 RIGDNCMlapgVHIytathpldPVARNSGAELgkPVTIGNNVWIGGRAVINpGVTIGD------------------NVVV 156

                         90       100
                 ....*....|....*....|....*....
gi 75165017  164 ASGALVRQNtrIPSGEVWGGNPAKFLRKV 192
Cdd:PRK10092 157 ASGAVVTKD--VPDNVVVGGNPARIIKKL 183
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 122-187 6.80e-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: 6.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75165017   122 IGDNVTIGHSAVLHG------------CTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPAK 187
Cdd:TIGR02353 134 IGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 41-187 7.01e-06

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: 45.11  E-value: 7.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  41 RHRTLMNVFdktPNVDKGAFVAPNASLS-GD-VHVGRGSSIWYGCVLRgDANSISVGAGTNIQDNalVHV--------AK 110
Cdd:cd03357  34 RRELLKELF---GSVGENVYIEPPFHCDyGYnIHIGDNFYANFNCTIL-DVAPVTIGDNVLIGPN--VQIytaghpldPE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017 111 TNLSGKV--LPTVIGDNVtighsavlhgctvedeaYIGTSATVLDGAHVEKHAMVASGALVrqnTR-IPSGEVWGGNPAK 187
Cdd:cd03357 108 ERNRGLEyaKPITIGDNV-----------------WIGGGVIILPGVTIGDNSVIGAGSVV---TKdIPANVVAAGNPAR 167
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 120-185 1.18e-05

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: 1.18e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75165017 120 TVIGDNVTIGHSAVL--------HGC-TVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGGNP 185
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 ...
 94-176 1.70e-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: 41.84  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  94 VGAGTNIQDNAlvhvaktnlsgKVLPTVIGDNVTIG------HSAVLHGCTVEDEAYIgTSATVLDGAHVEKHAMVASGA 167
Cdd:cd03356   2 IGESTVIGENA-----------IIKNSVIGDNVRIGdgvtitNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLC 69


                ....*....
gi 75165017 168 LVRQNTRIP 176
Cdd:cd03356  70 IIGDDVVVE 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 53-157 3.39e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.36  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   53 PNVDKGAFVAPNASLSGDVHVGRGSSIwygcvlrgdansisvGAGTNIQDNALVHvaktnlSGkvlpTVIGDNVTIGHSA 132
Cdd:PRK00892 101 AGIHPSAVIDPSAKIGEGVSIGPNAVI---------------GAGVVIGDGVVIG------AG----AVIGDGVKIGADC 155

                         90       100
                 ....*....|....*....|....*.
gi 75165017  133 VLH-GCTVEDEAYIGTSATVLDGAHV 157
Cdd:PRK00892 156 RLHaNVTIYHAVRIGNRVIIHSGAVI 181
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 122-186 3.42e-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: 3.42e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75165017   122 IGDNVTIGHSAVLH------------GCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNTRIPSGEVWGGNPA 186
Cdd:TIGR02353 619 IGDDSTLNEGSVIQthlfedrvmksdTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNPA 695
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 48-134 8.64e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.20  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   48 VFDKTPNVDKGAFVAPNASLSGDVHVGRGSSIWYGCVLRGDAnsiSVGAGTNIQDNALVHVAktnlsgkvlpTVIGDNVT 127
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV---KIGADCRLHANVTIYHA----------VRIGNRVI 174


                 ....*...
gi 75165017  128 IgHS-AVL 134
Cdd:PRK00892 175 I-HSgAVI 181
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 73-155 2.20e-04

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 38.71  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  73 VGRGSSIWYGCVLRgdaNSIsVGAGTNIQDNALVHVAktnlsgkvlptVIGDNVTIGHSAVLHGCTVEDEAYIGTSATVL 152
Cdd:cd05787   2 IGRGTSIGEGTTIK---NSV-IGRNCKIGKNVVIDNS-----------YIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66


                ...
gi 75165017 153 DGA 155
Cdd:cd05787  67 PGS 69
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 70-157 2.30e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017   70 DVHVGRGSSIWYGCVLRGDAnsiSVGAGTNIQDNALVHVAKtnlsgkvlptvIGDNVTIGHSAVLHGCTVEDEAYIGTSA 149
Cdd:PRK14355 268 GVVIGRDTTIYPGVCISGDT---RIGEGCTIEQGVVIKGCR-----------IGDDVTVKAGSVLEDSVVGDDVAIGPMA 333

                         90
                 ....*....|...
gi 75165017  150 -----TVLdGAHV 157
Cdd:PRK14355 334 hlrpgTEL-SAHV 345
PRK10502 PRK10502
putative acyl transferase; Provisional
 122-190 5.11e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.93  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  122 IGDNVTIGHSAVLhgCT------------------VEDEAYIGTSATVLDGAHVEKHAMVASGALVRQNtrIPSGEVWGG 183
Cdd:PRK10502  94 IGAHCVISQKSYL--CTgshdysdphfdlntapivIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKS--LPANTICRG 169


                 ....*..
gi 75165017  184 NPAKFLR 190
Cdd:PRK10502 170 NPAVPIR 176
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-187 7.45e-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: 40.00  E-value: 7.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  94 VGAGTNIqDNaLVHVAKtNlsgkvlpTVIGDNVTI-GHSAVLHGCTVEDEAYIGTSATVLDGAHVEKHAMVASGALVRQN 172
Cdd:COG1044 225 IGDGTKI-DN-LVQIAH-N-------VRIGEHTAIaAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKS 294

                        90
                ....*....|....*
gi 75165017 173 trIPSGEVWGGNPAK 187
Cdd:COG1044 295 --IPEGGVYSGSPAQ 307
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
119-146 1.69e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.69e-03
                          10        20
                  ....*....|....*....|....*....
gi 75165017   119 PTVIGDNVTIGHSAVL-HGCTVEDEAYIG 146
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIgGGVIIGDNVIIG 29
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 70-155 8.95e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 36.23  E-value: 8.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75165017  70 DVHVGRGSSIWYGCVlrgdansisVGAGTNIQDNALVHVAktnlsgkvlpTVIGDNVTIGHSAVLH-GCTVEDEAYIGTS 148
Cdd:cd03352   1 SAKIGENVSIGPNAV---------IGEGVVIGDGVVIGPG----------VVIGDGVVIGDDCVIHpNVTIYEGCIIGDR 61


                ....*..
gi 75165017 149 ATVLDGA 155
Cdd:cd03352  62 VIIHSGA 68
 
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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