|
Name |
Accession |
Description |
Interval |
E-value |
| carb_anhyd |
NF040597 |
carbonic anhydrase; |
1-249 |
1.82e-164 |
|
carbonic anhydrase;
Pssm-ID: 468571 Cd Length: 248 Bit Score: 454.69 E-value: 1.82e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 1 MRFNkQIFTILILSLSLALLGSGCISEGEGAEGNATQGITESEFSNIRENPVTPWNPVPTAPDIDPTAYIDPQASVIGNV 80
Cdd:NF040597 1 MKFN-QIFTILILSLSLTLAGSGCVSEGEGAEDNVAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 81 TIGASIMVSPMASIRSDEGMPIFVGSRSNVQDGVVLHALETIDEEGEPVEKNTVEVAGEKYAVYIGENVSLTHQSQVHGP 160
Cdd:NF040597 80 TIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 161 ASVGNDTFIGMQAFVFKSKIGNNCVLEPTAAAIGVTVPDGRYIPAGVVVTSQEEADKLPEITEDYAYKHTNEAVVYVNVH 240
Cdd:NF040597 160 AYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVN 239
|
....*....
gi 851229152 241 LAEGYNKAS 249
Cdd:NF040597 240 LAEGYNAAS 248
|
|
| LbH_gamma_CA |
cd00710 |
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
62-245 |
4.02e-77 |
|
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: 230.20 E-value: 4.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGMPIFVGSRSNVQDGVVLHALETideegepvekntvevagekY 141
Cdd:cd00710 3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG-------------------Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 142 AVYIGENVSLTHQSQVHGPASVGNDTFIGMQAFVFKSKIGNNCVLEPTAAAIGVTVPDGRYIPAGVVVTSQEEADKLPEI 221
Cdd:cd00710 64 SVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPDV 143
|
170 180
....*....|....*....|....
gi 851229152 222 TEDyaYKHTNEAVVYVNVHLAEGY 245
Cdd:cd00710 144 TDS--AREFNEKVITVNNELAEGY 165
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
61-245 |
6.25e-46 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 150.95 E-value: 6.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHALetideegepvekntvevagEK 140
Cdd:COG0663 10 TPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVD-------------------PG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 141 YAVYIGENVSLTHQSQVHGpASVGNDTFIGMQAFVF-KSKIGNNCVLeptaaAIGVTVPDGRYIPAGVVVTsQEEADKLP 219
Cdd:COG0663 70 YPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSPAKVVR 142
|
170 180
....*....|....*....|....*.
gi 851229152 220 EITEDYAYKHTNEAVVYVNvhLAEGY 245
Cdd:COG0663 143 ELTEEEIAFLRESAENYVE--LARRY 166
|
|
| PLN02296 |
PLN02296 |
carbonate dehydratase |
61-243 |
7.33e-13 |
|
carbonate dehydratase
Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 66.30 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHALETideegepvekntvEVAGEK 140
Cdd:PLN02296 52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 141 YAVYIGENVSLTHQSQVHGpASVGNDTFIGMQAFVFkskigNNCVLEPTA-AAIGVTVPDGRYIPAGVVVTSQeEADKLP 219
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLL-----DGVVVEKHAmVAAGALVRQNTRIPSGEVWAGN-PAKFLR 190
|
170 180
....*....|....*....|....*..
gi 851229152 220 EITEDYAYKHTNEAVVYVN---VHLAE 243
Cdd:PLN02296 191 KLTEEEIAFISQSATNYSNlaqVHAAE 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| carb_anhyd |
NF040597 |
carbonic anhydrase; |
1-249 |
1.82e-164 |
|
carbonic anhydrase;
Pssm-ID: 468571 Cd Length: 248 Bit Score: 454.69 E-value: 1.82e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 1 MRFNkQIFTILILSLSLALLGSGCISEGEGAEGNATQGITESEFSNIRENPVTPWNPVPTAPDIDPTAYIDPQASVIGNV 80
Cdd:NF040597 1 MKFN-QIFTILILSLSLTLAGSGCVSEGEGAEDNVAQEITESEFSNIRANPVTPWNPEPTEPVIDPTAYIHPQASVIGDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 81 TIGASIMVSPMASIRSDEGMPIFVGSRSNVQDGVVLHALETIDEEGEPVEKNTVEVAGEKYAVYIGENVSLTHQSQVHGP 160
Cdd:NF040597 80 TIGASVMVSPMASVRSDEGMPIFVGDRSNVQDGVVLHALETIDEEGEPVEENLVEVDGKKYAVYIGERVSLAHQSQVHGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 161 ASVGNDTFIGMQAFVFKSKIGNNCVLEPTAAAIGVTVPDGRYIPAGVVVTSQEEADKLPEITEDYAYKHTNEAVVYVNVH 240
Cdd:NF040597 160 AYVGDDTFIGMQAFVFKAKIGNNCVLEPKSAAIGVTIPDGRYIPAGTVVTSQDEADKLPEITDDYAYKHTNEAVVYVNVN 239
|
....*....
gi 851229152 241 LAEGYNKAS 249
Cdd:NF040597 240 LAEGYNAAS 248
|
|
| LbH_gamma_CA |
cd00710 |
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ... |
62-245 |
4.02e-77 |
|
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: 230.20 E-value: 4.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGMPIFVGSRSNVQDGVVLHALETideegepvekntvevagekY 141
Cdd:cd00710 3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEG-------------------Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 142 AVYIGENVSLTHQSQVHGPASVGNDTFIGMQAFVFKSKIGNNCVLEPTAAAIGVTVPDGRYIPAGVVVTSQEEADKLPEI 221
Cdd:cd00710 64 SVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQTQADALPDV 143
|
170 180
....*....|....*....|....
gi 851229152 222 TEDyaYKHTNEAVVYVNVHLAEGY 245
Cdd:cd00710 144 TDS--AREFNEKVITVNNELAEGY 165
|
|
| PaaY |
COG0663 |
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ... |
61-245 |
6.25e-46 |
|
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 440427 [Multi-domain] Cd Length: 170 Bit Score: 150.95 E-value: 6.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHALetideegepvekntvevagEK 140
Cdd:COG0663 10 TPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGVVLHVD-------------------PG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 141 YAVYIGENVSLTHQSQVHGpASVGNDTFIGMQAFVF-KSKIGNNCVLeptaaAIGVTVPDGRYIPAGVVVTsQEEADKLP 219
Cdd:COG0663 70 YPLTIGDDVTIGHGAILHG-CTIGDNVLIGMGAIVLdGAVIGDGSIV-----GAGALVTEGKVVPPGSLVV-GSPAKVVR 142
|
170 180
....*....|....*....|....*.
gi 851229152 220 EITEDYAYKHTNEAVVYVNvhLAEGY 245
Cdd:COG0663 143 ELTEEEIAFLRESAENYVE--LARRY 166
|
|
| LbH_gamma_CA_like |
cd04645 |
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ... |
63-243 |
1.11e-34 |
|
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: 121.36 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 63 DIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHaletideegepvekntvevAGEKYA 142
Cdd:cd04645 1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVN-PIRIGERTNIQDGSVLH-------------------VDPGYP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 143 VYIGENVSLTHQSQVHGpASVGNDTFIGMQAFVF-KSKIGNNCVLEPtaaaiGVTVPDGRYIPAGVVVTSQeEADKLPEI 221
Cdd:cd04645 61 TIIGDNVTVGHGAVLHG-CTIGDNCLIGMGAIILdGAVIGKGSIVAA-----GSLVPPGKVIPPGSLVAGS-PAKVVREL 133
|
170 180
....*....|....*....|..
gi 851229152 222 TEDyaYKHTNEAVVYVNVHLAE 243
Cdd:cd04645 134 TDE--EIAELRESAEHYVELAK 153
|
|
| LbH_paaY_like |
cd04745 |
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ... |
62-225 |
4.47e-19 |
|
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: 80.88 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHaletideeGEPVEKNTVEVAGeky 141
Cdd:cd04745 1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFG-RIVIRDGANVQDNCVIH--------GFPGQDTVLEENG--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 142 avYIGenvsltHQSQVHGpASVGNDTFIGMQAFVF-KSKIGNNCVLEPTAAAIGVTVPDGRY----IPAGVVVT-SQEEA 215
Cdd:cd04745 69 --HIG------HGAILHG-CTIGRNALVGMNAVVMdGAVIGEESIVGAMAFVKAGTVIPPRSliagSPAKVIRElSDEEV 139
|
170
....*....|
gi 851229152 216 DKLPEITEDY 225
Cdd:cd04745 140 AWKTRGTKEY 149
|
|
| LbH_FBP |
cd04650 |
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ... |
62-209 |
1.55e-16 |
|
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: 74.14 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHAletidEEGEPVEkntvevageky 141
Cdd:cd04650 1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDND-SIYIGKYSNVQENVSIHT-----DHGYPTE----------- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851229152 142 avyIGENVSLTHQSQVHGpASVGNDTFIGMQAFVFK-SKIGNNCVLeptaaAIGVTVPDGRYIPAGVVV 209
Cdd:cd04650 64 ---IGDYVTIGHNAVVHG-AKVGNYVIVGMGAILLNgAKIGDHVII-----GAGAVVTPGKEIPDYSLV 123
|
|
| PLN02296 |
PLN02296 |
carbonate dehydratase |
61-243 |
7.33e-13 |
|
carbonate dehydratase
Pssm-ID: 215167 [Multi-domain] Cd Length: 269 Bit Score: 66.30 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHALETideegepvekntvEVAGEK 140
Cdd:PLN02296 52 APVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVN-SISVGSGTNIQDNSLVHVAKT-------------NLSGKV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 141 YAVYIGENVSLTHQSQVHGpASVGNDTFIGMQAFVFkskigNNCVLEPTA-AAIGVTVPDGRYIPAGVVVTSQeEADKLP 219
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLHG-CTVEDEAFVGMGATLL-----DGVVVEKHAmVAAGALVRQNTRIPSGEVWAGN-PAKFLR 190
|
170 180
....*....|....*....|....*..
gi 851229152 220 EITEDYAYKHTNEAVVYVN---VHLAE 243
Cdd:PLN02296 191 KLTEEEIAFISQSATNYSNlaqVHAAE 217
|
|
| PRK13627 |
PRK13627 |
carnitine operon protein CaiE; Provisional |
62-180 |
1.02e-12 |
|
carnitine operon protein CaiE; Provisional
Pssm-ID: 184189 [Multi-domain] Cd Length: 196 Bit Score: 64.83 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGMPIfVGSRSNVQDGVVLHALETIDeegepveknTVevageky 141
Cdd:PRK13627 11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLI-VQAGANLQDGCIMHGYCDTD---------TI------- 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 851229152 142 avyIGENVSLTHQSQVHGpASVGNDTFIGMQAFVFKSKI 180
Cdd:PRK13627 74 ---VGENGHIGHGAILHG-CVIGRDALVGMNSVIMDGAV 108
|
|
| LbetaH |
cd00208 |
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ... |
80-175 |
6.10e-09 |
|
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.
Pssm-ID: 100038 [Multi-domain] Cd Length: 78 Bit Score: 51.48 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 80 VTIGASIMVSPMASIRSdegmPIFVGSRSNVQDGVVLHALETIdeegepvekntvevaGEKYAVYIGENVSLTHQSQVHG 159
Cdd:cd00208 1 VFIGEGVKIHPKAVIRG----PVVIGDNVNIGPGAVIGAATGP---------------NEKNPTIIGDNVEIGANAVIHG 61
|
90
....*....|....*.
gi 851229152 160 PASVGNDTFIGMQAFV 175
Cdd:cd00208 62 GVKIGDNAVIGAGAVV 77
|
|
| PLN02472 |
PLN02472 |
uncharacterized protein |
62-241 |
4.09e-07 |
|
uncharacterized protein
Pssm-ID: 215263 [Multi-domain] Cd Length: 246 Bit Score: 49.58 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 62 PDIDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVLHALETiDEEGEPVEKNTvevagEKY 141
Cdd:PLN02472 60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLN-KITVGFCSNVQERCVLHAAWN-SPTGLPAETLI-----DRY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 142 aVYIGENVSLThqsqvhgPASVGNDTFIGMQAFVFK-SKIGNNCVLEPtaaaiGVTVPDGRYIPAGVV-----------V 209
Cdd:PLN02472 133 -VTIGAYSLLR-------SCTIEPECIIGQHSILMEgSLVETHSILEA-----GSVLPPGRRIPTGELwagnparfvrtL 199
|
170 180 190
....*....|....*....|....*....|....
gi 851229152 210 TSQE--EADKLPEITEDYAYKHTNEAVVYVNVHL 241
Cdd:PLN02472 200 TNEEtlEIPKLAVAINDLSQSHFSEFLPYSTAYL 233
|
|
| LbH_Dynactin_6 |
cd04646 |
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ... |
64-185 |
2.09e-05 |
|
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.
Pssm-ID: 100052 [Multi-domain] Cd Length: 164 Bit Score: 43.47 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 64 IDPTAYIDPQASVIGNVTIGASIMVSPMASIRSDEGmPIFVGSRSNVQDGVVL-HALETIDEEGEPV---EKNTVEVAGE 139
Cdd:cd04646 2 IAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAG-PIIIGENNIIEEQVTIvNKKPKDPAEPKPMiigSNNVFEVGCK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 851229152 140 KYAVYIGENVSLTHQSQVHGPASVGNDTFIGMQAFVFKSKIGNNCV 185
Cdd:cd04646 81 CEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENT 126
|
|
| LpxD |
COG1044 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ... |
61-203 |
2.23e-05 |
|
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: 44.62 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGasimvsPMASIrsdegmpifvGSRSNVQDGVVLHAletideegepvekntvevagek 140
Cdd:COG1044 96 APGIHPSAVIDPSAKIGEGVSIG------PFAVI----------GAGVVIGDGVVIGP---------------------- 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 141 yAVYIGENVslthqsqvhgpaSVGNDTFIGMQAFVFK-SKIGNNCVLEPtAAAIG------VTVPDGRYI 203
Cdd:COG1044 138 -GVVIGDGV------------VIGDDCVLHPNVTIYErCVIGDRVIIHS-GAVIGadgfgfAPDEDGGWV 193
|
|
| lpxD |
PRK00892 |
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional |
61-194 |
4.60e-04 |
|
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
Pssm-ID: 234858 [Multi-domain] Cd Length: 343 Bit Score: 40.89 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 61 APDIDPTAYIDPQASVIGNVTIGasimvsPMASIrsdegmpifvGSRSNVQDGVVLHAletideegepvekntvevagek 140
Cdd:PRK00892 100 AAGIHPSAVIDPSAKIGEGVSIG------PNAVI----------GAGVVIGDGVVIGA---------------------- 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 851229152 141 yAVYIGENVslthqsqvhgpaSVGNDTFIGMQAFV-FKSKIGNNCVLEPtAAAIG 194
Cdd:PRK00892 142 -GAVIGDGV------------KIGADCRLHANVTIyHAVRIGNRVIIHS-GAVIG 182
|
|
| PRK12461 |
PRK12461 |
UDP-N-acetylglucosamine acyltransferase; Provisional |
64-212 |
2.61e-03 |
|
UDP-N-acetylglucosamine acyltransferase; Provisional
Pssm-ID: 183539 [Multi-domain] Cd Length: 255 Bit Score: 38.08 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 64 IDPTAYIDPQA-----------SVIG-NVTIGASIMVSPMASIRSdegmPIFVGSRSNVQDGVVLHAletideegEPVEK 131
Cdd:PRK12461 2 IHPTAVIDPSAklgsgveigpfAVIGaNVEIGDGTWIGPHAVILG----PTRIGKNNKIHQGAVVGD--------EPQDF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 132 NtveVAGEKYAVYIG------ENVSLTHQSQVHGPASVGNDTFigmqaFVFKS------KIGNNCVLEPTAAAIGVTVPD 199
Cdd:PRK12461 70 T---YKGEESRLEIGdrnvirEGVTIHRGTKGGGVTRIGNDNL-----LMAYShvahdcQIGNNVILVNGALLAGHVTVG 141
|
170
....*....|...
gi 851229152 200 GRYIPAGVVVTSQ 212
Cdd:PRK12461 142 DRAIISGNCLVHQ 154
|
|
| WbbJ |
COG0110 |
Acetyltransferase, isoleucine patch superfamily [General function prediction only]; |
64-178 |
2.73e-03 |
|
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
Pssm-ID: 439880 [Multi-domain] Cd Length: 140 Bit Score: 37.16 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851229152 64 IDPTAYIDPQASV-IGNVTIGASIMVSPMASIrsDEGMPIFVGSRSNVQDGVVL----HALETIDEEGEPVEKntvevag 138
Cdd:COG0110 11 IGDGVVIGPGVRIyGGNITIGDNVYIGPGVTI--DDPGGITIGDNVLIGPGVTIltgnHPIDDPATFPLRTGP------- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 851229152 139 ekyaVYIGENVSLTHQSQVHGPASVGNDTFIGMQAFVFKS 178
Cdd:COG0110 82 ----VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD 117
|
|
| |
