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Conserved domains on  [gi|19111848|ref|NP_595056|]
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adducin, involved in actin cytoskeleton organization [Schizosaccharomyces pombe]

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

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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 ...
 8-246 6.81e-86

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 PRK06208:

Pssm-ID: 469663  Cd Length: 274  Bit Score: 256.84  E-value: 6.81e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    8 PEFEDLHTKRkwmlnHMAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKm 87
Cdd:PRK06208  36 VAEERLHRKQ-----RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDR- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   88 KYNTSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLAD 167
Cdd:PRK06208 110 PLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEDHALFDDFTGVVVDTSEGRRIAAALGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111848  168 YKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQIQLLIDSAtkvGERKHVHPTRAKAIRENADNPVGLYTAQQPnfLYE 246
Cdd:PRK06208 190 HKAVILQNHGLLTVGPSVDAAAWWFIALERACQTQLLAEAA---GPPQPIDHETARHTRSQVGSEYGGWFNFQP--LYQ 263
 
Name Accession Description Interval E-value
PRK06208 PRK06208
class II aldolase/adducin family protein;
8-246 6.81e-86

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 256.84  E-value: 6.81e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    8 PEFEDLHTKRkwmlnHMAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKm 87
Cdd:PRK06208  36 VAEERLHRKQ-----RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDR- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   88 KYNTSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLAD 167
Cdd:PRK06208 110 PLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEDHALFDDFTGVVVDTSEGRRIAAALGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111848  168 YKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQIQLLIDSAtkvGERKHVHPTRAKAIRENADNPVGLYTAQQPnfLYE 246
Cdd:PRK06208 190 HKAVILQNHGLLTVGPSVDAAAWWFIALERACQTQLLAEAA---GPPQPIDHETARHTRSQVGSEYGGWFNFQP--LYQ 263
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 24-227 1.02e-60

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: 190.43  E-value: 1.02e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  24 MAAAFRMFGRNGYNEGTAGHVTVRdpIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMkyNTSGFAIHYEMHKV 103
Cdd:COG0235  10 LAAAGRRLARRGLVDGTAGNISVR--LDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLK--PSSETPLHLAIYRA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848 104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTD-CCVFYNNHGIYFDMDdvISMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:COG0235  86 RPDVGAVVHTHSPYATALSALGEPLPPLEQTeAAAFLGDVPVVPYAG--PGTEELAEAIAEALGDRPAVLLRNHGVVVWG 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19111848 183 TTVDEAAYLLSLMERSCQIQLLIDSAtkvGERKHVHPTRAKAIRE 227
Cdd:COG0235 164 KDLAEAFDRAEVLEEAARIQLLALAL---GGPLVLSDEEIDKLAR 205
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 24-203 9.57e-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: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 177.06  E-value: 9.57e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848     24 MAAAFRMFGRNGYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKV 103
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTD-CCVFYNNHGIYFDMDDVIS-----MPEEGRRTAKGLADYKAVLVQNHG 177
Cdd:smart01007  80 RPDVGAVVHTHSPYATALAALGKPLPLLPTEqAAAFLGGEIPYAPYAGPGTelaeeGAELAEALAEALPDRPAVLLRNHG 159

                          170       180
                   ....*....|....*....|....*.
gi 19111848    178 IMTVGTTVDEAAYLLSLMERSCQIQL 203
Cdd:smart01007 160 LLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 22-203 9.95e-55

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: 173.89  E-value: 9.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    22 NHMAAAFRMFGRNGYNEGTAGHVTVRDPidENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGskMKYNTSGFAIHYEMH 101
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP--GDGFLITPSGVDFGELTPEDLVVVDLDGNVVEG--GLKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   102 KVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDmDDVISMPEEGRRTAKGL-ADYKAVLVQNHGIMT 180
Cdd:pfam00596  77 RARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIP-YYTPGTEELGERIAEALgGDRKAVLLRNHGLLV 155

                         170       180
                  ....*....|....*....|...
gi 19111848   181 VGTTVDEAAYLLSLMERSCQIQL 203
Cdd:pfam00596 156 WGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 19-203 3.63e-37

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: 130.18  E-value: 3.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  19 WMLNHMAAAFRMFGRNGYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKmkyNTSGFAIHY 98
Cdd:cd00398   2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDR-DRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK---PSSETPLHL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  99 EMHKVRPEVICVCHVHSIYGKAFSALGK-PLDMLNTDCCV-FYNNHGIYFDMddVISMPEEGRRT--AKGLADYKAVLVQ 174
Cdd:cd00398  78 ALYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVyFTGDIPCTPYM--TPETGEDEIGTqrALGFPNSKAVLLR 155

                       170       180
                ....*....|....*....|....*....
gi 19111848 175 NHGIMTVGTTVDEAAYLLSLMERSCQIQL 203
Cdd:cd00398 156 NHGLFAWGPTLDEAFHLAVVLEVAAEIQL 184
 
Name Accession Description Interval E-value
PRK06208 PRK06208
class II aldolase/adducin family protein;
8-246 6.81e-86

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 256.84  E-value: 6.81e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    8 PEFEDLHTKRkwmlnHMAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKm 87
Cdd:PRK06208  36 VAEERLHRKQ-----RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVEGDR- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   88 KYNTSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLAD 167
Cdd:PRK06208 110 PLNRAAFAIHSAIHEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEDHALFDDFTGVVVDTSEGRRIAAALGT 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111848  168 YKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQIQLLIDSAtkvGERKHVHPTRAKAIRENADNPVGLYTAQQPnfLYE 246
Cdd:PRK06208 190 HKAVILQNHGLLTVGPSVDAAAWWFIALERACQTQLLAEAA---GPPQPIDHETARHTRSQVGSEYGGWFNFQP--LYQ 263
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 24-227 1.02e-60

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: 190.43  E-value: 1.02e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  24 MAAAFRMFGRNGYNEGTAGHVTVRdpIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMkyNTSGFAIHYEMHKV 103
Cdd:COG0235  10 LAAAGRRLARRGLVDGTAGNISVR--LDDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLK--PSSETPLHLAIYRA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848 104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTD-CCVFYNNHGIYFDMDdvISMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:COG0235  86 RPDVGAVVHTHSPYATALSALGEPLPPLEQTeAAAFLGDVPVVPYAG--PGTEELAEAIAEALGDRPAVLLRNHGVVVWG 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19111848 183 TTVDEAAYLLSLMERSCQIQLLIDSAtkvGERKHVHPTRAKAIRE 227
Cdd:COG0235 164 KDLAEAFDRAEVLEEAARIQLLALAL---GGPLVLSDEEIDKLAR 205
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 24-203 9.57e-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: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 177.06  E-value: 9.57e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848     24 MAAAFRMFGRNGYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKV 103
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGPKPSSETPLHLAIYRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTD-CCVFYNNHGIYFDMDDVIS-----MPEEGRRTAKGLADYKAVLVQNHG 177
Cdd:smart01007  80 RPDVGAVVHTHSPYATALAALGKPLPLLPTEqAAAFLGGEIPYAPYAGPGTelaeeGAELAEALAEALPDRPAVLLRNHG 159

                          170       180
                   ....*....|....*....|....*.
gi 19111848    178 IMTVGTTVDEAAYLLSLMERSCQIQL 203
Cdd:smart01007 160 LLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 22-203 9.95e-55

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: 173.89  E-value: 9.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848    22 NHMAAAFRMFGRNGYNEGTAGHVTVRDPidENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGskMKYNTSGFAIHYEMH 101
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLP--GDGFLITPSGVDFGELTPEDLVVVDLDGNVVEG--GLKPSSETPLHLAIY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   102 KVRPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDmDDVISMPEEGRRTAKGL-ADYKAVLVQNHGIMT 180
Cdd:pfam00596  77 RARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFLGGDIPIIP-YYTPGTEELGERIAEALgGDRKAVLLRNHGLLV 155

                         170       180
                  ....*....|....*....|...
gi 19111848   181 VGTTVDEAAYLLSLMERSCQIQL 203
Cdd:pfam00596 156 WGKTLEEAFYLAEELERAAEIQL 178
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 25-230 1.31e-40

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 140.37  E-value: 1.31e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   25 AAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKVR 104
Cdd:PRK07044  22 AAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDDSPYPVNPAGFTIHSAIHAAR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  105 PEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGiYFDMDDVISMPEEGRRTAKGLADYKAVLVQNHGIMTVGTT 184
Cdd:PRK07044 102 PDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFYGRLA-YHDYEGIALDLDEGERLVADLGDKPAMLLRNHGLLTVGRT 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 19111848  185 VDEAAYLLSLMERSCQIQLlidsATKVGERKHVHPTRAKAIRENAD 230
Cdd:PRK07044 181 VAEAFLLMYTLERACEIQV----AAQAGGGELVLPPPEVAERTARQ 222
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 19-203 3.63e-37

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: 130.18  E-value: 3.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  19 WMLNHMAAAFRMFGRNGYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKmkyNTSGFAIHY 98
Cdd:cd00398   2 KLKRKIIAACLLLDLYGWVTGTGGNVSARDR-DRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKK---PSSETPLHL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  99 EMHKVRPEVICVCHVHSIYGKAFSALGK-PLDMLNTDCCV-FYNNHGIYFDMddVISMPEEGRRT--AKGLADYKAVLVQ 174
Cdd:cd00398  78 ALYRARPDIGCIVHTHSTHATAVSQLKEgLIPAGHTACAVyFTGDIPCTPYM--TPETGEDEIGTqrALGFPNSKAVLLR 155

                       170       180
                ....*....|....*....|....*....
gi 19111848 175 NHGIMTVGTTVDEAAYLLSLMERSCQIQL 203
Cdd:cd00398 156 NHGLFAWGPTLDEAFHLAVVLEVAAEIQL 184
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 24-223 1.05e-30

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 114.73  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   24 MAAAFRMFGRNGYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFaiHYEMHKV 103
Cdd:PRK07090  35 LALTCRILFDAGHDSGLAGQITARAE-APGTYYTQRLGLGFDEITASNLLLVDEDLNVLDGEGMPNPANRF--HSWIYRA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLADYKAVLVQNHGIMTVGT 183
Cdd:PRK07090 112 RPDVNCIIHTHPPHVAALSMLEVPLVVSHMDTCPLYDDCAFLKDWPGVPVGNEEGEIISAALGDKRAILLSHHGQLVAGK 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19111848  184 TVDEAAYLLSLMERSCQIQLLidsATKVGERKHVHPTRAK 223
Cdd:PRK07090 192 SIEEACVLALLIERAARLQLL---AMAAGPIKPIPPELAR 228
PRK07490 PRK07490
hypothetical protein; Provisional
 24-204 9.63e-30

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 111.74  E-value: 9.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   24 MAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKV 103
Cdd:PRK07490  15 LAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLDADDPSTAERPDVPDATAWAIHGQIHRR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  104 RPEVICVCHVHSIYGKAFSALGKP-LDMLNTDCCVFYNNHGIyfDMD-DVISMPEEGRRTAKGLADYKAVLVQNHGIMTV 181
Cdd:PRK07490  95 LPHARCVMHVHSVYATALACLADPtLPPIDQNTARFFNRVAV--DTLyGGMALEEEGERLAGLLGDKRRLLMGNHGVLVT 172

                        170       180
                 ....*....|....*....|...
gi 19111848  182 GTTVDEAAYLLSLMERSCQIQLL 204
Cdd:PRK07490 173 GDTVAEAFDDLYYFERACQTYIT 195
PRK06661 PRK06661
hypothetical protein; Provisional
 24-210 3.05e-27

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 104.91  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   24 MAAAFRMFGRNGYNEGTAGHVTVRdPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKV 103
Cdd:PRK06661   7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILEGEEYQYNKTGYFIHGSIYKT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  104 RPEVICVCHVHSIYGKAFSALGKPLDMLNTDCCVFYNNHGiYFDMDD-VISMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:PRK06661  86 RPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDRIS-YHNYNSlALDADKQSSRLVNDLKQNYVMLLRNHGAITCG 164

                        170       180
                 ....*....|....*....|....*...
gi 19111848  183 TTVDEAAYLLSLMERSCQIQLLIDSATK 210
Cdd:PRK06661 165 KTIHEAMFYTYHLEQACKTQCLLNSTKK 192
PRK06486 PRK06486
aldolase;
24-204 5.17e-25

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 99.79  E-value: 5.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   24 MAAAFRMFGRNGYNEGTAGHVTVRDPIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSgFAIHYEMHKV 103
Cdd:PRK06486  31 LAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVLAGRGEPEATA-FFIHARIHRA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  104 RPEVICVCHVHSIYGKAFSAL-GKPLDMLNTDCCVFYNNHGIYFDMDDVISMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:PRK06486 110 IPRAKAAFHTHMPYATALSLTeGRPLTTLGQTALKFYGRTAVDEDYNGLALDAAEGDRIARAMGDADIVFLKNHGVMVCG 189

                        170       180
                 ....*....|....*....|..
gi 19111848  183 TTVDEAAYLLSLMERSCQIQLL 204
Cdd:PRK06486 190 PRIAEAWDDLYYLERACEVQVL 211
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 40-188 2.90e-18

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 80.82  E-value: 2.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   40 TAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKynTSGFAIHYEMHKVRPEVICVCHVHSIYGK 119
Cdd:PRK06557  31 TSGNVSARDP-GTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEGDLKP--SSDTASHLYVYRHMPDVGGVVHTHSTYAT 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  120 AFSALGKPLDMLNTdccvfynnhgiyfDMDDVISMP------------EEGRRTAKGLADYK--AVLVQNHGIMTVGTTV 185
Cdd:PRK06557 108 AWAARGEPIPCVLT-------------AMADEFGGPipvgpfaligdeAIGKGIVETLKGGRspAVLMQNHGVFTIGKDA 174


                 ...
gi 19111848  186 DEA 188
Cdd:PRK06557 175 EDA 177
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
32-191 5.36e-17

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 77.09  E-value: 5.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   32 GRNGYNEGTAGHVTVRDpidENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGskmKYNTSGFAIHYEMHKVRPEVICVC 111
Cdd:PRK08087  18 TRLGLNQGTAGNVSVRY---QDGMLITPTGIPYEKLTESHIVFVDGNGKHEEG---KLPSSEWRFHMAAYQTRPDANAVV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  112 HVHSIYGKAFSALGKPLDML---------NTDCCVFYNNHGiyfdmddvisMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:PRK08087  92 HNHAVHCTAVSILNRPIPAIhymiaaaggNSIPCAPYATFG----------TRELSEHVALALKNRKATLLQHHGLIACE 161


                 ....*....
gi 19111848  183 TTVDEAAYL 191
Cdd:PRK08087 162 VNLEKALWL 170
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 24-201 2.01e-16

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 75.45  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   24 MAAAFRMFgRNGYNEGTAGHVTVRDPiDENTFwINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKYNTSGFAIHYEMHKV 103
Cdd:PRK05874  12 LAAAKDML-RRGLVEGTAGNISARRS-DGNVV-ITPSSVDYAEMLLHDLVLVDAGGAVLHAKDGRSPSTELNLHLACYRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  104 RPEVICVCHVHSIYGKAFSALGKPL----DMLNTDC-----CVFYNNHGiyfdmddvisMPEEGRRTAKGLADYKAVLVQ 174
Cdd:PRK05874  89 FDDIGSVIHSHPVWATMFAVAHEPIpaciDEFAIYCggdvrCTEYAASG----------TPEVGRNAVRALEGRAAALIA 158

                        170       180
                 ....*....|....*....|....*..
gi 19111848  175 NHGIMTVGTTVDEAAYLLSLMERSCQI 201
Cdd:PRK05874 159 NHGLVAVGPRPDQVLRVTALVERTAQI 185
PRK08130 PRK08130
putative aldolase; Validated
 30-208 4.40e-11

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 60.66  E-value: 4.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   30 MFGRnGYNEGTAGHVTVRdpIDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKmkyNTSGFAIHYEMHKVRPEVIC 109
Cdd:PRK08130  17 LFQR-GYTVGSAGNISAR--LDDGGWLVTPTGSCLGRLDPARLSKVDADGNWLSGDK---PSKEVPLHRAIYRNNPECGA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  110 VCHVHSIYGKAFSALGKpLDmlNTDCcvfynnhgI-----YFDMD----DVISM-----PEEGRRTAKGLADYKAVLVQN 175
Cdd:PRK08130  91 VVHLHSTHLTALSCLGG-LD--PTNV--------LppftpYYVMRvghvPLIPYyrpgdPAIAEALAGLAARYRAVLLAN 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 19111848  176 HGIMTVGTTVDEAAYL---------LSLMERSCQIQLLIDSA 208
Cdd:PRK08130 160 HGPVVWGSSLEAAVNAteeleetakLILLLGGRPPRYLTDEE 201
PRK08333 PRK08333
aldolase;
67-201 6.57e-11

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 59.84  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   67 MKPSDLVHINSDGEIIGGSKmkyNTSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSA-LGKPLDMLNTDCCVFynnhgiy 145
Cdd:PRK08333  48 LTREQVAVIDLNGNQLSSVR---PSSEYRLHLAVYRNRPDVRAIAHLHPPYSIVASTlLEEELPIITPEAELY------- 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19111848  146 fdMDDVISMP-------EEGRRTAKGLADYKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQI 201
Cdd:PRK08333 118 --LKKIPILPfrpagsvELAEQVAEAMKEYDAVIMERHGIVTVGRSLREAFYKAELVEESAKL 178
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
35-188 9.19e-10

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 57.07  E-value: 9.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   35 GYNEGTAGHVTVRDPiDENTFWINPLEVPFSLMKPSDLVHINSDGEIIGGSKMKyntsgfAIHYEMHKV----RPEVICV 110
Cdd:PRK06833  21 GLTKGTGGNISIFNR-EQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVEGERKP------SSELDMHLIfyrnREDINAI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  111 CHVHSIYGKAFSALGKPLDMLN-------TDC-CVFYNNHGiyfdmddvisMPEEGRRTAKGLADYKAVLVQNHGIMTVG 182
Cdd:PRK06833  94 VHTHSPYATTLACLGWELPAVHyliavagPNVrCAEYATFG----------TKELAENAFEAMEDRRAVLLANHGLLAGA 163


                 ....*.
gi 19111848  183 TTVDEA 188
Cdd:PRK06833 164 NNLKNA 169
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
50-216 4.24e-07

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 49.45  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   50 IDENT--FWINPLEVPFSLMKPSDLVHINSDGEIIGGskmKYN-TSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGK 126
Cdd:PRK08193  32 IDRERglFVIKPSGVDYDKMTAEDMVVVDLEGNVVEG---KLKpSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWAQAGR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  127 PLDMLNTdccvfynNHGIYF--------DMDD-------------VISmpEEGRRTAKGLADYKAVLVQNHGIMTVGTTV 185
Cdd:PRK08193 109 DIPALGT-------THADYFygdipctrKMTDeeingeyewetgkVIV--ETFEKRGIDPAAVPGVLVHSHGPFTWGKDA 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 19111848  186 DEAAYLLSLMERSCQI---------------QLLIDsatKVGERKH 216
Cdd:PRK08193 180 EDAVHNAVVLEEVAKMayftrqlnpqlpdmqQTLLD---KHYLRKH 222
PRK03634 PRK03634
rhamnulose-1-phosphate aldolase; Provisional
 72-207 2.03e-06

rhamnulose-1-phosphate aldolase; Provisional


Pssm-ID: 179615 [Multi-domain]  Cd Length: 274  Bit Score: 47.67  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   72 LVHINSDG---EII-GGSKMKYNTSGFAIHYEMHKVR-----PEVICVCHVHSIYGKAFSALgKPLD----------MLn 132
Cdd:PRK03634  92 VIRIDSDGagyHILwGLTNGGKPTSELPAHLMSHIARlkatnGKDRVIMHCHATNLIALTYV-LELDeavftrtlweMS- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  133 TDCCVFYNNhGIyfdmdDVIS--MP---EEGRRTAKGLADYKAVLVQNHGIMTVGTTVDEAAYLLSLMERSCQIQLLIDS 207
Cdd:PRK03634 170 TECLVVFPD-GV-----GIVPwmVPgtdEIGQATAEKMQKHDLVLWPKHGVFGSGPTLDEAFGLIDTAEKSAEIYVKVLS 243
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 57-149 3.89e-06

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 46.72  E-value: 3.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848   57 INPLEVPFSLMKPSDLVHINSDGEIIGGskmKYN-TSGFAIHYEMHKVRPEVICVCHVHSIYGKAFSALGKPLDMLNTdc 135
Cdd:PRK12348  40 IKPSGVAYETMKADDMVVVDMSGKVVEG---EYRpSSDTATHLELYRRYPSLGGIVHTHSTHATAWAQAGLAIPALGT-- 114

                         90
                 ....*....|....
gi 19111848  136 cvfynNHGIYFDMD 149
Cdd:PRK12348 115 -----THADYFFGD 123
PRK08660 PRK08660
aldolase;
109-210 9.98e-05

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 41.87  E-value: 9.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111848  109 CVCHVHSIYGKAFSALG---KPLDmlntdccvfynNHGIYFdMDDV------ISMPEEGRRTAKGLADYKAVLVQNHGIM 179
Cdd:PRK08660  83 AIVHAHPPYAVALSLLEdeiVPLD-----------SEGLYF-LGTIpvvggdIGSGELAENVARALSEHKGVVVRGHGTF 150

                         90       100       110
                 ....*....|....*....|....*....|.
gi 19111848  180 TVGTTVDEAAYLLSLMERSCQIQLLIDSATK 210
Cdd:PRK08660 151 AIGKTLEEAYIYTSQLEHSCKVLYLVRTAKK 181
 
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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