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Conserved domains on  [gi|1864420678|ref|XP_035124927|]
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gamma-adducin isoform X1 [Callithrix jacchus]

Protein Classification

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

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

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 137-385 4.61e-71

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: 231.66  E-value: 4.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG---SLDEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 293 NHGVVALGETVEEAFHYIFNVQLACEIQVQALAGAGGVDNLS--VLDfqkykaftHTVAVSGGGGVNMGshqkwkvGEIE 370
Cdd:PRK07044  171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPpeVAE--------RTARQSLFDPGAGA-------GELA 235

                         250
                  ....*....|....*..
gi 1864420678 371 FEGLMRTLD--NLGYRT 385
Cdd:PRK07044  236 WPALLRKLDriDPGYRD 252
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 4.61e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 231.66  E-value: 4.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG---SLDEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 293 NHGVVALGETVEEAFHYIFNVQLACEIQVQALAGAGGVDNLS--VLDfqkykaftHTVAVSGGGGVNMGshqkwkvGEIE 370
Cdd:PRK07044  171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPpeVAE--------RTARQSLFDPGAGA-------GELA 235

                         250
                  ....*....|....*..
gi 1864420678 371 FEGLMRTLD--NLGYRT 385
Cdd:PRK07044  236 WPALLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 2.55e-50

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 173.50  E-value: 2.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 139 CKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEQEERIQLQKVLGPSCKVLVLRNHGV 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1864420678 297 VALGETVEEAFHYIFNVQLACEIQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 3.21e-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: 174.09  E-value: 3.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 134 EKLTRcKLASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdht 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEqEERIQLQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETG-EDEIGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864420678 288 VLVLRNHGVVALGETVEEAFHYIFNVQLACEIQVQALAGAGGV--DNLSVLDFQKYKA 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 4.47e-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: 162.04  E-value: 4.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678  141 LASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1864420678  294 HGVVALGETVEEAFHYIFNVQLACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-334 6.76e-45

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: 159.61  E-value: 6.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 138 RCKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHTGFSPHA 217
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEqEERIQLQKVLGpSCKVLVLRNHG 295
Cdd:COG0235    81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTE-ELAEAIAEALG-DRPAVLLRNHG 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1864420678 296 VVALGETVEEAFHYIFNVQLACEIQVQALAgAGGVDNLS 334
Cdd:COG0235   159 VVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVLS 196
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-317 3.53e-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: 56.89  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 240 VSSM---KCGILPISQESLILGDVAYYDYQGSL---------DEQEERIQLQKVL--GP-SCKVLVlRNHGVVALGETVE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiientqDIARLADSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170
                  ....*....|....*....
gi 1864420678 305 ------EAFHYIFNVQLAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
 137-385 4.61e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 231.66  E-value: 4.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 137 TRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHTGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQG---SLDEQEeriQLQKVLGPsCKVLVLR 292
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGialDLDEGE---RLVADLGD-KPAMLLR 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 293 NHGVVALGETVEEAFHYIFNVQLACEIQVQALAGAGGVDNLS--VLDfqkykaftHTVAVSGGGGVNMGshqkwkvGEIE 370
Cdd:PRK07044  171 NHGLLTVGRTVAEAFLLMYTLERACEIQVAAQAGGGELVLPPpeVAE--------RTARQSLFDPGAGA-------GELA 235

                         250
                  ....*....|....*..
gi 1864420678 371 FEGLMRTLD--NLGYRT 385
Cdd:PRK07044  236 WPALLRKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 139-321 2.55e-50

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 173.50  E-value: 2.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 139 CKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhTGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDEQEERIQLQKVLGPSCKVLVLRNHGV 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153

                         170       180
                  ....*....|....*....|....*
gi 1864420678 297 VALGETVEEAFHYIFNVQLACEIQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 134-343 3.21e-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: 174.09  E-value: 3.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 134 EKLTRcKLASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdht 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDEqEERIQLQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPETG-EDEIGTQRALGfPNSK 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1864420678 288 VLVLRNHGVVALGETVEEAFHYIFNVQLACEIQVQALAGAGGV--DNLSVLDFQKYKA 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 4.47e-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: 162.04  E-value: 4.47e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678  141 LASLYRLVDLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHTGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDEQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157

                          170       180
                   ....*....|....*....|....*...
gi 1864420678  294 HGVVALGETVEEAFHYIFNVQLACEIQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 138-334 6.76e-45

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: 159.61  E-value: 6.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 138 RCKLASLYRLVDLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHTGFSPHA 217
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDEqEERIQLQKVLGpSCKVLVLRNHG 295
Cdd:COG0235    81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTE-ELAEAIAEALG-DRPAVLLRNHG 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1864420678 296 VVALGETVEEAFHYIFNVQLACEIQVQALAgAGGVDNLS 334
Cdd:COG0235   159 VVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVLS 196
PRK06661 PRK06661
hypothetical protein; Provisional
 141-325 9.75e-37

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 137.66  E-value: 9.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 141 LASLYRLVDLFGWAHLANTYISVRiSKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgSTNLKIDHTGFSPHAAIY 220
Cdd:PRK06661    7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 221 STRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGD-VAYYDYQG-SLDEQEERIQLQKVLGpSCKVLVLRNHGVVA 298
Cdd:PRK06661   84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSlALDADKQSSRLVNDLK-QNYVMLLRNHGAIT 162

                         170       180
                  ....*....|....*....|....*..
gi 1864420678 299 LGETVEEAFHYIFNVQLACEIQVQALA 325
Cdd:PRK06661  163 CGKTIHEAMFYTYHLEQACKTQCLLNS 189
PRK06208 PRK06208
class II aldolase/adducin family protein;
140-329 3.66e-25

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 105.84  E-value: 3.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 140 KLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgsTNLKIDHTGFSPHAAI 219
Cdd:PRK06208   46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 220 YSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYD-YQGSLDEQEERIQLQKVLGPScKVLVLRNHGVV 297
Cdd:PRK06208  123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFyEDHALFDdFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1864420678 298 ALGETVEEA-FHYIfNVQLACeiQVQALAGAGG 329
Cdd:PRK06208  202 TVGPSVDAAaWWFI-ALERAC--QTQLLAEAAG 231
PRK06486 PRK06486
aldolase;
138-391 4.26e-22

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 96.32  E-value: 4.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 138 RCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVD-QGstnlKIDHTGFSPH 216
Cdd:PRK06486   28 RVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVLAgRG----EPEATAFFIH 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 217 AAIYSTRPDVKCVIHIHT-LATAAVSSMKCGILPISQESL-ILGDVAY-YDYQG-SLDEQE-ERIQlqKVLGPScKVLVL 291
Cdd:PRK06486  104 ARIHRAIPRAKAAFHTHMpYATALSLTEGRPLTTLGQTALkFYGRTAVdEDYNGlALDAAEgDRIA--RAMGDA-DIVFL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 292 RNHGVVALGETVEEAFHYIFNVQLACEIQVqaLAGAGGvdnlsvldfQKYKAFTHTVAVSGGGGVNMGSHQKwkvGEIEF 371
Cdd:PRK06486  181 KNHGVMVCGPRIAEAWDDLYYLERACEVQV--LAMSTG---------RPLVPVDPAIAAAVARQMREGDRES---ARLHL 246

                         250       260
                  ....*....|....*....|
gi 1864420678 372 EGLMRTLDnlgyRTGYAYRH 391
Cdd:PRK06486  247 EALRRTLD----REEPAYRT 262
PRK07490 PRK07490
hypothetical protein; Provisional
 134-325 6.45e-21

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 92.48  E-value: 6.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 134 EKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNiigevVDQGSTNLK---IDH 210
Cdd:PRK07490    8 EEQIRVDLAAAFRWIARLGMHEAVANHFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD-----ADDPSTAERpdvPDA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 211 TGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCG-ILPISQESLI-LGDVAYYDYQGSLDEQEERIQLQKVLGPScKV 288
Cdd:PRK07490   83 TAWAIHGQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARfFNRVAVDTLYGGMALEEEGERLAGLLGDK-RR 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1864420678 289 LVLRNHGVVALGETVEEAFHYIFNVQLACEIQVQALA 325
Cdd:PRK07490  162 LLMGNHGVLVTGDTVAEAFDDLYYFERACQTYITALS 198
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
 178-328 2.00e-13

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 70.82  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 178 GLSFSEATASNLVKVNIIGEVVD-QGSTNlkidhtgfsP----HAAIYSTRPDVKCVIHIHTLATAAVSSMKCGiLPISQ 252
Cdd:PRK07090   71 GLGFDEITASNLLLVDEDLNVLDgEGMPN---------PanrfHSWIYRARPDVNCIIHTHPPHVAALSMLEVP-LVVSH 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864420678 253 ESL--ILGDVAYY-DYQGSLDEQEERIQLQKVLGpSCKVLVLRNHGVVALGETVEEAFHYIFNVQLACEIQVQALAgAG 328
Cdd:PRK07090  141 MDTcpLYDDCAFLkDWPGVPVGNEEGEIISAALG-DKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMA-AG 217
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 161-306 8.38e-11

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 62.33  E-value: 8.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHtgfSPHAAIYSTRPDVKCVIHIH-TLATA- 238
Cdd:PRK06557   35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDT---ASHLYVYRHMPDVGGVVHTHsTYATAw 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 239 AV--SSMKCGILPISQEslILGDVAYYDYQGSLDEQEERIQLQKVLGPSCKVLVLRNHGVVALGETVEEA 306
Cdd:PRK06557  110 AArgEPIPCVLTAMADE--FGGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 161-317 3.53e-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: 56.89  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKI-DHTGFspHAAIYSTRpDVKCVIHIHTLAtAA 239
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPsAETLL--HTQLYRLT-GAGAVLHTHSVE-AT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 240 VSSM---KCGILPISQESLILGDVAYYDYQGSL---------DEQEERIQLQKVL--GP-SCKVLVlRNHGVVALGETVE 304
Cdd:TIGR03328  92 VLSRlypSNGGFELEGYEMLKGLPGITTHEDTLvvpiientqDIARLADSVAPALnaYPdVPGVLI-RGHGLYAWGRDWE 170

                         170
                  ....*....|....*....
gi 1864420678 305 ------EAFHYIFNVQLAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
161-323 1.72e-08

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 55.53  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVrISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGStnlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK06833   30 ISI-FNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GE---RKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 241 SSMKCGILPISQESLILGD---VAYYDYQGSLDEQEERIQLQKvlgpSCKVLVLRNHGVVALGETVEEAFHYIFNVQLAC 317
Cdd:PRK06833  105 ACLGWELPAVHYLIAVAGPnvrCAEYATFGTKELAENAFEAME----DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCA 180


                  ....*.
gi 1864420678 318 EIQVQA 323
Cdd:PRK06833  181 EIYYQT 186
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
161-323 1.83e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 52.44  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNIIGEVvDQGstnlKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK08087   30 VSVRY---QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEG----KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 241 SSMKCGILPISQESLILGD-----VAYYDYqGSLDEQEERIQLQKvlgpSCKVLVLRNHGVVALGETVEEAfhyifnVQL 315
Cdd:PRK08087  102 SILNRPIPAIHYMIAAAGGnsipcAPYATF-GTRELSEHVALALK----NRKATLLQHHGLIACEVNLEKA------LWL 170


                  ....*...
gi 1864420678 316 ACEIQVQA 323
Cdd:PRK08087  171 AHEVEVLA 178
PRK08130 PRK08130
putative aldolase; Validated
 161-306 7.59e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 50.64  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLkidhtgfSPHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08130   30 ISARL--DDGGWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 239 AVSS------------------MKCGILPIsqeslilgdVAYYDyQGSLDEQEERIQlqkvLGPSCKVLVLRNHGVVALG 300
Cdd:PRK08130  101 ALSClggldptnvlppftpyyvMRVGHVPL---------IPYYR-PGDPAIAEALAG----LAARYRAVLLANHGPVVWG 166


                  ....*.
gi 1864420678 301 ETVEEA 306
Cdd:PRK08130  167 SSLEAA 172
PRK08660 PRK08660
aldolase;
161-319 3.38e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 48.03  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNII--GEVVDQGSTNLKIdhtgfspHAAIYsTRPDVKCVIHIHTLATA 238
Cdd:PRK08660   25 ISVRT---GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIY-RRTSAKAIVHAHPPYAV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 239 AVSSMKCGILPISQESL-ILGDVAYYDyqGSLDEQEERIQLQKVLGpSCKVLVLRNHGVVALGETVEEAFHYIFNVQLAC 317
Cdd:PRK08660   94 ALSLLEDEIVPLDSEGLyFLGTIPVVG--GDIGSGELAENVARALS-EHKGVVVRGHGTFAIGKTLEEAYIYTSQLEHSC 170


                  ..
gi 1864420678 318 EI 319
Cdd:PRK08660  171 KV 172
PRK08333 PRK08333
aldolase;
161-308 4.45e-06

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 47.90  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRISkeqDHIIIIPRGLSFSEATASNLVKVNIIGEVVD--QGSTNLKIdhtgfspHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08333   28 LSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSEYRL-------HLAVYRNRPDVRAIAHLHPPYSI 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864420678 239 AVSSMKCGILPI--SQESLILGDVAYYDYQ--GSLDEQEERIQLQKvlgpSCKVLVLRNHGVVALGETVEEAFH 308
Cdd:PRK08333   98 VASTLLEEELPIitPEAELYLKKIPILPFRpaGSVELAEQVAEAMK----EYDAVIMERHGIVTVGRSLREAFY 167
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 165-309 1.82e-05

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 46.75  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 165 ISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdQGSTNLKIDhtgFSPHAAIYSTRPDVKCVIHIHTlaTAAVS--- 241
Cdd:PRK13145   33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVV-EGDLNPSSD---LPTHVELYKAWPEVGGIVHTHS--TEAVGwaq 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 242 ---SMKC----------GILPISQeSLILGDV--AYYDYQGS-LDEQEERIQLQKVLGPSckvLVLRNHGVVALGETVEE 305
Cdd:PRK13145  107 agrDIPFygtthadyfyGPIPCAR-SLTKDEVngAYEKETGSvIIEEFEKRGLDPMAVPG---IVVRNHGPFTWGKNPEQ 182


                  ....
gi 1864420678 306 AFHY 309
Cdd:PRK13145  183 AVYH 186
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 145-308 3.14e-05

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 45.95  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 145 YRLVdLFGWAHLANtyisvrISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHtgfSPHAAIYSTRP 224
Cdd:PRK12348   18 YGLV-TFTWGNVSA------IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVE-GEYRPSSDT---ATHLELYRRYP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 225 DVKCVIHIH-TLATA-AVSSMKCGILPISQESLILGDVAyydYQGSLDEQEERIQLQKVLGpscKVL------------- 289
Cdd:PRK12348   87 SLGGIVHTHsTHATAwAQAGLAIPALGTTHADYFFGDIP---CTRGLSEEEVQGEYELNTG---KVIietlgnaeplhtp 160

                         170       180
                  ....*....|....*....|.
gi 1864420678 290 --VLRNHGVVALGETVEEAFH 308
Cdd:PRK12348  161 giVVYQHGPFAWGKDAHDAVH 181
PRK06357 PRK06357
hypothetical protein; Provisional
 138-233 1.30e-04

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 44.00  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 138 RCKLASLYRLVDLFGWAHLANTYISVRIS--KEQDHIIIIPRGLSfsEATASNLVKVNIIgeVVDQgSTNLKIDHTG--- 212
Cdd:PRK06357    7 REDLAKVVKTMFDRKETNAAGGNISVRMTaeKNKEYIIMTPTLMS--EAKLCDLSPYQIL--VVDL-NTGEVIEGVGrvt 81

                          90       100
                  ....*....|....*....|...
gi 1864420678 213 --FSPHAAIYSTRPDVKCVIHIH 233
Cdd:PRK06357   82 reINMHEAAYVANPKIKCVYHSH 104
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 161-330 4.04e-04

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 42.32  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVD--QG---STNLKIdhtgfspHAAIYSTRPDVKCVIHIHTL 235
Cdd:PRK05874   31 ISARRS--DGNVVITPSSVDYAEMLLHDLVLVDAGGAVLHakDGrspSTELNL-------HLACYRAFDDIGSVIHSHPV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864420678 236 ATAAVSSMKCGILPISQESLIL--GDVAYYDYQGSLDEQEERIQLQKVLGPSCKVLVlrNHGVVALGETVEEAFHYIFNV 313
Cdd:PRK05874  102 WATMFAVAHEPIPACIDEFAIYcgGDVRCTEYAASGTPEVGRNAVRALEGRAAALIA--NHGLVAVGPRPDQVLRVTALV 179

                         170
                  ....*....|....*..
gi 1864420678 314 QLACEIQVQALAGAGGV 330
Cdd:PRK05874  180 ERTAQIVWGARALGGPV 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.
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