NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1241781194|ref|NP_001341687|]
View 

alpha-adducin isoform c [Homo sapiens]

Protein Classification

class II aldolase/adducin head domain-containing protein( domain architecture ID 842)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 145-391 1.11e-99

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


The actual alignment was detected with superfamily member PRK07044:

Pssm-ID: 469663  Cd Length: 252  Bit Score: 304.46  E-value: 1.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                         250
                  ....*....|
gi 1241781194 384 LD--NLGYRT 391
Cdd:PRK07044  243 LDriDPGYRD 252
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 1.11e-99

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.46  E-value: 1.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                         250
                  ....*....|
gi 1241781194 384 LD--NLGYRT 391
Cdd:PRK07044  243 LDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 142-352 6.83e-69

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 222.63  E-value: 6.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398    75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1241781194 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 4.28e-58

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 194.28  E-value: 4.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235     6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235    80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1241781194 303 GLVSVGESVEEAFYYIHNLVVACEIQVRTLAsAGGPDNL 341
Cdd:COG0235   158 GVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 147-329 3.26e-56

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 188.14  E-value: 3.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1241781194 305 VSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 149-329 1.18e-53

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 181.68  E-value: 1.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194  149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194  229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1241781194  302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 145-391 1.11e-99

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.46  E-value: 1.11e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGtgsppkwqIGEQEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAG--------AGELAWPALLRK 242

                         250
                  ....*....|
gi 1241781194 384 LD--NLGYRT 391
Cdd:PRK07044  243 LDriDPGYRD 252
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 142-352 6.83e-69

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 222.63  E-value: 6.83e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLGvnqa 219
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398    75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1241781194 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 145-341 4.28e-58

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 194.28  E-value: 4.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnlGVNQAGFTLH 224
Cdd:COG0235     6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235    80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1241781194 303 GLVSVGESVEEAFYYIHNLVVACEIQVRTLAsAGGPDNL 341
Cdd:COG0235   158 GVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 147-329 3.26e-56

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 188.14  E-value: 3.26e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1241781194 305 VSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 149-329 1.18e-53

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 181.68  E-value: 1.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194  149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194  229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1241781194  302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06661 PRK06661
hypothetical protein; Provisional
 149-334 6.57e-44

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 156.92  E-value: 6.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 149 LAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgSTNLGVNQAGFTLHSAIY 228
Cdd:PRK06661    7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 229 AARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE-VAYHDYHGILVDEE-EKVLIQKNLGpKSKVLILRNHGLVS 306
Cdd:PRK06661   84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSLALDADkQSSRLVNDLK-QNYVMLLRNHGAIT 162

                         170       180
                  ....*....|....*....|....*...
gi 1241781194 307 VGESVEEAFYYIHNLVVACEIQVRTLAS 334
Cdd:PRK06661  163 CGKTIHEAMFYTYHLEQACKTQCLLNST 190
PRK06208 PRK06208
class II aldolase/adducin family protein;
148-361 3.64e-42

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 153.61  E-value: 3.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 148 KLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrgsTNLGVNQAGFTLHSAI 227
Cdd:PRK06208   46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 228 YAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE--VAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHGLV 305
Cdd:PRK06208  123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEdhALFDDFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1241781194 306 SVGESVEEA-FYYIhNLVVACEIQVrtLASAGGPdnLVLLNPEKYKAKSRSPGSPVG 361
Cdd:PRK06208  202 TVGPSVDAAaWWFI-ALERACQTQL--LAEAAGP--PQPIDHETARHTRSQVGSEYG 253
PRK06486 PRK06486
aldolase;
114-385 1.06e-26

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 109.42  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 114 MA-ALNMSLGMVTPVNDLRGSDSIAYdkgeklLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEV 192
Cdd:PRK06486    1 MAhSLTTDSAPPAGNRPLLDSDAVAQ------ARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 193 TASSLVKINLQGDIVD-RGStnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMK-CGLLPISPEALSL-GEVA 269
Cdd:PRK06486   75 TASDLLICDFDGNVLAgRGE----PEATAFFIHARIHRAIPRAKAAFHTHMPYATALSLTEgRPLTTLGQTALKFyGRTA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 270 Y-HDYHGILVDEEEKVLIQKNLGPKSkVLILRNHGLVSVGESVEEAF---YYihnLVVACEIQVRTLaSAGGPdnLVLLN 345
Cdd:PRK06486  151 VdEDYNGLALDAAEGDRIARAMGDAD-IVFLKNHGVMVCGPRIAEAWddlYY---LERACEVQVLAM-STGRP--LVPVD 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1241781194 346 PEKYKAKSRspgspvgegtgsppKWQIGEQE-----FEALMRMLD 385
Cdd:PRK06486  224 PAIAAAVAR--------------QMREGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
 135-385 2.13e-20

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 90.93  E-value: 2.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 135 SIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINlqGDIVDRGSTNL 214
Cdd:PRK07490    1 MTMALSDEEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD--ADDPSTAERPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 215 GVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCG-LLPISPE-ALSLGEVAYHDYHGILVDEEEKVLIQKNLGP 292
Cdd:PRK07490   79 VPDATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNtARFFNRVAVDTLYGGMALEEEGERLAGLLGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 293 KSkVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASaGGPdnLVLLNPEkykaksrspgspVGEGTGSppKWQ- 371
Cdd:PRK07490  159 KR-RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST-GQP--LRVLSDA------------VAEKTAR--DWEd 220

                         250
                  ....*....|....*..
gi 1241781194 372 ---IGEQEFEALMRMLD 385
Cdd:PRK07490  221 ypgFSRQHFAELKALLD 237
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 145-338 3.33e-19

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 87.77  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 145 LRCKLAAFYRLADLFGWSQLIYNHITTRvnSEQEH-FLIVPFGLLYSEVTASSLVKINLQGDIVD-RGSTNlGVNQagft 222
Cdd:PRK07090   31 LRQKLALTCRILFDAGHDSGLAGQITAR--AEAPGtYYTQRLGLGFDEITASNLLLVDEDLNVLDgEGMPN-PANR---- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 223 LHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAY-HDYHGILVDEEEKVLIQKNLGPKSKVLiLR 300
Cdd:PRK07090  104 FHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLVVSHMDTCPLyDDCAFlKDWPGVPVGNEEGEIISAALGDKRAIL-LS 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1241781194 301 NHGLVSVGESVEEAFYYIHNLVVACEIQVrtLASAGGP 338
Cdd:PRK07090  183 HHGQLVAGKSIEEACVLALLIERAARLQL--LAMAAGP 218
PRK08333 PRK08333
aldolase;
143-316 1.75e-13

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 69.08  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 143 KLLRCKLAAFYRLADLFGWSQLIYNHITTRVNseqEHFLIVPFGLLYSEVTASSLVKINLQGDIVD--RGSTNlgvnqag 220
Cdd:PRK08333    2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSE------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 221 FTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLP-ISPEA-LSLGEVAYHDYHGI----LVDEEEKVLIQKNlgpks 294
Cdd:PRK08333   72 YRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPiITPEAeLYLKKIPILPFRPAgsveLAEQVAEAMKEYD----- 146

                         170       180
                  ....*....|....*....|..
gi 1241781194 295 kVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08333  147 -AVIMERHGIVTVGRSLREAFY 167
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 176-314 2.10e-12

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 66.96  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 176 EQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTNLGVNQAGftlHSAIYAARPDVKCVVHIHTPAGAAVSA----M 251
Cdd:PRK06557   41 GTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDTAS---HLYVYRHMPDVGGVVHTHSTYATAWAArgepI 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1241781194 252 KCGLLPISPEAlsLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEA 314
Cdd:PRK06557  117 PCVLTAMADEF--GGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
PRK08130 PRK08130
putative aldolase; Validated
 179-316 8.11e-08

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 53.34  E-value: 8.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 179 HFLIVPFGLLYSEVTASSLVKINLQGDIV--DRGSTNLgvnqagfTLHSAIYAARPDVKCVVHIHTPAGAAVS------- 249
Cdd:PRK08130   38 GWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLTALSclggldp 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 250 -----------AMKCGLLPISPealslgevayhdYH--GilvDEEEKVLIQKnLGPKSKVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08130  111 tnvlppftpyyVMRVGHVPLIP------------YYrpG---DPAIAEALAG-LAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
174-338 4.04e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 51.29  E-value: 4.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 174 NSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKC 253
Cdd:PRK06833   34 NREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 254 GLLPISPE-ALSLGEVAYHDYHGI----LVDEEEKVLIQKnlgpksKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQ 328
Cdd:PRK06833  110 ELPAVHYLiAVAGPNVRCAEYATFgtkeLAENAFEAMEDR------RAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIY 183

                         170
                  ....*....|
gi 1241781194 329 VRTlASAGGP 338
Cdd:PRK06833  184 YQT-KSIGEP 192
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
177-333 2.76e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 48.58  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 177 QEHFLIVPFGLLYSEVTASSLVKINlqgdivDRGSTNLG-VNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGL 255
Cdd:PRK08087   35 QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEGkLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 256 --------------LPISPEAlSLG--EVAYHDYHGIlvdeeekvliqknlgPKSKVLILRNHGLVSVGESVEEAFYYIH 319
Cdd:PRK08087  109 paihymiaaaggnsIPCAPYA-TFGtrELSEHVALAL---------------KNRKATLLQHHGLIACEVNLEKALWLAH 172

                         170
                  ....*....|....
gi 1241781194 320 NLVVACEIQVRTLA 333
Cdd:PRK08087  173 EVEVLAQLYLKTLA 186
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 173-323 4.05e-05

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 45.59  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDrGSTNlgvNQAGFTLHSAIYAARPDVKCVVHIHTPAGA----AV 248
Cdd:PRK13145   33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVE-GDLN---PSSDLPTHVELYKAWPEVGGIVHTHSTEAVgwaqAG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 249 SAMKC----------GLLPISpEALSLGEV--AYHDYHGILVDEEEKvliQKNLGPKS-KVLILRNHGLVSVGESVEEAF 315
Cdd:PRK13145  109 RDIPFygtthadyfyGPIPCA-RSLTKDEVngAYEKETGSVIIEEFE---KRGLDPMAvPGIVVRNHGPFTWGKNPEQAV 184


                  ....*...
gi 1241781194 316 YyiHNLVV 323
Cdd:PRK13145  185 Y--HSVVL 190
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 173-327 5.00e-05

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 45.18  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVD---RGSTNLGVnqagftlHSAIYAARPDVKCVVHIHTP------ 243
Cdd:PRK12348   31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSSDTAT-------HLELYRRYPSLGGIVHTHSThatawa 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 244 -AGAAVSAMKC-------GLLPISpEALSLGEVAyHDYHgilvDEEEKVLIQkNLGPKSKV----LILRNHGLVSVGESV 311
Cdd:PRK12348  104 qAGLAIPALGTthadyffGDIPCT-RGLSEEEVQ-GEYE----LNTGKVIIE-TLGNAEPLhtpgIVVYQHGPFAWGKDA 176

                         170
                  ....*....|....*.
gi 1241781194 312 EEAfyyIHNLVVACEI 327
Cdd:PRK12348  177 HDA---VHNAVVMEEV 189
PRK08660 PRK08660
aldolase;
224-327 7.47e-03

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 38.01  E-value: 7.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1241781194 224 HSAIYAaRPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALS-LGE--VAYHDYHGILVDEEEKVLIQKNlgpksKVLILR 300
Cdd:PRK08660   72 HRAIYR-RTSAKAIVHAHPPYAVALSLLEDEIVPLDSEGLYfLGTipVVGGDIGSGELAENVARALSEH-----KGVVVR 145

                          90       100
                  ....*....|....*....|....*..
gi 1241781194 301 NHGLVSVGESVEEAFYYIHNLVVACEI 327
Cdd:PRK08660  146 GHGTFAIGKTLEEAYIYTSQLEHSCKV 172
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH