NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|62912453|ref|NP_001112|]
View 

gamma-adducin isoform b [Homo sapiens]

Protein Classification

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

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

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 137-385 1.01e-70

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: 230.12  E-value: 1.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESL-LLGDVAYYDYQG---SLEEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALqFYGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  293 NHGVVALGETLEEAFHYIFNVQLACEIQVQALagAGGVDNLH----VLDfqkyKAFTYTVAASGGGGvnmgshqkwkvGE 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLpppeVAE----RTARQSLFDPGAGA-----------GE 233

                        250
                 ....*....|....*....
gi 62912453  369 IEFEGLMRTLD--NLGYRT 385
Cdd:PRK07044 234 LAWPALLRKLDriDPGYRD 252
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 1.01e-70

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 230.12  E-value: 1.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESL-LLGDVAYYDYQG---SLEEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALqFYGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  293 NHGVVALGETLEEAFHYIFNVQLACEIQVQALagAGGVDNLH----VLDfqkyKAFTYTVAASGGGGvnmgshqkwkvGE 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLpppeVAE----RTARQSLFDPGAGA-----------GE 233

                        250
                 ....*....|....*....
gi 62912453  369 IEFEGLMRTLD--NLGYRT 385
Cdd:PRK07044 234 LAWPALLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 8.92e-51

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: 174.27  E-value: 8.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   139 CKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQES--LLLGDVAYYDY--QGSLEEQEEriqLQKVLGPSCKVLVLRNH 294
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIPYytPGTEELGER---IAEALGGDRKAVLLRNH 151

                         170       180
                  ....*....|....*....|....*..
gi 62912453   295 GVVALGETLEEAFHYIFNVQLACEIQV 321
Cdd:pfam00596 152 GLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 1.54e-50

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: 174.86  E-value: 1.54e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 134 EKLTRcKLASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdht 211
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLL---GDVAYYDYQGSLEEqEERIQLQKVLG-PSCK 287
Cdd:cd00398  76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETG-EDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62912453 288 VLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGV--DNLHVLDFQKYKA 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 6.63e-46

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: 161.27  E-value: 6.63e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453    141 LASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453    221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQES-LLLGDVAYYDYQGSLEEQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAaFLGGEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 62912453    294 HGVVALGETLEEAFHYIFNVQLACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-333 1.41e-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: 158.45  E-value: 1.41e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 138 RCKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHTGFSPHA 217
Cdd:COG0235   7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLLLGDVAYYDYQ--GSLEEQEEriqLQKVLGpSCKVLVLRN 293
Cdd:COG0235  81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAgpGTEELAEA---IAEALG-DRPAVLLRN 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 62912453 294 HGVVALGETLEEAFHYIFNVQLACEIQVQALAgAGGVDNL 333
Cdd:COG0235 157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-317 7.54e-09

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: 56.12  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   240 VSSM---KCGILPISQESLLLGDVAYYDYQGSLE-------EQEERI--QLQKVL--GP-SCKVLVlRNHGVVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLVvpiientQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170
                  ....*....|....*....
gi 62912453   305 ------EAFHYIFNVQLAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 1.01e-70

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 230.12  E-value: 1.01e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044  17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESL-LLGDVAYYDYQG---SLEEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044  95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALqFYGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  293 NHGVVALGETLEEAFHYIFNVQLACEIQVQALagAGGVDNLH----VLDfqkyKAFTYTVAASGGGGvnmgshqkwkvGE 368
Cdd:PRK07044 171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLpppeVAE----RTARQSLFDPGAGA-----------GE 233

                        250
                 ....*....|....*....
gi 62912453  369 IEFEGLMRTLD--NLGYRT 385
Cdd:PRK07044 234 LAWPALLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 8.92e-51

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: 174.27  E-value: 8.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   139 CKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQES--LLLGDVAYYDY--QGSLEEQEEriqLQKVLGPSCKVLVLRNH 294
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAadFLGGDIPIIPYytPGTEELGER---IAEALGGDRKAVLLRNH 151

                         170       180
                  ....*....|....*....|....*..
gi 62912453   295 GVVALGETLEEAFHYIFNVQLACEIQV 321
Cdd:pfam00596 152 GLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 1.54e-50

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: 174.86  E-value: 1.54e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 134 EKLTRcKLASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdht 211
Cdd:cd00398   1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLL---GDVAYYDYQGSLEEqEERIQLQKVLG-PSCK 287
Cdd:cd00398  76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETG-EDEIGTQRALGfPNSK 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62912453 288 VLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGV--DNLHVLDFQKYKA 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 6.63e-46

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: 161.27  E-value: 6.63e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453    141 LASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453    221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQES-LLLGDVAYYDYQGSLEEQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAaFLGGEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 62912453    294 HGVVALGETLEEAFHYIFNVQLACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-333 1.41e-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: 158.45  E-value: 1.41e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 138 RCKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHTGFSPHA 217
Cdd:COG0235   7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLLLGDVAYYDYQ--GSLEEQEEriqLQKVLGpSCKVLVLRN 293
Cdd:COG0235  81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAgpGTEELAEA---IAEALG-DRPAVLLRN 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 62912453 294 HGVVALGETLEEAFHYIFNVQLACEIQVQALAgAGGVDNL 333
Cdd:COG0235 157 HGVVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
PRK06661 PRK06661
hypothetical protein; Provisional
 141-325 2.77e-36

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 136.11  E-value: 2.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  141 LASLYRLVDLFGWAHLANTYISVRiSKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgSTNLKIDHTGFSPHAAIY 220
Cdd:PRK06661   7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  221 STRPDVKCVIHIHTLATAAVSSMKCGILPISQESL-LLGDVAYYDYQG-SLEEQEERIQLQKVLGpSCKVLVLRNHGVVA 298
Cdd:PRK06661  84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALhFYDRISYHNYNSlALDADKQSSRLVNDLK-QNYVMLLRNHGAIT 162

                        170       180
                 ....*....|....*....|....*..
gi 62912453  299 LGETLEEAFHYIFNVQLACEIQVQALA 325
Cdd:PRK06661 163 CGKTIHEAMFYTYHLEQACKTQCLLNS 189
PRK06208 PRK06208
class II aldolase/adducin family protein;
140-329 1.14e-24

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 104.30  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  140 KLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgsTNLKIDHTGFSPHAAI 219
Cdd:PRK06208  46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  220 YSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLL-GDVAYYD-YQGSLEEQEERIQLQKVLGPScKVLVLRNHGVV 297
Cdd:PRK06208 123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFyEDHALFDdFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                        170       180       190
                 ....*....|....*....|....*....|...
gi 62912453  298 ALGETLEEA-FHYIfNVQLACeiQVQALAGAGG 329
Cdd:PRK06208 202 TVGPSVDAAaWWFI-ALERAC--QTQLLAEAAG 231
PRK06486 PRK06486
aldolase;
99-391 4.40e-21

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 93.24  E-value: 4.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   99 MANSFSGFSSPPLSLGmvtpindlPGADTSSYVKgeklTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRG 178
Cdd:PRK06486   1 MAHSLTTDSAPPAGNR--------PLLDSDAVAQ----ARVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  179 LSFSEATASNLVKVNIIGEVVD-QGstnlKIDHTGFSPHAAIYSTRPDVKCVIHIHT-LATAAVSSMKCGILPISQESL- 255
Cdd:PRK06486  69 YAFSEITASDLLICDFDGNVLAgRG----EPEATAFFIHARIHRAIPRAKAAFHTHMpYATALSLTEGRPLTTLGQTALk 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  256 LLGDVAY-YDYQG-SLEEQE-ERIQlqKVLGPScKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVqaLAGAGGvdn 332
Cdd:PRK06486 145 FYGRTAVdEDYNGlALDAAEgDRIA--RAMGDA-DIVFLKNHGVMVCGPRIAEAWDDLYYLERACEVQV--LAMSTG--- 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62912453  333 lhvldfQKYKAFTYTVAASGGGGVNMGSHQKwkvGEIEFEGLMRTLDnlgyRTGYAYRH 391
Cdd:PRK06486 217 ------RPLVPVDPAIAAAVARQMREGDRES---ARLHLEALRRTLD----REEPAYRT 262
PRK07490 PRK07490
hypothetical protein; Provisional
 134-325 6.28e-20

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 89.39  E-value: 6.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  134 EKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNiigevVDQGSTNLK---IDH 210
Cdd:PRK07490   8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD-----ADDPSTAERpdvPDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  211 TGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCG-ILPISQESL-LLGDVAYYDYQGSLEEQEERIQLQKVLGPScKV 288
Cdd:PRK07490  83 TAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTArFFNRVAVDTLYGGMALEEEGERLAGLLGDK-RR 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 62912453  289 LVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALA 325
Cdd:PRK07490 162 LLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALS 198
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 178-328 9.61e-14

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 71.59  E-value: 9.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  178 GLSFSEATASNLVKVNIIGEVVD-QGSTNlkidhtgfsP----HAAIYSTRPDVKCVIHIHTLATAAVSSMKCGiLPISQ 252
Cdd:PRK07090  71 GLGFDEITASNLLLVDEDLNVLDgEGMPN---------PanrfHSWIYRARPDVNCIIHTHPPHVAALSMLEVP-LVVSH 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62912453  253 ESL--LLGDVAYY-DYQGSLEEQEERIQLQKVLGpSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAgAG 328
Cdd:PRK07090 141 MDTcpLYDDCAFLkDWPGVPVGNEEGEIISAALG-DKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMA-AG 217
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 161-306 1.06e-09

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 58.87  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHtgfSPHAAIYSTRPDVKCVIHIH-TLATA- 238
Cdd:PRK06557  35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDT---ASHLYVYRHMPDVGGVVHTHsTYATAw 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62912453  239 AV--SSMKCGILPISQEslLLGDVAYYDYQ--GSleeqeERI--QLQKVL--GPSCKVLvLRNHGVVALGETLEEA 306
Cdd:PRK06557 110 AArgEPIPCVLTAMADE--FGGPIPVGPFAliGD-----EAIgkGIVETLkgGRSPAVL-MQNHGVFTIGKDAEDA 177
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
161-323 1.16e-09

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 58.61  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVrISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGStnlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK06833  30 ISI-FNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GE---RKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  241 SSMKCGILPISQESLLLGD---VAYYDYQGSLEEQEERIQLQKvlgpSCKVLVLRNHGVVALGETLEEAFHYIFNVQLAC 317
Cdd:PRK06833 105 ACLGWELPAVHYLIAVAGPnvrCAEYATFGTKELAENAFEAME----DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCA 180


                 ....*.
gi 62912453  318 EIQVQA 323
Cdd:PRK06833 181 EIYYQT 186
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-317 7.54e-09

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: 56.12  E-value: 7.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453   240 VSSM---KCGILPISQESLLLGDVAYYDYQGSLE-------EQEERI--QLQKVL--GP-SCKVLVlRNHGVVALGETLE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLVvpiientQDIARLadSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170
                  ....*....|....*....
gi 62912453   305 ------EAFHYIFNVQLAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
161-323 3.10e-08

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 54.75  E-value: 3.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNIIGEVvDQGstnlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK08087  30 VSVRY---QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEG----KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  241 SSMKCGILPISQESLLLGD-----VAYYDYqGSLEEQEERIQLQKvlgpSCKVLVLRNHGVVALGETLEEAfhyifnVQL 315
Cdd:PRK08087 102 SILNRPIPAIHYMIAAAGGnsipcAPYATF-GTRELSEHVALALK----NRKATLLQHHGLIACEVNLEKA------LWL 170


                 ....*...
gi 62912453  316 ACEIQVQA 323
Cdd:PRK08087 171 AHEVEVLA 178
PRK08660 PRK08660
aldolase;
161-319 4.34e-08

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 53.42  E-value: 4.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNII--GEVVDQGSTNLKIdhtgfspHAAIYsTRPDVKCVIHIHTLATA 238
Cdd:PRK08660  25 ISVRT---GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIY-RRTSAKAIVHAHPPYAV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  239 AVSSMKCGILPISQESL-LLGDVAYYDYQ-GSLEEQEEriqLQKVLGpSCKVLVLRNHGVVALGETLEEAFHYIFNVQLA 316
Cdd:PRK08660  94 ALSLLEDEIVPLDSEGLyFLGTIPVVGGDiGSGELAEN---VARALS-EHKGVVVRGHGTFAIGKTLEEAYIYTSQLEHS 169


                 ...
gi 62912453  317 CEI 319
Cdd:PRK08660 170 CKV 172
PRK08333 PRK08333
aldolase;
161-308 2.42e-07

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.36  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRISkeqDHIIIIPRGLSFSEATASNLVKVNIIGEVVD--QGSTNLKIdhtgfspHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08333  28 LSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSEYRL-------HLAVYRNRPDVRAIAHLHPPYSI 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62912453  239 AVSSMKCGILPI--SQESLLLGDVAYYDYQ--GSLEEQEERIQLQKvlgpSCKVLVLRNHGVVALGETLEEAFH 308
Cdd:PRK08333  98 VASTLLEEELPIitPEAELYLKKIPILPFRpaGSVELAEQVAEAMK----EYDAVIMERHGIVTVGRSLREAFY 167
PRK08130 PRK08130
putative aldolase; Validated
 161-306 5.69e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 50.64  E-value: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLkidhtgfSPHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08130  30 ISARL--DDGGWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  239 AVSS------------------MKCGILPIsqeslllgdVAYYDyQGSLEEQEERIQlqkvLGPSCKVLVLRNHGVVALG 300
Cdd:PRK08130 101 ALSClggldptnvlppftpyyvMRVGHVPL---------IPYYR-PGDPAIAEALAG----LAARYRAVLLANHGPVVWG 166


                 ....*.
gi 62912453  301 ETLEEA 306
Cdd:PRK08130 167 SSLEAA 172
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 165-309 7.32e-06

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 47.91  E-value: 7.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  165 ISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdQGSTNLKIDhtgFSPHAAIYSTRPDVKCVIHIHTlaTAAVS--- 241
Cdd:PRK13145  33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVV-EGDLNPSSD---LPTHVELYKAWPEVGGIVHTHS--TEAVGwaq 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  242 ---SMKC----------GILPISQeSLLLGDV--AYYDYQGS--LEEQEERiQLQKVLGPSckvLVLRNHGVVALGETLE 304
Cdd:PRK13145 107 agrDIPFygtthadyfyGPIPCAR-SLTKDEVngAYEKETGSviIEEFEKR-GLDPMAVPG---IVVRNHGPFTWGKNPE 181


                 ....*
gi 62912453  305 EAFHY 309
Cdd:PRK13145 182 QAVYH 186
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 145-308 1.05e-04

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 44.02  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  145 YRLVdLFGWAHLANtyisvrISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHtgfSPHAAIYSTRP 224
Cdd:PRK12348  18 YGLV-TFTWGNVSA------IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVE-GEYRPSSDT---ATHLELYRRYP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  225 DVKCVIHIH-TLATA-AVSSMKCGILPISQESLLLGDV------AYYDYQGSLEEQEERI------QLQKVLGPSckvLV 290
Cdd:PRK12348  87 SLGGIVHTHsTHATAwAQAGLAIPALGTTHADYFFGDIpctrglSEEEVQGEYELNTGKViietlgNAEPLHTPG---IV 163

                        170
                 ....*....|....*...
gi 62912453  291 LRNHGVVALGETLEEAFH 308
Cdd:PRK12348 164 VYQHGPFAWGKDAHDAVH 181
PRK06357 PRK06357
hypothetical protein; Provisional
 138-233 1.29e-04

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 43.61  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  138 RCKLASLYRLVDLFGWAHLANTYISVRIS--KEQDHIIIIPRGLSfsEATASNLVKVNIIgeVVDQgSTNLKIDHTG--- 212
Cdd:PRK06357   7 REDLAKVVKTMFDRKETNAAGGNISVRMTaeKNKEYIIMTPTLMS--EAKLCDLSPYQIL--VVDL-NTGEVIEGVGrvt 81

                         90       100
                 ....*....|....*....|...
gi 62912453  213 --FSPHAAIYSTRPDVKCVIHIH 233
Cdd:PRK06357  82 reINMHEAAYVANPKIKCVYHSH 104
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 161-330 6.38e-04

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 41.55  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVD--QG---STNLKIdhtgfspHAAIYSTRPDVKCVIHIHTL 235
Cdd:PRK05874  31 ISARRS--DGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHakDGrspSTELNL-------HLACYRAFDDIGSVIHSHPV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912453  236 aTAAVSSMKCGILPISQESLLL---GDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVlrNHGVVALGETLEEAFHYIFN 312
Cdd:PRK05874 102 -WATMFAVAHEPIPACIDEFAIycgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPDQVLRVTAL 178

                        170
                 ....*....|....*...
gi 62912453  313 VQLACEIQVQALAGAGGV 330
Cdd:PRK05874 179 VERTAQIVWGARALGGPV 196
 
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