NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|459447367|ref|NP_001264029|]
View 

gamma-adducin isoform a [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 459447367 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044 172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                        250
                 ....*....|....
gi 459447367 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 459447367 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044 172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                        250
                 ....*....|....
gi 459447367 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 459447367  139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367  219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEEEERIELQKVLGPSCKVLVLRNHGM 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 459447367  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 459447367 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLKIdht 211
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEEEErIELQKVLG-PSCK 287
Cdd:cd00398   76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETGEDE-IGTQRALGfPNSK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 459447367 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 459447367   141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTdlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367   221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEEEERI-ELQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 459447367   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 459447367 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLKIdhtgfs 214
Cdd:COG0235    7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDlkpSSETPL------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 215 pHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEEEERiELQKVLGpSCKVLVLR 292
Cdd:COG0235   79 -HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTEELAE-AIAEALG-DRPAVLLR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 459447367 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 459447367  161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG---LKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367  240 VSSM---KCGILPISQESLILGDVAYYDYQGSL-------DEEEERI--ELQKVL--GP-SCKVLVlRNHGMVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiienTQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170       180
                  ....*....|....*....|..
gi 459447367  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 459447367 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQgsTDLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG-SLDEEE-ERieLQKVLGPsCKVLVLRN 293
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGiALDLDEgER--LVADLGD-KPAMLLRN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 294 HGMVALGETLEEAFHYIFNVQMACEIQVQavAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGvnmashqkwkvGEIEFEG 373
Cdd:PRK07044 172 HGLLTVGRTVAEAFLLMYTLERACEIQVA--AQAGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPA 238

                        250
                 ....*....|....
gi 459447367 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 459447367  139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367  219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEEEERIELQKVLGPSCKVLVLRNHGM 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 459447367  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 459447367 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLKIdht 211
Cdd:cd00398    1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEEEErIELQKVLG-PSCK 287
Cdd:cd00398   76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETGEDE-IGTQRALGfPNSK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 459447367 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 459447367   141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTdlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367   221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEEEERI-ELQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGaELAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 459447367   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 459447367 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLKIdhtgfs 214
Cdd:COG0235    7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDlkpSSETPL------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 215 pHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEEEERiELQKVLGpSCKVLVLR 292
Cdd:COG0235   79 -HLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTEELAE-AIAEALG-DRPAVLLR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 459447367 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 459447367 141 LASLYRLADLFGWAHLANTYISVRiSKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgSTDLKIDHTGFSPHAAIY 220
Cdd:PRK06661   7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 221 STRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGD-VAYYDYQG-SLDEEEERIELQKVLGpSCKVLVLRNHGMVA 298
Cdd:PRK06661  84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSlALDADKQSSRLVNDLK-QNYVMLLRNHGAIT 162

                        170       180
                 ....*....|....*....|...
gi 459447367 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 459447367 140 KLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgsTDLKIDHTGFSPHAAI 219
Cdd:PRK06208  46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 220 YSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYD-YQGSLDEEEERIELQKVLGPScKVLVLRNHGMV 297
Cdd:PRK06208 123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFyEDHALFDdFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                        170       180       190
                 ....*....|....*....|....*....|...
gi 459447367 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 459447367 138 RCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVdqgSTDLKIDHTGFSPHA 217
Cdd:PRK06486  28 RVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVL---AGRGEPEATAFFIHA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 218 AIYSTRPDVKCVIHIHT-LATAAVSSMKCGILPISQESL-ILGDVAY-YDYQG-SLDEEE-ERIelQKVLGPScKVLVLR 292
Cdd:PRK06486 105 RIHRAIPRAKAAFHTHMpYATALSLTEGRPLTTLGQTALkFYGRTAVdEDYNGlALDAAEgDRI--ARAMGDA-DIVFLK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 293 NHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAggvdnllvldlQKYKAFTHGVAmsggggvnMASHQKWKVGEIE-- 370
Cdd:PRK06486 182 NHGVMVCGPRIAEAWDDLYYLERACEVQVLAMSTG-----------RPLVPVDPAIA--------AAVARQMREGDREsa 242

                        250       260
                 ....*....|....*....|....
gi 459447367 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 459447367 147 LADLFGW-AHL------ANtYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNiiGEVVDQGSTDLKIDHTGFSPHAAI 219
Cdd:PRK07490  15 LAAAFRWiARLgmheavAN-HFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD--ADDPSTAERPDVPDATAWAIHGQI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 220 YSTRPDVKCVIHIHTLATAAVSSMKCG-ILPISQESLI-LGDVAYYDYQGSLDEEEERIELQKVLGPScKVLVLRNHGMV 297
Cdd:PRK07490  92 HRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARfFNRVAVDTLYGGMALEEEGERLAGLLGDK-RRLLMGNHGVL 170

                        170       180
                 ....*....|....*....|....*...
gi 459447367 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 459447367 178 GLSFSEATASTLVKVNiigevvdqgsTDLK-IDHTGF-SP----HAAIYSTRPDVKCVIHIHTLATAAVSSMKCGiLPIS 251
Cdd:PRK07090  71 GLGFDEITASNLLLVD----------EDLNvLDGEGMpNPanrfHSWIYRARPDVNCIIHTHPPHVAALSMLEVP-LVVS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 252 QESL--ILGDVAYY-DYQGSL--DEEEERIelQKVLGpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAg 326
Cdd:PRK07090 140 HMDTcpLYDDCAFLkDWPGVPvgNEEGEII--SAALG-DKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMA- 215


                 ..
gi 459447367 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 459447367 161 ISVRIsKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVD---QGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIH-TLA 236
Cdd:PRK06557  35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEgdlKPSSDT-------ASHLYVYRHMPDVGGVVHTHsTYA 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 459447367 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 459447367 161 ISVrISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqGStdlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK06833  30 ISI-FNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GE---RKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 241 SSMKCGILPISQESLILGD---VAYYDYQGSLDEEEERIELQKvlgpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMAC 317
Cdd:PRK06833 105 ACLGWELPAVHYLIAVAGPnvrCAEYATFGTKELAENAFEAME----DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCA 180


                 ....*.
gi 459447367 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 459447367 161 ISVRIskeQDHIIIIPRGLSFSEATASTLVKVNiigevvDQGSTDL-KIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAA 239
Cdd:PRK08087  30 VSVRY---QDGMLITPTGIPYEKLTESHIVFVD------GNGKHEEgKLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTA 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 459447367 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 459447367  161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGstdLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPVSGG---LKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367  240 VSSM---KCGILPISQESLILGDVAYYDYQGSL-------DEEEERI--ELQKVL--GP-SCKVLVlRNHGMVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiienTQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170       180
                  ....*....|....*....|..
gi 459447367  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 459447367 135 KLTRCKLASLYRLADLFGWAHLANTYISVRISkeqDHIIIIPRGLSFSEATASTLVKVNIIGEVVD--QGSTDLKIdhtg 212
Cdd:PRK08333   2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSEYRL---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 213 fspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPI--SQESLILGDVAYYDYQ--GSLDEEEERIELQKvlgpSCKV 288
Cdd:PRK08333  75 ---HLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPIitPEAELYLKKIPILPFRpaGSVELAEQVAEAMK----EYDA 147

                        170       180
                 ....*....|....*....|
gi 459447367 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 459447367 161 ISVRIskEQDHIIIIPRGLSFSEATASTLVKVNIIGEVV--DQGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08130  30 ISARL--DDGGWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 239 AVSS------------------MKCGILPIsqeslilgdVAYYDyQGSLDEEEERIElqkvLGPSCKVLVLRNHGMVALG 300
Cdd:PRK08130 101 ALSClggldptnvlppftpyyvMRVGHVPL---------IPYYR-PGDPAIAEALAG----LAARYRAVLLANHGPVVWG 166


                 ....*.
gi 459447367 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 459447367 161 ISVRIskeQDHIIIIPRGLSFSEATASTLVKVNII--GEVVDQGSTDLKIdhtgfspHAAIYsTRPDVKCVIHIHTLATA 238
Cdd:PRK08660  25 ISVRT---GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIY-RRTSAKAIVHAHPPYAV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 239 AVSSMKCGILPISQESL-ILGDVAYYDyqGSLDEEEERIELQKVLGpSCKVLVLRNHGMVALGETLEEAFHYIFNVQMAC 317
Cdd:PRK08660  94 ALSLLEDEIVPLDSEGLyFLGTIPVVG--GDIGSGELAENVARALS-EHKGVVVRGHGTFAIGKTLEEAYIYTSQLEHSC 170


                 ..
gi 459447367 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 459447367 165 ISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQG---STDLkidhtgfSPHAAIYSTRPDVKCVIHIH-TLATA-A 239
Cdd:PRK12348  31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEGEyrpSSDT-------ATHLELYRRYPSLGGIVHTHsTHATAwA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 240 VSSMKCGILPISQESLILGDVAyydYQGSLDEEEERIELQKVLGpscKVL---------------VLRNHGMVALGETLE 304
Cdd:PRK12348 104 QAGLAIPALGTTHADYFFGDIP---CTRGLSEEEVQGEYELNTG---KVIietlgnaeplhtpgiVVYQHGPFAWGKDAH 177


                 ....
gi 459447367 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 459447367 161 ISVRISkeQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDqgSTDLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK05874  31 ISARRS--DGNVVITPSSVDYAEMLLHDLVLVDAGGAVLH--AKDGRSPSTELNLHLACYRAFDDIGSVIHSHPVWATMF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 241 SSMKCGILPISQESLIL--GDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVlrNHGMVALGETLEEAFHYIFNVQMACE 318
Cdd:PRK05874 107 AVAHEPIPACIDEFAIYcgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPDQVLRVTALVERTAQ 184

                        170
                 ....*....|..
gi 459447367 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 459447367 165 ISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVD---QGSTDLkidhtgfSPHAAIYSTRPDVKCVIHIHTlaTAAVS 241
Cdd:PRK13145  33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEgdlNPSSDL-------PTHVELYKAWPEVGGIVHTHS--TEAVG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459447367 242 ------SMKC----------GILPISQeSLILGDV--AYYDYQGS-LDEEEERIELQKVLGPSckvLVLRNHGMVALGET 302
Cdd:PRK13145 104 waqagrDIPFygtthadyfyGPIPCAR-SLTKDEVngAYEKETGSvIIEEFEKRGLDPMAVPG---IVVRNHGPFTWGKN 179


                 ....*..
gi 459447367 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 459447367 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