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Conserved domains on  [gi|300567625|emb|CBV15527|]
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unnamed protein product [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 300567625   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300567625 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 300567625   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300567625 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 300567625  66 FFVGGNWKCNGTKDSIAKLISDLNSAT-LEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLkDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVA 223
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFLD 239


                 ...
gi 300567625 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 300567625   66 FFVGGNWKCNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALAdESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  145 DLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD-NIVVA 223
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFLD 239


                  ....*
gi 300567625  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 300567625  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLE-ADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:COG0149    3 KPLIAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAAM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPS--WDNI 220
Cdd:COG0149   83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAeqAANV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:COG0149  163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAED 242


                 ....*..
gi 300567625 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 300567625   67 FVGGNWK-CNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLtdRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVAsEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  145 DLGCKWVILGHSERRHvigeKDEFIGKKAAYALSEGLGVIACIGEKLEEReagktfdvcfaqlkafadAVPSWDNIVVAY 224
Cdd:TIGR00419  79 DIGAKGTLINHSERRM----KLADIEKKIARLKELGLTSVVCTNNVLTTA------------------AAAALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300567625  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 300567625   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80
Cdd:PLN02429   1 MAATSLTAPPSFSGLRRISPKLDAAAVSSHQSFFHRVNSSTRLVSSSSSSHRSPRGVVAMAGSGKFFVGGNWKCNGTKDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PLN02429  81 IAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240
Cdd:PLN02429 161 VIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTGKVASPQQ 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300567625 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 300567625  61 AGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEAD-VDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEI 138
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNnVDVVVAPPSLHIPLVQEKLKNkNFKISSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 139 SVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP--S 216
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSdeA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 217 WDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASL 296
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|....*.
gi 300567625 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 300567625  65 KFFVGGNWKCNGTKDSIAKLISDLNSATL--EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:PLN02561   4 KFFVGGNWKCNGTVEEVKKIVTTLNEAEVpsEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISAEM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222
Cdd:PLN02561  84 LVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302
Cdd:PLN02561 164 AYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLK-PEFI 242

                        250
                 ....*....|
gi 300567625 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 300567625  66 FFVGGNWKCNGTKDSIAKLISDLNSAT-LEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLkDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVA 223
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFLD 239


                 ...
gi 300567625 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 300567625   66 FFVGGNWKCNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALAdESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  145 DLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD-NIVVA 223
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  224 YEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFAT 303
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFLD 239


                  ....*
gi 300567625  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 300567625  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLE-ADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQ 142
Cdd:COG0149    3 KPLIAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGsPIALGAQNVHWEDSGAYTGEISAAM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPS--WDNI 220
Cdd:COG0149   83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAeqAANV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:COG0149  163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAED 242


                 ....*..
gi 300567625 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 300567625  65 KFFVGGNWKCNGTKDSIAKLISDLNSA-TLEADVDVVVSPPFVYIDQVKSSL-TDRIDISGQN-SWVGKGgAFTGEISVE 141
Cdd:PRK00042   2 KPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALkGSNIKLGAQNvHPEDSG-AFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 142 QLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD--N 219
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQfaN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSeEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGP 299
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239


                 ....*..
gi 300567625 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 300567625  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSL-TDRIDISGQNSWVGKGGAFTGEISVEQL 143
Cdd:PRK13962 398 KPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVdGSNIKLGAQNVFYEEKGAYTGEISGPML 477

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 144 KDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWD--NIV 221
Cdd:PRK13962 478 AEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQvkKVV 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 222 VAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEF 301
Cdd:PRK13962 558 IAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAQEF 637


                 ....*...
gi 300567625 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 300567625   67 FVGGNWK-CNGTKDSIAKLISDLNSATL-EADVDVVVSPPFVYIDQVKSSLtdRIDISGQNSWVGKGGAFTGEISVEQLK 144
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVAsEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625  145 DLGCKWVILGHSERRHvigeKDEFIGKKAAYALSEGLGVIACIGEKLEEReagktfdvcfaqlkafadAVPSWDNIVVAY 224
Cdd:TIGR00419  79 DIGAKGTLINHSERRM----KLADIEKKIARLKELGLTSVVCTNNVLTTA------------------AAAALEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300567625  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 300567625  66 FFVGGNWKCNGTKDSIAKLISDLN--SATLEADVDVVVSPPFVyidqVKSSLTDR---IDISGQNSWVGKGGAFTGEISV 140
Cdd:PRK14565   3 FLIVANWKMNGDFSLFSSFLKELSnkLANNEITLKLVICPPFT----AMSSFVECnpnIKLGAQNCFYGSSGGYTGEISA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 141 EQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKafaDAVPSWDNI 220
Cdd:PRK14565  79 KMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGEF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 221 VVAYEPVWAIGTGKVASPQQAQEVHVAVRGWlkknvseevASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPE 300
Cdd:PRK14565 156 IIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDS 226


                 ....*...
gi 300567625 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 300567625  65 KFFVGGN---WKCNG-TKDSIAKLISDLNSATLEADVDVVVSPPFVY----IDQVKSSLT-DRIDISGQNSWVGKGGAFT 135
Cdd:PRK14905   4 KIYFGTNlkmYKGNAeTVDYLSELLAFAEKFKSDYDIELFVIPSYIAlkdaVEAAASETGhPKIKIGAQNMNAKDKGQFT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 136 GEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP 215
Cdd:PRK14905  84 GEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 216 S--WDNIVVAYEPVWAIGTGKV-ASPQQAQEVHVAVRGWLKKNVSEEvASKTRIIYGGSVNGGNSAELAKEEDIDGFLVG 292
Cdd:PRK14905 164 AeqLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGLFIG 242

                        250
                 ....*....|....*.
gi 300567625 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 300567625  65 KFFVGGN---WKCNG-TKDSIAKLISDLNSATLEADVDVVVSPPFVYI-DQVKSSLT----DRIDISGQNSWVGKGGAFT 135
Cdd:PRK15492   3 KIYFGTNlkmYKGIAdATDFLAKLSELADDIPADKDIELFVIPSFTAIqDAIAATLAiphdHPIIIGAQNMNPNDNGQFT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 136 GEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP 215
Cdd:PRK15492  83 GDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGIN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 216 S--WDNIVVAYEPVWAIGTGKV-ASPQQAQEVHVAVRGWLKKNVSEEvASKTRIIYGGSVNGGNSAELAKEEDIDGFLVG 292
Cdd:PRK15492 163 PdqLAKLRIAYEPVWAIGEAGIpASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPHIDGLFIG 241

                        250
                 ....*....|....*....
gi 300567625 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 300567625  81 IAKLISDLNSatlEADVDVVVSPPFVYIDQVKSSLTdrIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRH 160
Cdd:PRK04302  24 IAKAAEKVSK---ETGVRIAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300567625 161 VIGEkdefIGKKAAYALSEGLGVIACigekleereagkTFDVcfAQLKAFADAVPSWdnivVAYEPVWAIGTGKVASPQQ 240
Cdd:PRK04302  99 TLAD----IEAVVERAKKLGLESVVC------------VNNP--ETSAAAAALGPDY----VAVEPPELIGTGIPVSKAK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300567625 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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