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Conserved domains on  [gi|1063704338|ref|NP_001323967|]
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triosephosphate isomerase [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02429 PLN02429
triosephosphate isomerase
 1-315 0e+00

triosephosphate isomerase


:

Pssm-ID: 166070  Cd Length: 315  Bit Score: 584.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429    1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429   81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429  161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063704338 241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
Cdd:PLN02429  241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
 
Name Accession Description Interval E-value
PLN02429 PLN02429
triosephosphate isomerase
 1-315 0e+00

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 584.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429    1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429   81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429  161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063704338 241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
Cdd:PLN02429  241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 66-306 8.81e-126

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: 359.16  E-value: 8.81e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  66 FFVGGNWKCNGTKDSIAKLISDLNSAT-LEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVLkDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVA 223
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFLD 239


                  ...
gi 1063704338 304 IVN 306
Cdd:cd00311   240 IIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 66-308 1.00e-119

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: 344.11  E-value: 1.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  66 FFVGGNWKCNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALAdESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 145 DLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD-NIVVA 223
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFLD 239


                  ....*
gi 1063704338 304 IVNSV 308
Cdd:pfam00121 240 IINAA 244
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 65-307 7.91e-117

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: 336.64  E-value: 7.91e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLE-ADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:COG0149     3 KPLIAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAAM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPS--WDNI 220
Cdd:COG0149    83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAeqAANV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:COG0149   163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAED 242


                  ....*..
gi 1063704338 301 FATIVNS 307
Cdd:COG0149   243 FLAIVRA 249
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 67-297 1.12e-61

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: 195.02  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  67 FVGGNWK-CNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLtdRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVAsEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 145 DLGCKWVILGHSERRHvigeKDEFIGKKAAYALSEGLGVIACIGEKLEEReagktfdvcfaqlkafadAVPSWDNIVVAY 224
Cdd:TIGR00419  79 DIGAKGTLINHSERRM----KLADIEKKIARLKELGLTSVVCTNNVLTTA------------------AAAALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063704338 225 EPVWAIGTGKVASPQQAQEVHVAVRgwlkknVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLK 297
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLK 203
 
Name Accession Description Interval E-value
PLN02429 PLN02429
triosephosphate isomerase
 1-315 0e+00

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 584.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429    1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429   81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429  161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063704338 241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
Cdd:PLN02429  241 AQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSKKVAA 315
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 61-312 5.26e-129

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 368.09  E-value: 5.26e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  61 AGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEAD-VDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEI 138
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNnVDVVVAPPSLHIPLVQEKLKNkNFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 139 SVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP--S 216
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSdeA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 217 WDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASL 296
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|....*.
gi 1063704338 297 KgPEFATIVNSVTSKK 312
Cdd:PTZ00333  241 K-PDFVDIIKSAEQSK 255
PLN02561 PLN02561
triosephosphate isomerase
 65-312 5.00e-126

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 360.29  E-value: 5.00e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGNWKCNGTKDSIAKLISDLNSATL--EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:PLN02561    4 KFFVGGNWKCNGTVEEVKKIVTTLNEAEVpsEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISAEM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222
Cdd:PLN02561   84 LVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVVL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302
Cdd:PLN02561  164 AYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLK-PEFI 242

                         250
                  ....*....|
gi 1063704338 303 TIVNSVTSKK 312
Cdd:PLN02561  243 DIIKSATVKK 252
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 66-306 8.81e-126

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: 359.16  E-value: 8.81e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  66 FFVGGNWKCNGTKDSIAKLISDLNSAT-LEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVLkDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVA 223
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFLD 239


                  ...
gi 1063704338 304 IVN 306
Cdd:cd00311   240 IIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 66-308 1.00e-119

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: 344.11  E-value: 1.00e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  66 FFVGGNWKCNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALAdESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 145 DLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD-NIVVA 223
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFLD 239


                  ....*
gi 1063704338 304 IVNSV 308
Cdd:pfam00121 240 IINAA 244
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 65-307 7.91e-117

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: 336.64  E-value: 7.91e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLE-ADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:COG0149     3 KPLIAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAAM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPS--WDNI 220
Cdd:COG0149    83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAeqAANV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:COG0149   163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAED 242


                  ....*..
gi 1063704338 301 FATIVNS 307
Cdd:COG0149   243 FLAIVRA 249
tpiA PRK00042
triosephosphate isomerase; Provisional
 65-306 1.74e-112

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 325.92  E-value: 1.74e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGNWKCNGTKDSIAKLISDLNSA-TLEADVDVVVSPPFVYIDQVKSSL-TDRIDISGQN-SWVGKGgAFTGEISVE 141
Cdd:PRK00042    2 KPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALkGSNIKLGAQNvHPEDSG-AFTGEISAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 142 QLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD--N 219
Cdd:PRK00042   81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQfaN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGP 299
Cdd:PRK00042  161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239


                  ....*..
gi 1063704338 300 EFATIVN 306
Cdd:PRK00042  240 DFLAIVK 246
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 65-309 1.80e-86

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 271.99  E-value: 1.80e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSL-TDRIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:PRK13962  398 KPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVdGSNIKLGAQNVFYEEKGAYTGEISGPML 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD--NIV 221
Cdd:PRK13962  478 AEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQvkKVV 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 222 VAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEF 301
Cdd:PRK13962  558 IAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAQEF 637


                  ....*...
gi 1063704338 302 ATIVNSVT 309
Cdd:PRK13962  638 AAIANYFI 645
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 67-297 1.12e-61

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: 195.02  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  67 FVGGNWK-CNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLtdRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVAsEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 145 DLGCKWVILGHSERRHvigeKDEFIGKKAAYALSEGLGVIACIGEKLEEReagktfdvcfaqlkafadAVPSWDNIVVAY 224
Cdd:TIGR00419  79 DIGAKGTLINHSERRM----KLADIEKKIARLKELGLTSVVCTNNVLTTA------------------AAAALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063704338 225 EPVWAIGTGKVASPQQAQEVHVAVRgwlkknVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLK 297
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLK 203
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 66-308 1.44e-58

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 188.04  E-value: 1.44e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  66 FFVGGNWKCNGTKDSIAKLISDLN--SATLEADVDVVVSPPFVyidqVKSSLTDR---IDISGQNSWVGKGGAFTGEISV 140
Cdd:PRK14565    3 FLIVANWKMNGDFSLFSSFLKELSnkLANNEITLKLVICPPFT----AMSSFVECnpnIKLGAQNCFYGSSGGYTGEISA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 141 EQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKafaDAVPSWDNI 220
Cdd:PRK14565   79 KMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGEF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWlkknvseevASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:PRK14565  156 IIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDS 226


                  ....*...
gi 1063704338 301 FATIVNSV 308
Cdd:PRK14565  227 FCKIIQQV 234
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 65-308 1.19e-37

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 137.09  E-value: 1.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGN---WKCNG-TKDSIAKLISDLNSATLEADVDVVVSPPFVY----IDQVKSSLT-DRIDISGQNSWVGKGGAFT 135
Cdd:PRK14905    4 KIYFGTNlkmYKGNAeTVDYLSELLAFAEKFKSDYDIELFVIPSYIAlkdaVEAAASETGhPKIKIGAQNMNAKDKGQFT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 136 GEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP 215
Cdd:PRK14905   84 GEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 216 S--WDNIVVAYEPVWAIGTGKV-ASPQQAQEVHVAVRGWLKKNVSEEvASKTRIIYGGSVNGGNSAELAKEEDIDGFLVG 292
Cdd:PRK14905  164 AeqLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGLFIG 242

                         250
                  ....*....|....*.
gi 1063704338 293 GASLKGPEFATIVNSV 308
Cdd:PRK14905  243 RSAWDAQCFHALIADA 258
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 65-311 2.19e-35

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 128.57  E-value: 2.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  65 KFFVGGN---WKCNG-TKDSIAKLISDLNSATLEADVDVVVSPPFVYI-DQVKSSLT----DRIDISGQNSWVGKGGAFT 135
Cdd:PRK15492    3 KIYFGTNlkmYKGIAdATDFLAKLSELADDIPADKDIELFVIPSFTAIqDAIAATLAiphdHPIIIGAQNMNPNDNGQFT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 136 GEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP 215
Cdd:PRK15492   83 GDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGIN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 216 S--WDNIVVAYEPVWAIGTGKV-ASPQQAQEVHVAVRGWLKKNVSEEvASKTRIIYGGSVNGGNSAELAKEEDIDGFLVG 292
Cdd:PRK15492  163 PdqLAKLRIAYEPVWAIGEAGIpASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPHIDGLFIG 241

                         250
                  ....*....|....*....
gi 1063704338 293 GASLKGPEFATIVNSVTSK 311
Cdd:PRK15492  242 RSAWDADKFFAIIEGILNK 260
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 81-311 1.49e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 57.18  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338  81 IAKLISDLNSatlEADVDVVVSPPFVYIDQVKSSLTdrIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PRK04302   24 IAKAAEKVSK---ETGVRIAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704338 161 VIGEkdefIGKKAAYALSEGLGVIACigekleereagkTFDVcfAQLKAFADAVPSWdnivVAYEPVWAIGTGKVASPQQ 240
Cdd:PRK04302   99 TLAD----IEAVVERAKKLGLESVVC------------VNNP--ETSAAAAALGPDY----VAVEPPELIGTGIPVSKAK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063704338 241 AQEVHVAVrgwlkkNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSK 311
Cdd:PRK04302  157 PEVVEDAV------EAVKKVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKDPEAALRDLVSP 221
 
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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