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Conserved domains on  [gi|300567659|emb|CBV15544|]
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unnamed protein product [Caenorhabditis elegans]

Protein Classification

triose-phosphate isomerase( domain architecture ID 10794370)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate

CATH:  3.20.20.70
EC:  5.3.1.1
Gene Ontology:  GO:0004807|GO:0006096|GO:0031625|GO:0042803
PubMed:  11257493|12206759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-245 5.13e-132

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 372.71  E-value: 5.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   1 MTRKFFVGGNWKMNGDYASV-DGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLK-AGVLVAAQNCYKVPKGAFTGEIS 78
Cdd:PTZ00333   2 MKRKPFVGGNWKCNGTKASIkELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  79 PAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKgVS--- 155
Cdd:PTZ00333  82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKK-VSdea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 156 WENIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASL 235
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 300567659 236 KPDFVKIINA 245
Cdd:PTZ00333 241 KPDFVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-245 5.13e-132

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 372.71  E-value: 5.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   1 MTRKFFVGGNWKMNGDYASV-DGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLK-AGVLVAAQNCYKVPKGAFTGEIS 78
Cdd:PTZ00333   2 MKRKPFVGGNWKCNGTKASIkELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  79 PAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKgVS--- 155
Cdd:PTZ00333  82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKK-VSdea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 156 WENIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASL 235
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 300567659 236 KPDFVKIINA 245
Cdd:PTZ00333 241 KPDFVDIIKS 250
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-245 5.41e-131

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439919 [Multi-domain]  Cd Length: 249  Bit Score: 369.77  E-value: 5.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   3 RKFFVGGNWKMNGDYASVDGIVT-FLNASADNSSVDVVVAPPAPYLAYAKSKLKA-GVLVAAQNCYKVPKGAFTGEISPA 80
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAaLAAALADLADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  81 MIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVdKGVS---WE 157
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAAL-AGLSaeqAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 158 NIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP 237
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 300567659 238 -DFVKIINA 245
Cdd:COG0149  241 eDFLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 5-244 8.88e-129

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.


Pssm-ID: 238190  Cd Length: 242  Bit Score: 363.78  E-value: 8.88e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   5 FFVGGNWKMNGDYASVDGIV-TFLNASADNSSVDVVVAPPAPYLAYAKSKLKA-GVLVAAQNCYKVPKGAFTGEISPAMI 82
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAkALNAVLKDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  83 KDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKGVSWENIVIA 162
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 163 YEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSpAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD-FVK 241
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                 ...
gi 300567659 242 IIN 244
Cdd:cd00311  240 IIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 5-245 1.52e-124

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.


Pssm-ID: 459680  Cd Length: 244  Bit Score: 353.35  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659    5 FFVGGNWKMNGDYASVDGIVT-FLNASADNSSVDVVVAPPAPYLAYAKSKLKAGVLVAAQNCYKVPKGAFTGEISPAMIK 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAeLAEALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   84 DLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDK-GVSWENIVIA 162
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGlGAEQKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  163 YEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKvSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP-DFVK 241
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLD 239


                  ....
gi 300567659  242 IINA 245
Cdd:pfam00121 240 IINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 6-238 3.26e-55

triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 129513 [Multi-domain]  Cd Length: 205  Bit Score: 175.76  E-value: 3.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659    6 FVGGNWKM-NGDYASVDGIVTFLNAS-ADNSSVDVVVAPPAPYLAYAKSKLKagVLVAAQNCYKVPKGAFTGEISPAMIK 83
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEEvASEAGVAVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   84 DLGLEWVILGHSERRHVfgESDalIAEKTVHALEAGIKVVFCIGEKLEEREAghtkdvnfrqlqaivdkgVSWENIVIAY 163
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCTNNVLTTAAA------------------AALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300567659  164 EPVWAIGTGKTASGEQAQEVHEWIRAflkekvSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD 238
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVRA------VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-245 5.13e-132

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 372.71  E-value: 5.13e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   1 MTRKFFVGGNWKMNGDYASV-DGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLK-AGVLVAAQNCYKVPKGAFTGEIS 78
Cdd:PTZ00333   2 MKRKPFVGGNWKCNGTKASIkELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEIS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  79 PAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKgVS--- 155
Cdd:PTZ00333  82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKK-VSdea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 156 WENIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASL 235
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 300567659 236 KPDFVKIINA 245
Cdd:PTZ00333 241 KPDFVDIIKS 250
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-245 5.41e-131

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439919 [Multi-domain]  Cd Length: 249  Bit Score: 369.77  E-value: 5.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   3 RKFFVGGNWKMNGDYASVDGIVT-FLNASADNSSVDVVVAPPAPYLAYAKSKLKA-GVLVAAQNCYKVPKGAFTGEISPA 80
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAaLAAALADLADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  81 MIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVdKGVS---WE 157
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAAL-AGLSaeqAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 158 NIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP 237
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 300567659 238 -DFVKIINA 245
Cdd:COG0149  241 eDFLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 5-244 8.88e-129

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.


Pssm-ID: 238190  Cd Length: 242  Bit Score: 363.78  E-value: 8.88e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   5 FFVGGNWKMNGDYASVDGIV-TFLNASADNSSVDVVVAPPAPYLAYAKSKLKA-GVLVAAQNCYKVPKGAFTGEISPAMI 82
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAkALNAVLKDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  83 KDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKGVSWENIVIA 162
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 163 YEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSpAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD-FVK 241
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                 ...
gi 300567659 242 IIN 244
Cdd:cd00311  240 IIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 5-245 1.52e-124

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.


Pssm-ID: 459680  Cd Length: 244  Bit Score: 353.35  E-value: 1.52e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659    5 FFVGGNWKMNGDYASVDGIVT-FLNASADNSSVDVVVAPPAPYLAYAKSKLKAGVLVAAQNCYKVPKGAFTGEISPAMIK 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAeLAEALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   84 DLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDK-GVSWENIVIA 162
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGlGAEQKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  163 YEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKvSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP-DFVK 241
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLD 239


                  ....
gi 300567659  242 IINA 245
Cdd:pfam00121 240 IINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
 3-245 7.69e-122

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 346.72  E-value: 7.69e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   3 RKFFVGGNWKMNGDYASVDGIVT-FLNASADNSSVDVVVAPPAPYLAYAKSKLKA-GVLVAAQNCYKVPKGAFTGEISPA 80
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEeLKAALPDADGVEVAVAPPFTALASVKEALKGsNIKLGAQNVHPEDSGAFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  81 MIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAiVDKGVS---WE 157
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEA-ALAGLSaeqFA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 158 NIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSpAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP 237
Cdd:PRK00042 160 NLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKA 238


                 ....*....
gi 300567659 238 -DFVKIINA 245
Cdd:PRK00042 239 eDFLAIVKA 247
PLN02561 PLN02561
triosephosphate isomerase
 1-245 4.57e-109

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 314.45  E-value: 4.57e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   1 MTRKFFVGGNWKMNGDYASVDGIVTFLNASADNSS--VDVVVAPPAPYLAYAKSKLKAGVLVAAQNCYKVPKGAFTGEIS 78
Cdd:PLN02561   1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEdvVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  79 PAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKGVSWEN 158
Cdd:PLN02561  81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 159 IVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD 238
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240


                 ....*..
gi 300567659 239 FVKIINA 245
Cdd:PLN02561 241 FIDIIKS 247
PLN02429 PLN02429
triosephosphate isomerase
 4-245 6.44e-86

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 258.18  E-value: 6.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   4 KFFVGGNWKMNGDYASVDGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLKAGVLVAAQNCYKVPKGAFTGEISPAMIK 83
Cdd:PLN02429  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLK 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  84 DLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKGVSWENIVIAY 163
Cdd:PLN02429 145 DLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAY 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 164 EPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLK-PDFVKI 242
Cdd:PLN02429 225 EPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFATI 304


                 ...
gi 300567659 243 INA 245
Cdd:PLN02429 305 VNS 307
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 2-245 8.18e-85

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 265.05  E-value: 8.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   2 TRKFFVGGNWKMNGDYASVDGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLK-AGVLVAAQNCYKVPKGAFTGEISPA 80
Cdd:PRK13962 396 PRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTGEISGP 475

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  81 MIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDkGVSWEN-- 158
Cdd:PRK13962 476 MLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALN-GLSAEQvk 554

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 159 -IVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKP 237
Cdd:PRK13962 555 kVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKA 634


                 ....*....
gi 300567659 238 -DFVKIINA 245
Cdd:PRK13962 635 qEFAAIANY 643
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 5-243 1.42e-58

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 185.73  E-value: 1.42e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   5 FFVGGNWKMNGDYASVDGIVTFLNASADN--SSVDVVVAPPapYLAYAKS-KLKAGVLVAAQNCYKVPKGAFTGEISPAM 81
Cdd:PRK14565   3 FLIVANWKMNGDFSLFSSFLKELSNKLANneITLKLVICPP--FTAMSSFvECNPNIKLGAQNCFYGSSGGYTGEISAKM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  82 IKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKgvsWENIVI 161
Cdd:PRK14565  81 LKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPK---HGEFII 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 162 AYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKvspavadatRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD-FV 240
Cdd:PRK14565 158 AYEPVWAIGGSTIPSNDAIAEAFEIIRSYDSKS---------HIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsFC 228


                 ...
gi 300567659 241 KII 243
Cdd:PRK14565 229 KII 231
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 6-238 3.26e-55

triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 129513 [Multi-domain]  Cd Length: 205  Bit Score: 175.76  E-value: 3.26e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659    6 FVGGNWKM-NGDYASVDGIVTFLNAS-ADNSSVDVVVAPPAPYLAYAKSKLKagVLVAAQNCYKVPKGAFTGEISPAMIK 83
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEEvASEAGVAVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   84 DLGLEWVILGHSERRHVfgESDalIAEKTVHALEAGIKVVFCIGEKLEEREAghtkdvnfrqlqaivdkgVSWENIVIAY 163
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCTNNVLTTAAA------------------AALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300567659  164 EPVWAIGTGKTASGEQAQEVHEWIRAflkekvSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPD 238
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVRA------VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 1-231 3.08e-44

triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 152.11  E-value: 3.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   1 MTRKFFVGGNWKM-NGDYASVDGIVTFLN-ASADNSSVDVVVAPPAPYLAY------AKSKL-KAGVLVAAQNCYKVPKG 71
Cdd:PRK14905   1 MAKKIYFGTNLKMyKGNAETVDYLSELLAfAEKFKSDYDIELFVIPSYIALkdaveaAASETgHPKIKIGAQNMNAKDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  72 AFTGEISPAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQaIVD 151
Cdd:PRK14905  81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLK-IGL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 152 KGVSWE---NIVIAYEPVWAIGTGKT-ASGEQAQEVHEWIRAFLKEKVSPAvADATRIIYGGSVTADNAAELGKKPDIDG 227
Cdd:PRK14905 160 HGVSAEqlpHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDG 238


                 ....
gi 300567659 228 FLVG 231
Cdd:PRK14905 239 LFIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 2-243 4.01e-43

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 146.68  E-value: 4.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659   2 TRKFFVGGNWKMNGDYASVDGIVTFLNASAD----NSSVDVVVAPPAPYLAYAKSKLKA-----GVLVAAQNCYKVPKGA 72
Cdd:PRK15492   1 MKKIYFGTNLKMYKGIADATDFLAKLSELADdipaDKDIELFVIPSFTAIQDAIAATLAiphdhPIIIGAQNMNPNDNGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  73 FTGEISPAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQaIVDK 152
Cdd:PRK15492  81 FTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLK-IGLH 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659 153 GVSWENIV---IAYEPVWAIGT-GKTASGEQAQEVHEWIRAFLKEKVSPAvADATRIIYGGSVTADNAAELGKKPDIDGF 228
Cdd:PRK15492 160 GINPDQLAklrIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPHIDGL 238

                        250
                 ....*....|....*.
gi 300567659 229 LVGGASLKPD-FVKII 243
Cdd:PRK15492 239 FIGRSAWDADkFFAII 254
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 31-125 1.78e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 56.03  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567659  31 ADNSSVDVVVAPPAPYLAYAKSKLkaGVLVAAQNCYKVPKGAFTGEISPAMIKDLGLEWVILGHSERRHVFGESDALIAE 110
Cdd:PRK04302  32 SKETGVRIAVAPQALDIRRVAEEV--DIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVER 109

                         90
                 ....*....|....*
gi 300567659 111 ktvhALEAGIKVVFC 125
Cdd:PRK04302 110 ----AKKLGLESVVC 120
 
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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