NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720395359|ref|XP_030106825|]
View 

gamma-adducin isoform X1 [Mus musculus]

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 ...
 137-385 1.49e-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.


The actual alignment was detected with superfamily member PRK07044:

Pssm-ID: 469663  Cd Length: 252  Bit Score: 227.81  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044  172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                         250
                  ....*....|....
gi 1720395359 374 LMRTLD--NLGYRT 385
Cdd:PRK07044  239 LLRKLDriDPGYRD 252
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 1.49e-69

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 227.81  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044  172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                         250
                  ....*....|....
gi 1720395359 374 LMRTLD--NLGYRT 385
Cdd:PRK07044  239 LLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 1.07e-49

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: 171.57  E-value: 1.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEEEERIELQKVLGPSCKVLVLRNHGM 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1720395359 297 VALGETLEEAFHYIFNVQMACEIQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 1.68e-49

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: 172.16  E-value: 1.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLKIdht 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEEEErIELQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETGEDE-IGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395359 288 VLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAGGV--DNLLVLDLQKYKA 343
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLppISLELLNKEYLRK 208
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 141-321 1.08e-45

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: 160.88  E-value: 1.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359  141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTdlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEEEERI-ELQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1720395359  294 HGMVALGETLEEAFHYIFNVQMACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-333 2.25e-44

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: 158.07  E-value: 2.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLKIdhtgfs 214
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDlkpSSETPL------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 215 pHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEEEERiELQKVLGpSCKVLVLR 292
Cdd:COG0235    79 -HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTEELAE-AIAEALG-DRPAVLLR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720395359 293 NHGMVALGETLEEAFHYIFNVQMACEIQVQAVAgAGGVDNL 333
Cdd:COG0235   156 NHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-320 8.53e-08

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 53.04  E-value: 8.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG---LKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 240 VSSM---KCGILPISQESLILGDVAYYDYQGSL-------DEEEERI--ELQKVL--GP-SCKVLVlRNHGMVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiienTQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170       180
                  ....*....|....*....|..
gi 1720395359 305 ------EAFHYIFnvqmACEIQ 320
Cdd:TIGR03328 171 eakrhlEALEFLF----ECELE 188
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 1.49e-69

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 227.81  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044  172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                         250
                  ....*....|....
gi 1720395359 374 LMRTLD--NLGYRT 385
Cdd:PRK07044  239 LLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 1.07e-49

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: 171.57  E-value: 1.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEEEERIELQKVLGPSCKVLVLRNHGM 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1720395359 297 VALGETLEEAFHYIFNVQMACEIQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 1.68e-49

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: 172.16  E-value: 1.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLKIdht 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEEEErIELQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETGEDE-IGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395359 288 VLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAGGV--DNLLVLDLQKYKA 343
Cdd:cd00398   151 AVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLppISLELLNKEYLRK 208
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 141-321 1.08e-45

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: 160.88  E-value: 1.08e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359  141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTdlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEEEERI-ELQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1720395359  294 HGMVALGETLEEAFHYIFNVQMACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-333 2.25e-44

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: 158.07  E-value: 2.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLKIdhtgfs 214
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDlkpSSETPL------ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 215 pHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEEEERiELQKVLGpSCKVLVLR 292
Cdd:COG0235    79 -HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTEELAE-AIAEALG-DRPAVLLR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720395359 293 NHGMVALGETLEEAFHYIFNVQMACEIQVQAVAgAGGVDNL 333
Cdd:COG0235   156 NHGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
PRK06661 PRK06661
hypothetical protein; Provisional
 141-321 2.18e-36

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 136.50  E-value: 2.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 141 LASLYRLADLFGWAHLANTYISVRiSKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgSTDLKIDHTGFSPHAAIY 220
Cdd:PRK06661    7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 221 STRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGD-VAYYDYQG-SLDEEEERIELQKVLGpSCKVLVLRNHGMVA 298
Cdd:PRK06661   84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSlALDADKQSSRLVNDLK-QNYVMLLRNHGAIT 162

                         170       180
                  ....*....|....*....|...
gi 1720395359 299 LGETLEEAFHYIFNVQMACEIQV 321
Cdd:PRK06661  163 CGKTIHEAMFYTYHLEQACKTQC 185
PRK06208 PRK06208
class II aldolase/adducin family protein;
140-329 8.67e-23

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 98.91  E-value: 8.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 140 KLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgsTDLKIDHTGFSPHAAI 219
Cdd:PRK06208   46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 220 YSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYD-YQGSLDEEEERIELQKVLGPScKVLVLRNHGMV 297
Cdd:PRK06208  123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFyEDHALFDdFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720395359 298 ALGETLEEA-FHYIfNVQMACeiQVQAVAGAGG 329
Cdd:PRK06208  202 TVGPSVDAAaWWFI-ALERAC--QTQLLAEAAG 231
PRK06486 PRK06486
aldolase;
138-391 2.26e-21

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 94.39  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 138 RCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVdqgSTDLKIDHTGFSPHA 217
Cdd:PRK06486   28 RVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVL---AGRGEPEATAFFIHA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 218 AIYSTRPDVKCVIHIHT-LATAAVSSMKCGILPISQESL-ILGDVAY-YDYQG-SLDEEE-ERIelQKVLGPScKVLVLR 292
Cdd:PRK06486  105 RIHRAIPRAKAAFHTHMpYATALSLTEGRPLTTLGQTALkFYGRTAVdEDYNGlALDAAEgDRI--ARAMGDA-DIVFLK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 293 NHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAggvdnllvldlQKYKAFTHGVAmsggggvnMASHQKWKVGEIE-- 370
Cdd:PRK06486  182 NHGVMVCGPRIAEAWDDLYYLERACEVQVLAMSTG-----------RPLVPVDPAIA--------AAVARQMREGDREsa 242

                         250       260
                  ....*....|....*....|....
gi 1720395359 371 ---FEGLMRTLDnlgyRTGYAYRH 391
Cdd:PRK06486  243 rlhLEALRRTLD----REEPAYRT 262
PRK07490 PRK07490
hypothetical protein; Provisional
 147-325 3.42e-19

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 87.47  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 147 LADLFGW-AHL------ANtYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNiiGEVVDQGSTDLKIDHTGFSPHAAI 219
Cdd:PRK07490   15 LAAAFRWiARLgmheavAN-HFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD--ADDPSTAERPDVPDATAWAIHGQI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 220 YSTRPDVKCVIHIHTLATAAVSSMKCG-ILPISQESLI-LGDVAYYDYQGSLDEEEERIELQKVLGPScKVLVLRNHGMV 297
Cdd:PRK07490   92 HRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARfFNRVAVDTLYGGMALEEEGERLAGLLGDK-RRLLMGNHGVL 170

                         170       180
                  ....*....|....*....|....*...
gi 1720395359 298 ALGETLEEAFHYIFNVQMACEIQVQAVA 325
Cdd:PRK07490  171 VTGDTVAEAFDDLYYFERACQTYITALS 198
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 178-328 3.61e-12

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 66.97  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 178 GLSFSEATASTLVKVNiigevvdqgsTDLK-IDHTGF-SP----HAAIYSTRPDVKCVIHIHTLATAAVSSMKCGiLPIS 251
Cdd:PRK07090   71 GLGFDEITASNLLLVD----------EDLNvLDGEGMpNPanrfHSWIYRARPDVNCIIHTHPPHVAALSMLEVP-LVVS 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 252 QESL--ILGDVAYY-DYQGSL--DEEEERIelQKVLGpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAg 326
Cdd:PRK07090  140 HMDTcpLYDDCAFLkDWPGVPvgNEEGEII--SAALG-DKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMA- 215


                  ..
gi 1720395359 327 AG 328
Cdd:PRK07090  216 AG 217
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 161-306 8.67e-10

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 59.25  E-value: 8.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVD---QGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIH-TLA 236
Cdd:PRK06557   35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEgdlKPSSDT-------ASHLYVYRHMPDVGGVVHTHsTYA 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720395359 237 TA-AV--SSMKCGILPISQEslILGDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVLRNHGMVALGETLEEA 306
Cdd:PRK06557  107 TAwAArgEPIPCVLTAMADE--FGGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
161-323 1.13e-09

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 58.99  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVrISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqGStdlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK06833   30 ISI-FNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GE---RKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 241 SSMKCGILPISQESLILGD---VAYYDYQGSLDEEEERIELQKvlgpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMAC 317
Cdd:PRK06833  105 ACLGWELPAVHYLIAVAGPnvrCAEYATFGTKELAENAFEAME----DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCA 180


                  ....*.
gi 1720395359 318 EIQVQA 323
Cdd:PRK06833  181 EIYYQT 186
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
161-306 7.06e-08

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 53.59  E-value: 7.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRIskeQDHIIIIPRGLSFSEATASTLVKVNiigevvDQGSTDL-KIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAA 239
Cdd:PRK08087   30 VSVRY---QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEgKLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTA 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720395359 240 VSSMKCGILPISQESLILGD-----VAYYDYqGSLDEEEERIELQKvlgpSCKVLVLRNHGMVALGETLEEA 306
Cdd:PRK08087  101 VSILNRPIPAIHYMIAAAGGnsipcAPYATF-GTRELSEHVALALK----NRKATLLQHHGLIACEVNLEKA 167
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-320 8.53e-08

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 53.04  E-value: 8.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG---LKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 240 VSSM---KCGILPISQESLILGDVAYYDYQGSL-------DEEEERI--ELQKVL--GP-SCKVLVlRNHGMVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiienTQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170       180
                  ....*....|....*....|..
gi 1720395359 305 ------EAFHYIFnvqmACEIQ 320
Cdd:TIGR03328 171 eakrhlEALEFLF----ECELE 188
PRK08333 PRK08333
aldolase;
135-308 2.04e-07

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.75  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 135 KLTRCKLASLYRLADLFGWAHLANTYISVRISkeqDHIIIIPRGLSFSEATASTLVKVNIIGEVVD--QGSTDLKIdhtg 212
Cdd:PRK08333    2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSEYRL---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 213 fspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPI--SQESLILGDVAYYDYQ--GSLDEEEERIELQKvlgpSCKV 288
Cdd:PRK08333   75 ---HLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPIitPEAELYLKKIPILPFRpaGSVELAEQVAEAMK----EYDA 147

                         170       180
                  ....*....|....*....|
gi 1720395359 289 LVLRNHGMVALGETLEEAFH 308
Cdd:PRK08333  148 VIMERHGIVTVGRSLREAFY 167
PRK08130 PRK08130
putative aldolase; Validated
 161-306 5.48e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 51.03  E-value: 5.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08130   30 ISARL--DDGGWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 239 AVSS------------------MKCGILPIsqeslilgdVAYYDyQGSLDEEEERIElqkvLGPSCKVLVLRNHGMVALG 300
Cdd:PRK08130  101 ALSClggldptnvlppftpyyvMRVGHVPL---------IPYYR-PGDPAIAEALAG----LAARYRAVLLANHGPVVWG 166


                  ....*.
gi 1720395359 301 ETLEEA 306
Cdd:PRK08130  167 SSLEAA 172
PRK08660 PRK08660
aldolase;
161-319 1.94e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 48.80  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRIskeQDHIIIIPRGLSFSEATASTLVKVNII--GEVVDQGSTDLKIdhtgfspHAAIYsTRPDVKCVIHIHTLATA 238
Cdd:PRK08660   25 ISVRT---GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIY-RRTSAKAIVHAHPPYAV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 239 AVSSMKCGILPISQESL-ILGDVAYYDyqGSLDEEEERIELQKVLGpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMAC 317
Cdd:PRK08660   94 ALSLLEDEIVPLDSEGLyFLGTIPVVG--GDIGSGELAENVARALS-EHKGVVVRGHGTFAIGKTLEEAYIYTSQLEHSC 170


                  ..
gi 1720395359 318 EI 319
Cdd:PRK08660  171 KV 172
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 165-308 2.84e-05

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 45.95  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 165 ISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLkidhtgfSPHAAIYSTRPDVKCVIHIH-TLATA-A 239
Cdd:PRK12348   31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEyrpSSDT-------ATHLELYRRYPSLGGIVHTHsTHATAwA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 240 VSSMKCGILPISQESLILGDVAyydYQGSLDEEEERIELQKVLGpscKVL---------------VLRNHGMVALGETLE 304
Cdd:PRK12348  104 QAGLAIPALGTTHADYFFGDIP---CTRGLSEEEVQGEYELNTG---KVIietlgnaeplhtpgiVVYQHGPFAWGKDAH 177


                  ....
gi 1720395359 305 EAFH 308
Cdd:PRK12348  178 DAVH 181
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 161-330 8.06e-05

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 44.63  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgSTDLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK05874   31 ISARRS--DGNVVITPSSVDYAEMLLHDLVLVDAGGAVLH--AKDGRSPSTELNLHLACYRAFDDIGSVIHSHPVWATMF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 241 SSMKCGILPISQESLIL--GDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVlrNHGMVALGETLEEAFHYIFNVQMACE 318
Cdd:PRK05874  107 AVAHEPIPACIDEFAIYcgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPDQVLRVTALVERTAQ 184

                         170
                  ....*....|..
gi 1720395359 319 IQVQAVAGAGGV 330
Cdd:PRK05874  185 IVWGARALGGPV 196
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 165-309 9.06e-05

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 44.44  E-value: 9.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 165 ISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVD---QGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIHTlaTAAVS 241
Cdd:PRK13145   33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEgdlNPSSDL-------PTHVELYKAWPEVGGIVHTHS--TEAVG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 242 ------SMKC----------GILPISQeSLILGDV--AYYDYQGS-LDEEEERIELQKVLGPSckvLVLRNHGMVALGET 302
Cdd:PRK13145  104 waqagrDIPFygtthadyfyGPIPCAR-SLTKDEVngAYEKETGSvIIEEFEKRGLDPMAVPG---IVVRNHGPFTWGKN 179


                  ....*..
gi 1720395359 303 LEEAFHY 309
Cdd:PRK13145  180 PEQAVYH 186
PRK06357 PRK06357
hypothetical protein; Provisional
 161-233 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 40.91  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395359 161 ISVRIS--KEQDHIIIIPRGLSfsEATASTLVKVNIIgeVVDQgSTDLKIDHTG-----FSPHAAIYSTRPDVKCVIHIH 233
Cdd:PRK06357   30 ISVRMTaeKNKEYIIMTPTLMS--EAKLCDLSPYQIL--VVDL-NTGEVIEGVGrvtreINMHEAAYVANPKIKCVYHSH 104
 
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