NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1176161327|gb|OQX77705|]
View 

tryptophan synthase subunit alpha [Epsilonproteobacteria bacterium 4484_65]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10785067)

Tryptophan synthase (TRPS) alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P).

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 2-244 1.96e-97

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 439929  Cd Length: 262  Bit Score: 285.03  E-value: 1.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT-- 79
Cdd:COG0159    16 KALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFELVREFREDPDTpl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  80 LWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLV 159
Cdd:COG0159    96 VLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKKIAAAASGFVYYV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 160 AYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLldESLSDTQKITNISAI 236
Cdd:COG0159   176 SVTGVTGARTavSDDLAELVARIRAHTDLPVAVGFGIsTPEQAAEVAAYADGVIVGSALVKLI--EEGGDDEALEALAAF 253


                  ....*...
gi 1176161327 237 AKEIKEKI 244
Cdd:COG0159   254 VRELKAAL 261
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 2-244 1.96e-97

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 285.03  E-value: 1.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT-- 79
Cdd:COG0159    16 KALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFELVREFREDPDTpl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  80 LWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLV 159
Cdd:COG0159    96 VLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKKIAAAASGFVYYV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 160 AYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLldESLSDTQKITNISAI 236
Cdd:COG0159   176 SVTGVTGARTavSDDLAELVARIRAHTDLPVAVGFGIsTPEQAAEVAAYADGVIVGSALVKLI--EEGGDDEALEALAAF 253


                  ....*...
gi 1176161327 237 AKEIKEKI 244
Cdd:COG0159   254 VRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 4-241 2.91e-96

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 281.67  E-value: 2.91e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT--LW 81
Cdd:cd04724     2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIpiVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  82 MGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVAY 161
Cdd:cd04724    82 MGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 162 AGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLldESLSDTQKITNISAIAK 238
Cdd:cd04724   162 TGVTGARTelPDDLKELIKRIRKYTDLPIAVGFGIsTPEQAAEVAKYADGVIVGSALVKII--EEGGEEEALEALKELAE 239


                  ...
gi 1176161327 239 EIK 241
Cdd:cd04724   240 SLK 242
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 2-242 2.60e-93

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 274.68  E-value: 2.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHID 78
Cdd:PRK13111   12 KALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELVREIrekDPTIP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  79 TLWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYL 158
Cdd:PRK13111   92 IVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKKIASHASGFVYY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 159 VAYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLLDeslsDTQKITNISA 235
Cdd:PRK13111  172 VSRAGVTGARSadAADLAELVARLKAHTDLPVAVGFGIsTPEQAAAIAAVADGVIVGSALVKIIEE----NPEALEALAA 247


                  ....*..
gi 1176161327 236 IAKEIKE 242
Cdd:PRK13111  248 FVKELKA 254
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
4-219 9.65e-74

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 224.88  E-value: 9.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHIDTL 80
Cdd:pfam00290  12 FVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVrskGVEVPIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  81 WMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVA 160
Cdd:pfam00290  92 LMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEQAEGFVYLVS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176161327 161 YAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGVDQ-NTAKEKAKGVDGVIVGSAFVKVL 219
Cdd:pfam00290 172 RAGVTGAENavNAQVDELVERLKKYTAVPVAVGFGISTpEHVKQAAAGADGVIVGSALVRII 233
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 2-241 4.37e-63

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 197.57  E-value: 4.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHID 78
Cdd:TIGR00262  10 GAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVrqkHPNIP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  79 TLWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYL 158
Cdd:TIGR00262  90 IGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEKSQGFVYL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 159 VAYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGVDQNTAKEKAK--GVDGVIVGSAFVKVLLDESLSDTQKITNIS 234
Cdd:TIGR00262 170 VSRAGVTGARNraASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIdaGADGVIVGSAIVKIIEENLNTPEKMLQALE 249


                  ....*..
gi 1176161327 235 AIAKEIK 241
Cdd:TIGR00262 250 EFVQNLK 256
 
Name Accession Description Interval E-value
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 2-244 1.96e-97

Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase alpha chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439929  Cd Length: 262  Bit Score: 285.03  E-value: 1.96e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT-- 79
Cdd:COG0159    16 KALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFELVREFREDPDTpl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  80 LWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLV 159
Cdd:COG0159    96 VLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIKKIAAAASGFVYYV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 160 AYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLldESLSDTQKITNISAI 236
Cdd:COG0159   176 SVTGVTGARTavSDDLAELVARIRAHTDLPVAVGFGIsTPEQAAEVAAYADGVIVGSALVKLI--EEGGDDEALEALAAF 253


                  ....*...
gi 1176161327 237 AKEIKEKI 244
Cdd:COG0159   254 VRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 4-241 2.91e-96

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 281.67  E-value: 2.91e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT--LW 81
Cdd:cd04724     2 LIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIpiVL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  82 MGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVAY 161
Cdd:cd04724    82 MGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 162 AGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLldESLSDTQKITNISAIAK 238
Cdd:cd04724   162 TGVTGARTelPDDLKELIKRIRKYTDLPIAVGFGIsTPEQAAEVAKYADGVIVGSALVKII--EEGGEEEALEALKELAE 239


                  ...
gi 1176161327 239 EIK 241
Cdd:cd04724   240 SLK 242
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 2-242 2.60e-93

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 274.68  E-value: 2.60e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHID 78
Cdd:PRK13111   12 KALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELVREIrekDPTIP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  79 TLWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYL 158
Cdd:PRK13111   92 IVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKKIASHASGFVYY 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 159 VAYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGV-DQNTAKEKAKGVDGVIVGSAFVKVLLDeslsDTQKITNISA 235
Cdd:PRK13111  172 VSRAGVTGARSadAADLAELVARLKAHTDLPVAVGFGIsTPEQAAAIAAVADGVIVGSALVKIIEE----NPEALEALAA 247


                  ....*..
gi 1176161327 236 IAKEIKE 242
Cdd:PRK13111  248 FVKELKA 254
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
4-219 9.65e-74

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 224.88  E-value: 9.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHIDTL 80
Cdd:pfam00290  12 FVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVREVrskGVEVPIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  81 WMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVA 160
Cdd:pfam00290  92 LMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVVEQAEGFVYLVS 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176161327 161 YAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGVDQ-NTAKEKAKGVDGVIVGSAFVKVL 219
Cdd:pfam00290 172 RAGVTGAENavNAQVDELVERLKKYTAVPVAVGFGISTpEHVKQAAAGADGVIVGSALVRII 233
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 2-241 4.37e-63

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 197.57  E-value: 4.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   2 KKLVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKI---APHID 78
Cdd:TIGR00262  10 GAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKKVrqkHPNIP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  79 TLWMGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYL 158
Cdd:TIGR00262  90 IGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIAEKSQGFVYL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 159 VAYAGITGAGK--SEDLQPIITDIKSFTKTPVYVGFGVDQNTAKEKAK--GVDGVIVGSAFVKVLLDESLSDTQKITNIS 234
Cdd:TIGR00262 170 VSRAGVTGARNraASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIdaGADGVIVGSAIVKIIEENLNTPEKMLQALE 249


                  ....*..
gi 1176161327 235 AIAKEIK 241
Cdd:TIGR00262 250 EFVQNLK 256
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 4-244 6.48e-63

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 197.68  E-value: 6.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT--LW 81
Cdd:CHL00200   17 LIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILSILSEVNGEIKApiVI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  82 MGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVAY 161
Cdd:CHL00200   97 FTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQKIARAAPGCIYLVST 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 162 AGITGaGKSE---DLQPIITDIKSFTKTPVYVGFGVdqNTAKE----KAKGVDGVIVGSAFVKVLLDESLSDTqkITNIS 234
Cdd:CHL00200  177 TGVTG-LKTEldkKLKKLIETIKKMTNKPIILGFGI--STSEQikqiKGWNINGIVIGSACVQILLGSSPEKG--LDQLS 251

                         250
                  ....*....|
gi 1176161327 235 AIAKEIKEKI 244
Cdd:CHL00200  252 EFCKVAKKSI 261
PLN02591 PLN02591
tryptophan synthase
 4-245 1.87e-60

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 190.65  E-value: 1.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   4 LVAYITTGFPSLEFTVDAALALGEAGVDTLELGMPFSDPVADGPVIEAANLKALQNGFKLDHLFEASAKIAPHIDT--LW 81
Cdd:PLN02591    4 FIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCpiVL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  82 MGYFNPFYHRGMDKFIAEANKAGVNGFIIPDLPFEEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIYLVAY 161
Cdd:PLN02591   84 FTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYLVSS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 162 AGITG--AGKSEDLQPIITDIKSFTKTPVYVGFGVDQ-NTAKEKAK-GVDGVIVGSAFVKvLLDESLSDTQKITNISAIA 237
Cdd:PLN02591  164 TGVTGarASVSGRVESLLQELKEVTDKPVAVGFGISKpEHAKQIAGwGADGVIVGSAMVK-ALGEAKSPEEGLKRLEKLA 242


                  ....*...
gi 1176161327 238 KEIKEKIN 245
Cdd:PLN02591  243 KSLKAALP 250
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 1-246 7.85e-20

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 85.09  E-value: 7.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327   1 MKKLVAYITTGFPSLEFTVDAALALGEAgVDTLELGMPFSDPVADGPVIEAANLKALQNGfKLDHLFEASAKiaPHIDTL 80
Cdd:PRK13125    3 RPGLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKSHRKVKGLD-IWPLLEEVRKD--VSVPII 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327  81 WMGYFNPFYHRgMDKFIAEANKAGVNGFIIPDLPF---EEAKPYKPQIEAAGLNLIDFIAPTDSKARIEQIVTDAKKFIY 157
Cdd:PRK13125   79 LMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 158 LVAYAGiTGAgksedlqPIITDIKSFTKT--------PVYVGFGVD--QNTAKEKAKGVDGVIVGSAFVKVLLDESLSDT 227
Cdd:PRK13125  158 YGLRPA-TGV-------PLPVSVERNIKRvrnlvgnkYLVVGFGLDspEDARDALSAGADGVVVGTAFIEELEKNGVESA 229

                         250
                  ....*....|....*....
gi 1176161327 228 QkitnisAIAKEIKEKINE 246
Cdd:PRK13125  230 L------NLLKKIRGALDE 242
BtpA COG0434
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
158-215 3.79e-03

Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440203  Cd Length: 268  Bit Score: 37.84  E-value: 3.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176161327 158 LVAYAGITGAGKS-EDLQpiitDIKSFTK-TPVYVGFGVDQNTAKEKAKGVDGVIVGSAF 215
Cdd:COG0434   187 VIVSGARTGEATDlEDLK----RVKEAAPdVPVLVGSGVTPENVAELLSVADGAIVGSSL 242
BtpA pfam03437
BtpA family; The BtpA protein is tightly associated with the thylakoid membranes, where it ...
 145-217 8.07e-03

BtpA family; The BtpA protein is tightly associated with the thylakoid membranes, where it stabilizes the reaction centre proteins of photosystem I.


Pssm-ID: 281436  Cd Length: 254  Bit Score: 36.68  E-value: 8.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176161327 145 IEQIVTDAkkfIYLVAYAGITGAGKSEDLQPIITDIKSFT---KTPVYVGFGVDQNTAKEKAKGVDGVIVGSAFVK 217
Cdd:pfam03437 160 IESIVLDT---VERGLADAVILSGKTTGGEPDLEELKLAKetvKTPVLAGSGVNLENLEELLSIADGFIIGTSIKK 232
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH