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Conserved domains on  [gi|1622937148|ref|XP_028703877|]
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alpha-adducin isoform X5 [Macaca mulatta]

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 ...
145-391 1.87e-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: 304.85  E-value: 1.87e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGTGSLpkwqigeqEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGAGEL--------AWPALLRK 242
                         250
                  ....*....|
gi 1622937148 384 LD--NLGYRT 391
Cdd:PRK07044  243 LDriDPGYRD 252
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
521-624 3.74e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  521 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPATGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 597
Cdd:PHA03307   100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179
                           90       100
                   ....*....|....*....|....*....
gi 1622937148  598 EEAQRPPSP--TEAPTEASPEPAPDPAPV 624
Cdd:PHA03307   180 EETARAPSSppAEPPPSTPPAAASPRPPR 208
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
145-391 1.87e-99

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.85  E-value: 1.87e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGTGSLpkwqigeqEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGAGEL--------AWPALLRK 242
                         250
                  ....*....|
gi 1622937148 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 1.36e-68

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: 223.01  E-value: 1.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVV--DRGSTNLGvnqa 219
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398    75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622937148 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
145-341 4.20e-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: 195.05  E-value: 4.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGstnlGVNQAGFTLH 224
Cdd:COG0235     6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235    80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622937148 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 4.31e-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: 188.52  E-value: 4.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153
                         170       180
                  ....*....|....*....|....*
gi 1622937148 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 1.79e-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: 1.79e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157
                          170       180
                   ....*....|....*....|....*...
gi 1622937148  302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
521-624 3.74e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  521 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPATGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 597
Cdd:PHA03307   100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179
                           90       100
                   ....*....|....*....|....*....
gi 1622937148  598 EEAQRPPSP--TEAPTEASPEPAPDPAPV 624
Cdd:PHA03307   180 EETARAPSSppAEPPPSTPPAAASPRPPR 208
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
145-391 1.87e-99

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 304.85  E-value: 1.87e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrgSTNLGVNQAGFTLH 224
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVD--DSPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHG 303
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGDK-PAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 304 LVSVGESVEEAFYYIHNLVVACEIQVRTLaSAGGPdnLVLLNPEKYKAKSRSPGSPVGEGTGSLpkwqigeqEFEALMRM 383
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ-AGGGE--LVLPPPEVAERTARQSLFDPGAGAGEL--------AWPALLRK 242
                         250
                  ....*....|
gi 1622937148 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 1.36e-68

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: 223.01  E-value: 1.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 142 EKLLRcKLAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVV--DRGSTNLGvnqa 219
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSAR-DRDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETP---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 220 gftLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL---GEVAYHDYHGILvDEEEKVLIQKNLG-PKSK 295
Cdd:cd00398    75 ---LHLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPE-TGEDEIGTQRALGfPNSK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622937148 296 VLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGG--PDNLVLLNPEKYKAK 352
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQlpPISLELLNKEYLRKH 209
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
145-341 4.20e-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: 195.05  E-value: 4.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGstnlGVNQAGFTLH 224
Cdd:COG0235     6 LREELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGD----LKPSSETPLH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 225 SAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPIS-PEAL-SLGEVAYHDYHGIlVDEEEKVLIQKNLGpKSKVLILRNH 302
Cdd:COG0235    80 LAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEqTEAAaFLGDVPVVPYAGP-GTEELAEAIAEALG-DRPAVLLRNH 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622937148 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 4.31e-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: 188.52  E-value: 4.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 147 CKLAAFYRLADLFGWSQLIYNHITTRVnsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGstnLGVNqAGFTLHSA 226
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 227 IYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL--GEVAYHDYHGiLVDEEEKVLIQKNLGPKSKVLILRNHGL 304
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153
                         170       180
                  ....*....|....*....|....*
gi 1622937148 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 1.79e-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: 1.79e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  149 LAAFYRLADLFGWSQLIYNHITTRVNsEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDRGSTnlGVNQAGFTLHSAIY 228
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVG-EEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  229 AARPDVKCVVHIHTPAGAAVSAM--KCGLLPIS-PEALSLGEVAYHDYHGILVDEEEKV-LIQKNLGPK---SKVLILRN 301
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEqAAAFLGGEIPYAPYAGPGTELAEEGaELAEALAEAlpdRPAVLLRN 157
                          170       180
                   ....*....|....*....|....*...
gi 1622937148  302 HGLVSVGESVEEAFYYIHNLVVACEIQV 329
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
PRK06661 PRK06661
hypothetical protein; Provisional
149-334 2.35e-43

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 155.76  E-value: 2.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 149 LAAFYRLADLFGWSQLIYNHITTRvNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrgSTNLGVNQAGFTLHSAIY 228
Cdd:PRK06661    7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 229 AARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE-VAYHDYHGILVDEE-EKVLIQKNLGpKSKVLILRNHGLVS 306
Cdd:PRK06661   84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSLALDADkQSSRLVNDLK-QNYVMLLRNHGAIT 162
                         170       180
                  ....*....|....*....|....*...
gi 1622937148 307 VGESVEEAFYYIHNLVVACEIQVRTLAS 334
Cdd:PRK06661  163 CGKTIHEAMFYTYHLEQACKTQCLLNST 190
PRK06208 PRK06208
class II aldolase/adducin family protein;
148-361 1.22e-41

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 152.45  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 148 KLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrgsTNLGVNQAGFTLHSAI 227
Cdd:PRK06208   46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 228 YAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGE--VAYHDYHGILVDEEEKVLIQKNLGPKsKVLILRNHGLV 305
Cdd:PRK06208  123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFYEdhALFDDFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622937148 306 SVGESVEEA-FYYIhNLVVACEIQVrtLASAGGPdnLVLLNPEKYKAKSRSPGSPVG 361
Cdd:PRK06208  202 TVGPSVDAAaWWFI-ALERACQTQL--LAEAAGP--PQPIDHETARHTRSQVGSEYG 253
PRK06486 PRK06486
aldolase;
114-385 2.91e-27

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 111.34  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 114 MA-ALNMSLGMVTPVNDLRGSDSIAYdkgeklLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEV 192
Cdd:PRK06486    1 MAhSLTTDSAPPAGNRPLLDSDAVAQ------ARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 193 TASSLVKINLQGDVVD-RGStnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMK-CGLLPISPEALSL-GEVA 269
Cdd:PRK06486   75 TASDLLICDFDGNVLAgRGE----PEATAFFIHARIHRAIPRAKAAFHTHMPYATALSLTEgRPLTTLGQTALKFyGRTA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 270 Y-HDYHGILVDEEEKVLIQKNLGPKSkVLILRNHGLVSVGESVEEAF---YYihnLVVACEIQVRTLaSAGGPdnLVLLN 345
Cdd:PRK06486  151 VdEDYNGLALDAAEGDRIARAMGDAD-IVFLKNHGVMVCGPRIAEAWddlYY---LERACEVQVLAM-STGRP--LVPVD 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1622937148 346 PEKYKAKSRspgspvgegtgslpKWQIGEQE-----FEALMRMLD 385
Cdd:PRK06486  224 PAIAAAVAR--------------QMREGDREsarlhLEALRRTLD 254
PRK07490 PRK07490
hypothetical protein; Provisional
135-385 1.67e-20

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 91.32  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 135 SIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINL-------QGDVV 207
Cdd:PRK07490    1 MTMALSDEEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLDAddpstaeRPDVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 208 DrgstnlgvnQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCG-LLPISPE-ALSLGEVAYHDYHGILVDEEEKVL 285
Cdd:PRK07490   81 D---------ATAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNtARFFNRVAVDTLYGGMALEEEGER 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 286 IQKNLGPKSkVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASaGGPdnLVLLNPEkykaksrspgspVGEGTG 365
Cdd:PRK07490  152 LAGLLGDKR-RLLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALST-GQP--LRVLSDA------------VAEKTA 215
                         250       260
                  ....*....|....*....|....
gi 1622937148 366 SlpKWQ----IGEQEFEALMRMLD 385
Cdd:PRK07490  216 R--DWEdypgFSRQHFAELKALLD 237
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
145-338 1.04e-19

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 89.31  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 145 LRCKLAAFYRLADLFGWSQLIYNHITTRvnSEQEH-FLIVPFGLLYSEVTASSLVKINLQGDVVD-RGSTNlGVNQagft 222
Cdd:PRK07090   31 LRQKLALTCRILFDAGHDSGLAGQITAR--AEAPGtYYTQRLGLGFDEITASNLLLVDEDLNVLDgEGMPN-PANR---- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 223 LHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSL-GEVAY-HDYHGILVDEEEKVLIQKNLGPKSKVLiLR 300
Cdd:PRK07090  104 FHSWIYRARPDVNCIIHTHPPHVAALSMLEVPLVVSHMDTCPLyDDCAFlKDWPGVPVGNEEGEIISAALGDKRAIL-LS 182
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622937148 301 NHGLVSVGESVEEAFYYIHNLVVACEIQVrtLASAGGP 338
Cdd:PRK07090  183 HHGQLVAGKSIEEACVLALLIERAARLQL--LAMAAGP 218
PRK08333 PRK08333
aldolase;
143-316 2.12e-13

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 69.08  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 143 KLLRCKLAAFYRLADLFGWSQLIYNHITTRVNseqEHFLIVPFGLLYSEVTASSLVKINLQGDVVD--RGSTNlgvnqag 220
Cdd:PRK08333    2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSE------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 221 FTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLP-ISPEA-LSLGEVAYHDYHGI----LVDEEEKVLIQKNlgpks 294
Cdd:PRK08333   72 YRLHLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPiITPEAeLYLKKIPILPFRPAgsveLAEQVAEAMKEYD----- 146
                         170       180
                  ....*....|....*....|..
gi 1622937148 295 kVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08333  147 -AVIMERHGIVTVGRSLREAFY 167
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
176-314 3.12e-12

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 66.57  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 176 EQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrGSTNLGVNQAGftlHSAIYAARPDVKCVVHIHTPAGAAVSA----M 251
Cdd:PRK06557   41 GTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDTAS---HLYVYRHMPDVGGVVHTHSTYATAWAArgepI 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622937148 252 KCGLLPISPEAlsLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEA 314
Cdd:PRK06557  117 PCVLTAMADEF--GGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
PRK08130 PRK08130
putative aldolase; Validated
179-316 1.40e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 52.57  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 179 HFLIVPFGLLYSEVTASSLVKINLQGDVV--DRGSTNLgvnqagfTLHSAIYAARPDVKCVVHIHTPAGAAVSAM----- 251
Cdd:PRK08130   38 GWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLTALSCLggldp 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622937148 252 KCGLLPISPEAL-SLGEVAYHDYH--GilvDEEEKVLIQKnLGPKSKVLILRNHGLVSVGESVEEAFY 316
Cdd:PRK08130  111 TNVLPPFTPYYVmRVGHVPLIPYYrpG---DPAIAEALAG-LAARYRAVLLANHGPVVWGSSLEAAVN 174
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
174-338 2.77e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 51.67  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 174 NSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrGSTnlgVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKC 253
Cdd:PRK06833   34 NREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GER---KPSSELDMHLIFYRNREDINAIVHTHSPYATTLACLGW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 254 GLLPISPE-ALSLGEVAYHDYHGI----LVDEEEKVLIQKnlgpksKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQ 328
Cdd:PRK06833  110 ELPAVHYLiAVAGPNVRCAEYATFgtkeLAENAFEAMEDR------RAVLLANHGLLAGANNLKNAFNIAEEIEFCAEIY 183
                         170
                  ....*....|
gi 1622937148 329 VRTlASAGGP 338
Cdd:PRK06833  184 YQT-KSIGEP 192
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
177-333 2.85e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 48.58  E-value: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 177 QEHFLIVPFGLLYSEVTASSLVKINlqgdvvDRGSTNLG-VNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGL 255
Cdd:PRK08087   35 QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEGkLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 256 --------------LPISPEAlSLG--EVAYHDYHGIlvdeeekvliqknlgPKSKVLILRNHGLVSVGESVEEAFYYIH 319
Cdd:PRK08087  109 paihymiaaaggnsIPCAPYA-TFGtrELSEHVALAL---------------KNRKATLLQHHGLIACEVNLEKALWLAH 172
                         170
                  ....*....|....
gi 1622937148 320 NLVVACEIQVRTLA 333
Cdd:PRK08087  173 EVEVLAQLYLKTLA 186
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
173-327 5.46e-05

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 45.18  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVD---RGSTNLGVnqagftlHSAIYAARPDVKCVVHIHTP------ 243
Cdd:PRK12348   31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEgeyRPSSDTAT-------HLELYRRYPSLGGIVHTHSThatawa 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 244 -AGAAVSAMKC-------GLLPISpEALSLGEVAyHDYHgilvDEEEKVLIQkNLGPKSKV----LILRNHGLVSVGESV 311
Cdd:PRK12348  104 qAGLAIPALGTthadyffGDIPCT-RGLSEEEVQ-GEYE----LNTGKVIIE-TLGNAEPLhtpgIVVYQHGPFAWGKDA 176
                         170
                  ....*....|....*.
gi 1622937148 312 EEAfyyIHNLVVACEI 327
Cdd:PRK12348  177 HDA---VHNAVVMEEV 189
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
173-323 8.24e-05

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 44.44  E-value: 8.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 173 VNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDVVDrGSTNlgvNQAGFTLHSAIYAARPDVKCVVHIHTPAGA----AV 248
Cdd:PRK13145   33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVE-GDLN---PSSDLPTHVELYKAWPEVGGIVHTHSTEAVgwaqAG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 249 SAMKC----------GLLPISpEALSLGEV--AYHDYHGILVDEEEKvliQKNLGPKS-KVLILRNHGLVSVGESVEEAF 315
Cdd:PRK13145  109 RDIPFygtthadyfyGPIPCA-RSLTKDEVngAYEKETGSVIIEEFE---KRGLDPMAvPGIVVRNHGPFTWGKNPEQAV 184

                  ....*...
gi 1622937148 316 YyiHNLVV 323
Cdd:PRK13145  185 Y--HSVVL 190
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
521-624 3.74e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 3.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  521 GSEENLDEAREQKEKSPPDQPAVP-HPPPSTPIKLEEDLVPEPATGDDSDAATFKPTLPDLSP--DEPSEALGFPMLEKE 597
Cdd:PHA03307   100 PAREGSPTPPGPSSPDPPPPTPPPaSPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVasDAASSRQAALPLSSP 179
                           90       100
                   ....*....|....*....|....*....
gi 1622937148  598 EEAQRPPSP--TEAPTEASPEPAPDPAPV 624
Cdd:PHA03307   180 EETARAPSSppAEPPPSTPPAAASPRPPR 208
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
450-622 2.71e-03

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 41.21  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 450 SGRGDEASEEGQNGSS-----------PKSKTKGELvtASKAIIEKEYQPHVI-VSTTGPN-PFTTLTDRELEEYR---- 512
Cdd:PTZ00449  522 KAPGDKEGEEGEHEDSkesdepkeggkPGETKEGEV--GKKPGPAKEHKPSKIpTLSKKPEfPKDPKHPKDPEEPKkpkr 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 513 -----REVERKQKGSEENLDEAREQKEKSPPDQPAVPHPP--PSTPIKLEEDLVPEPATGDDSDAATFKPTLPDLSPDEP 585
Cdd:PTZ00449  600 prsaqRPTRPKSPKLPELLDIPKSPKRPESPKSPKRPPPPqrPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKFYDDY 679
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622937148 586 SEA--------------LGFPMLEKEEEAQRPPSPTEAPTEASPEPAPDPA 622
Cdd:PTZ00449  680 LDAaaksketkttvvldESFESILKETLPETPGTPFTTPRPLPPKLPRDEE 730
PHA03247 PHA03247
large tegument protein UL36; Provisional
527-642 5.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 5.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148  527 DEAREQKEKSPPDQPAVPHPPPSTPIKleedlVPEPATGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAQrPPSP 606
Cdd:PHA03247  2861 DVRRRPPSRSPAAKPAAPARPPVRRLA-----RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ-PPPP 2934
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1622937148  607 TEAPTEASPEPAPDPAPVAEEAAPSAAEEGAAADPG 642
Cdd:PHA03247  2935 PPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPG 2970
PRK08660 PRK08660
aldolase;
197-327 7.69e-03

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 38.01  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937148 197 LVKINLQGDVVDRGSTNLGVnqagftlHSAIYAaRPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALS-LGE--VAYHDY 273
Cdd:PRK08660   52 EVGIDDDGSVDPLASSETPV-------HRAIYR-RTSAKAIVHAHPPYAVALSLLEDEIVPLDSEGLYfLGTipVVGGDI 123
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622937148 274 HGILVDEEEKVLIQKNlgpksKVLILRNHGLVSVGESVEEAFYYIHNLVVACEI 327
Cdd:PRK08660  124 GSGELAENVARALSEH-----KGVVVRGHGTFAIGKTLEEAYIYTSQLEHSCKV 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.
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