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Conserved domains on  [gi|1387244676|ref|XP_024841291|]
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gamma-adducin isoform X2 [Bos taurus]

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 2.47e-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: 2.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHAGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQGSLDDQEERIQLQKVLGPsCKVLVLRNHG 295
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 296 VVALGETVEEAFHYIFNVQIACETQVQALagAGGVDNLLVLDLQKYKASTHTVAASGGGGvnmgshqkwkvGEIEFEGLM 375
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPALL 240
                         250
                  ....*....|..
gi 1387244676 376 RTLD--NLGYRT 385
Cdd:PRK07044  241 RKLDriDPGYRD 252
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
137-385 2.47e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 231.66  E-value: 2.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHAGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQGSLDDQEERIQLQKVLGPsCKVLVLRNHG 295
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 296 VVALGETVEEAFHYIFNVQIACETQVQALagAGGVDNLLVLDLQKYKASTHTVAASGGGGvnmgshqkwkvGEIEFEGLM 375
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPALL 240
                         250
                  ....*....|..
gi 1387244676 376 RTLD--NLGYRT 385
Cdd:PRK07044  241 RKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
139-321 3.37e-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: 172.73  E-value: 3.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhAGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDDQEERIQLQKVLGPSCKVLVLRNHGV 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153
                         170       180
                  ....*....|....*....|....*
gi 1387244676 297 VALGETVEEAFHYIFNVQIACETQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
134-343 9.28e-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: 172.55  E-value: 9.28e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdha 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDdQEERIQLQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPET-GEDEIGTQRALGfPNSK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387244676 288 VLVLRNHGVVALGETVEEAFHYIFNVQIACETQVQALAGAGGV--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 3.40e-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: 3.40e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676  141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHAGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDDQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157
                          170       180
                   ....*....|....*....|....*...
gi 1387244676  294 HGVVALGETVEEAFHYIFNVQIACETQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
138-333 6.22e-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: 156.53  E-value: 6.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHAGFSPHA 217
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDDqEERIQLQKVLGpSCKVLVLRNHG 295
Cdd:COG0235    81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTE-ELAEAIAEALG-DRPAVLLRNHG 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1387244676 296 VVALGETVEEAFHYIFNVQIACETQVQALAgAGGVDNL 333
Cdd:COG0235   159 VVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
161-317 3.78e-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: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKIDhAGFSPHAAIYSTRpDVKCVIHIHTLAtAAV 240
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPS-AETLLHTQLYRLT-GAGAVLHTHSVE-ATV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 241 SSM---KCGILPISQESLILGDVAYYDYQGSLD------DQEERiQLQKVLGP-------SCKVLVlRNHGVVALGETVE 304
Cdd:TIGR03328  93 LSRlypSNGGFELEGYEMLKGLPGITTHEDTLVvpiienTQDIA-RLADSVAPalnaypdVPGVLI-RGHGLYAWGRDWE 170
                         170
                  ....*....|....*....
gi 1387244676 305 ------EAFHYIFNVQIAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
 
Name Accession Description Interval E-value
PRK07044 PRK07044
aldolase II superfamily protein; Provisional
137-385 2.47e-71

aldolase II superfamily protein; Provisional


Pssm-ID: 235916  Cd Length: 252  Bit Score: 231.66  E-value: 2.47e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 137 TRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQgsTNLKIDHAGFSPH 216
Cdd:PRK07044   17 ARVDLAAAYRLVALLGWDDLIYTHISARVPGEEHHFLINPYGLLFDEITASNLVKIDLDGNVVDD--SPYPVNPAGFTIH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYDYQGSLDDQEERIQLQKVLGPsCKVLVLRNHG 295
Cdd:PRK07044   95 SAIHAARPDAHCVMHTHTTAGVAVSAQRDGLLPLSQHALQFyGRLAYHDYEGIALDLDEGERLVADLGD-KPAMLLRNHG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 296 VVALGETVEEAFHYIFNVQIACETQVQALagAGGVDNLLVLDLQKYKASTHTVAASGGGGvnmgshqkwkvGEIEFEGLM 375
Cdd:PRK07044  174 LLTVGRTVAEAFLLMYTLERACEIQVAAQ--AGGGELVLPPPEVAERTARQSLFDPGAGA-----------GELAWPALL 240
                         250
                  ....*....|..
gi 1387244676 376 RTLD--NLGYRT 385
Cdd:PRK07044  241 RKLDriDPGYRD 252
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
139-321 3.37e-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: 172.73  E-value: 3.37e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 139 CKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGstnLKIDhAGFSPHAA 218
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL--PGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG---LKPS-SETPLHLA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 219 IYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL--GDVAYYDYQGsLDDQEERIQLQKVLGPSCKVLVLRNHGV 296
Cdd:pfam00596  75 IYRARPDAGAVVHTHSPYATALSLAKEGLPPITQEAADFlgGDIPIIPYYT-PGTEELGERIAEALGGDRKAVLLRNHGL 153
                         170       180
                  ....*....|....*....|....*
gi 1387244676 297 VALGETVEEAFHYIFNVQIACETQV 321
Cdd:pfam00596 154 LVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
134-343 9.28e-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: 172.55  E-value: 9.28e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 134 EKLTRcKLASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLKIdha 211
Cdd:cd00398     1 EKLKR-KIIAACLLLDLYGWVTGTGGNVSARD-RDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVegKKPSSETPL--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 212 gfspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL---GDVAYYDYQGSLDdQEERIQLQKVLG-PSCK 287
Cdd:cd00398    76 ----HLALYRARPDIGCIVHTHSTHATAVSQLKEGLIPAGHTACAVyftGDIPCTPYMTPET-GEDEIGTQRALGfPNSK 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1387244676 288 VLVLRNHGVVALGETVEEAFHYIFNVQIACETQVQALAGAGGV--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 3.40e-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: 3.40e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676  141 LASLYRLADLFGWAHLANTYISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTnlKIDHAGFSPHAAIY 220
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARV-GEEDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG--PKPSSETPLHLAIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676  221 STRPDVKCVIHIHTLATAAVSSM--KCGILPISQESLILG-DVAYYDYQGSLDDQEERIQ-LQKVLGP---SCKVLVLRN 293
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALgkPLPLLPTEQAAAFLGgEIPYAPYAGPGTELAEEGAeLAEALAEalpDRPAVLLRN 157
                          170       180
                   ....*....|....*....|....*...
gi 1387244676  294 HGVVALGETVEEAFHYIFNVQIACETQV 321
Cdd:smart01007 158 HGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
138-333 6.22e-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: 156.53  E-value: 6.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 138 RCKLASLYRLADLFGWAHLANTYISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNlkidHAGFSPHA 217
Cdd:COG0235     7 REELAAAGRRLARRGLVDGTAGNISVRL--DDDRFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLKP----SSETPLHL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 218 AIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQE--SLILGDVAYYDYQGSLDDqEERIQLQKVLGpSCKVLVLRNHG 295
Cdd:COG0235    81 AIYRARPDVGAVVHTHSPYATALSALGEPLPPLEQTeaAAFLGDVPVVPYAGPGTE-ELAEAIAEALG-DRPAVLLRNHG 158
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1387244676 296 VVALGETVEEAFHYIFNVQIACETQVQALAgAGGVDNL 333
Cdd:COG0235   159 VVVWGKDLAEAFDRAEVLEEAARIQLLALA-LGGPLVL 195
PRK06661 PRK06661
hypothetical protein; Provisional
141-325 7.80e-36

hypothetical protein; Provisional


Pssm-ID: 168637  Cd Length: 231  Bit Score: 134.96  E-value: 7.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 141 LASLYRLADLFGWAHLANTYISVRiSKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgSTNLKIDHAGFSPHAAIY 220
Cdd:PRK06661    7 LAAAYRIMAYLSLDDHTYTHLSAR-PKNADFYYIYPFGLRFEEVTTENLLKVSLDGQILE--GEEYQYNKTGYFIHGSIY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 221 STRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGD-VAYYDYQG-SLDDQEERIQLQKVLGpSCKVLVLRNHGVVA 298
Cdd:PRK06661   84 KTRPDISAIFHYHTPASIAVSALKCGLLPISQWALHFYDrISYHNYNSlALDADKQSSRLVNDLK-QNYVMLLRNHGAIT 162
                         170       180
                  ....*....|....*....|....*..
gi 1387244676 299 LGETVEEAFHYIFNVQIACETQVQALA 325
Cdd:PRK06661  163 CGKTIHEAMFYTYHLEQACKTQCLLNS 189
PRK06208 PRK06208
class II aldolase/adducin family protein;
140-329 4.14e-26

class II aldolase/adducin family protein;


Pssm-ID: 235743  Cd Length: 274  Bit Score: 108.15  E-value: 4.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 140 KLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqgsTNLKIDHAGFSPHAAI 219
Cdd:PRK06208   46 RLAAAFRLFARFGFDEGLAGHITARDPELPDHFWVNPLGVHFSQIKVSDLLLVDHDGEVVE---GDRPLNRAAFAIHSAI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 220 YSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLIL-GDVAYYD-YQGSLDDQEERIQLQKVLGPScKVLVLRNHGVV 297
Cdd:PRK06208  123 HEARPDVVAAAHTHSTYGKAWSTLGRPLDPITQDACAFyEDHALFDdFTGVVVDTSEGRRIAAALGTH-KAVILQNHGLL 201
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1387244676 298 ALGETVEEA-FHYIfNVQIACetQVQALAGAGG 329
Cdd:PRK06208  202 TVGPSVDAAaWWFI-ALERAC--QTQLLAEAAG 231
PRK06486 PRK06486
aldolase;
138-391 1.53e-22

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 97.47  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 138 RCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVD-QGstnlKIDHAGFSPH 216
Cdd:PRK06486   28 RVDLAACFRAAARHGLEEGICNHFSAVLPGHDDLFLVNPYGYAFSEITASDLLICDFDGNVLAgRG----EPEATAFFIH 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 217 AAIYSTRPDVKCVIHIHT-LATAAVSSMKCGILPISQESL-ILGDVAY-YDYQG-SLDDQE-ERIQlqKVLGPScKVLVL 291
Cdd:PRK06486  104 ARIHRAIPRAKAAFHTHMpYATALSLTEGRPLTTLGQTALkFYGRTAVdEDYNGlALDAAEgDRIA--RAMGDA-DIVFL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 292 RNHGVVALGETVEEAFHYIFNVQIACetQVQALAGAGGvdnllvldlQKYKASTHTVAASGGGGVNMGSHQKwkvGEIEF 371
Cdd:PRK06486  181 KNHGVMVCGPRIAEAWDDLYYLERAC--EVQVLAMSTG---------RPLVPVDPAIAAAVARQMREGDRES---ARLHL 246
                         250       260
                  ....*....|....*....|
gi 1387244676 372 EGLMRTLDnlgyRTGYAYRH 391
Cdd:PRK06486  247 EALRRTLD----REEPAYRT 262
PRK07490 PRK07490
hypothetical protein; Provisional
147-325 8.67e-20

hypothetical protein; Provisional


Pssm-ID: 236031 [Multi-domain]  Cd Length: 245  Bit Score: 89.01  E-value: 8.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 147 LADLFGW-AHL------ANtYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNiigevVDQGSTNLK---IDHAGFSPH 216
Cdd:PRK07490   15 LAAAFRWiARLgmheavAN-HFSAAVSADGKQFLLNPKWKHFSRIRASDLLLLD-----ADDPSTAERpdvPDATAWAIH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 217 AAIYSTRPDVKCVIHIHTLATAAVSSMKCG-ILPISQESLI-LGDVAYYDYQGSLDDQEERIQLQKVLGPScKVLVLRNH 294
Cdd:PRK07490   89 GQIHRRLPHARCVMHVHSVYATALACLADPtLPPIDQNTARfFNRVAVDTLYGGMALEEEGERLAGLLGDK-RRLLMGNH 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1387244676 295 GVVALGETVEEAFHYIFNVQIACETQVQALA 325
Cdd:PRK07490  168 GVLVTGDTVAEAFDDLYYFERACQTYITALS 198
PRK07090 PRK07090
class II aldolase/adducin domain protein; Provisional
178-328 4.57e-13

class II aldolase/adducin domain protein; Provisional


Pssm-ID: 180832  Cd Length: 260  Bit Score: 69.66  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 178 GLSFSEATASNLVKVNIIGEVVD-QGSTNlkidhagfsP----HAAIYSTRPDVKCVIHIHTLATAAVSSMKCGiLPISQ 252
Cdd:PRK07090   71 GLGFDEITASNLLLVDEDLNVLDgEGMPN---------PanrfHSWIYRARPDVNCIIHTHPPHVAALSMLEVP-LVVSH 140
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387244676 253 ESL--ILGDVAYY-DYQGSLDDQEERIQLQKVLGpSCKVLVLRNHGVVALGETVEEAFHYIFNVQIACETQVQALAgAG 328
Cdd:PRK07090  141 MDTcpLYDDCAFLkDWPGVPVGNEEGEIISAALG-DKRAILLSHHGQLVAGKSIEEACVLALLIERAARLQLLAMA-AG 217
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
161-306 2.04e-11

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 64.26  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRIsKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHAGfspHAAIYSTRPDVKCVIHIH-TLATA- 238
Cdd:PRK06557   35 VSARD-PGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-GDLKPSSDTAS---HLYVYRHMPDVGGVVHTHsTYATAw 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 239 AV--SSMKCGILPISQEslILGDVAYYDYQGSLDDQEERIQLQKVLGPSCKVLVLRNHGVVALGETVEEA 306
Cdd:PRK06557  110 AArgEPIPCVLTAMADE--FGGPIPVGPFALIGDEAIGKGIVETLKGGRSPAVLMQNHGVFTIGKDAEDA 177
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
161-317 3.78e-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: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRISkeQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdqgSTNLKIDhAGFSPHAAIYSTRpDVKCVIHIHTLAtAAV 240
Cdd:TIGR03328  21 LSARLD--EDEILITPSGVDKGRLTPEDFLVVDLQGKPV---SGGLKPS-AETLLHTQLYRLT-GAGAVLHTHSVE-ATV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 241 SSM---KCGILPISQESLILGDVAYYDYQGSLD------DQEERiQLQKVLGP-------SCKVLVlRNHGVVALGETVE 304
Cdd:TIGR03328  93 LSRlypSNGGFELEGYEMLKGLPGITTHEDTLVvpiienTQDIA-RLADSVAPalnaypdVPGVLI-RGHGLYAWGRDWE 170
                         170
                  ....*....|....*....
gi 1387244676 305 ------EAFHYIFNVQIAC 317
Cdd:TIGR03328 171 eakrhlEALEFLFECELEM 189
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
161-318 2.12e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 52.06  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVrISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGStnlKIDHAGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK06833   30 ISI-FNREQGLMAITPSGIDYFEIKPEDIVIMDLDGKVVE-GE---RKPSSELDMHLIFYRNREDINAIVHTHSPYATTL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 241 SSMKCGILPISQESLILGD---VAYYDYQGSLDDQEERIQLQKvlgpSCKVLVLRNHGVVALGETVEEAFHYIFNVQIAC 317
Cdd:PRK06833  105 ACLGWELPAVHYLIAVAGPnvrCAEYATFGTKELAENAFEAME----DRRAVLLANHGLLAGANNLKNAFNIAEEIEFCA 180

                  .
gi 1387244676 318 E 318
Cdd:PRK06833  181 E 181
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
161-325 5.68e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 50.89  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNIIGEVvDQGstnlKIDHAGFSPHAAIYSTRPDVKCVIHIHTLATAAV 240
Cdd:PRK08087   30 VSVRY---QDGMLITPTGIPYEKLTESHIVFVDGNGKH-EEG----KLPSSEWRFHMAAYQTRPDANAVVHNHAVHCTAV 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 241 SSMKCGILPISQESLILGD-----VAYYDYqGSLDDQEERIQLQKvlgpSCKVLVLRNHGVVALGETVEEAFHYIFNVQI 315
Cdd:PRK08087  102 SILNRPIPAIHYMIAAAGGnsipcAPYATF-GTRELSEHVALALK----NRKATLLQHHGLIACEVNLEKALWLAHEVEV 176
                         170
                  ....*....|
gi 1387244676 316 ACETQVQALA 325
Cdd:PRK08087  177 LAQLYLKTLA 186
PRK08130 PRK08130
putative aldolase; Validated
161-306 8.72e-07

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 50.26  E-value: 8.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRIskEQDHIIIIPRGLSFSEATASNLVKVNIIGEVV--DQGSTNLkidhagfSPHAAIYSTRPDVKCVIHIHTLATA 238
Cdd:PRK08130   30 ISARL--DDGGWLVTPTGSCLGRLDPARLSKVDADGNWLsgDKPSKEV-------PLHRAIYRNNPECGAVVHLHSTHLT 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 239 AVSS------------------MKCGILPIsqeslilgdVAYYDyQGSLDDQEERIQlqkvLGPSCKVLVLRNHGVVALG 300
Cdd:PRK08130  101 ALSClggldptnvlppftpyyvMRVGHVPL---------IPYYR-PGDPAIAEALAG----LAARYRAVLLANHGPVVWG 166

                  ....*.
gi 1387244676 301 ETVEEA 306
Cdd:PRK08130  167 SSLEAA 172
PRK08333 PRK08333
aldolase;
135-308 2.40e-06

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 48.28  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 135 KLTRCKLASLYRLADLFGWAHLANTYISVRISkeqDHIIIIPRGLSFSEATASNLVKVNIIGEVVD--QGSTNLKIdhag 212
Cdd:PRK08333    2 RNVKAQLVKYSKLAHERGLTAAFGGNLSIRVG---NLVFIKATGSVMDELTREQVAVIDLNGNQLSsvRPSSEYRL---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 213 fspHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPI--SQESLILGDVAYYDYQ--GSLDDQEERIQLQKvlgpSCKV 288
Cdd:PRK08333   75 ---HLAVYRNRPDVRAIAHLHPPYSIVASTLLEEELPIitPEAELYLKKIPILPFRpaGSVELAEQVAEAMK----EYDA 147
                         170       180
                  ....*....|....*....|
gi 1387244676 289 LVLRNHGVVALGETVEEAFH 308
Cdd:PRK08333  148 VIMERHGIVTVGRSLREAFY 167
PRK08660 PRK08660
aldolase;
161-317 1.63e-05

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 46.10  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRIskeQDHIIIIPRGLSFSEATASNLVKVNII--GEVVDQGSTNLKIdhagfspHAAIYsTRPDVKCVIHIHTLATA 238
Cdd:PRK08660   25 ISVRT---GDGLLITRTGSMLDEITEGDVIEVGIDddGSVDPLASSETPV-------HRAIY-RRTSAKAIVHAHPPYAV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 239 AVSSMKCGILPISQESL-ILGDVAYYDyqGSLDDQEERIQLQKVLGpSCKVLVLRNHGVVALGETVEEAFHYIFNVQIAC 317
Cdd:PRK08660   94 ALSLLEDEIVPLDSEGLyFLGTIPVVG--GDIGSGELAENVARALS-EHKGVVVRGHGTFAIGKTLEEAYIYTSQLEHSC 170
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
165-309 2.30e-05

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 46.37  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 165 ISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVdQGSTNLKIDhagFSPHAAIYSTRPDVKCVIHIHTlaTAAVS--- 241
Cdd:PRK13145   33 VCRELGRIVIKPSGVDYDELTPENMVVTDLDGNVV-EGDLNPSSD---LPTHVELYKAWPEVGGIVHTHS--TEAVGwaq 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 242 ---SMKC----------GILPISQeSLILGDV--AYYDYQGSLDDQE-ERIQLQKVLGPSckvLVLRNHGVVALGETVEE 305
Cdd:PRK13145  107 agrDIPFygtthadyfyGPIPCAR-SLTKDEVngAYEKETGSVIIEEfEKRGLDPMAVPG---IVVRNHGPFTWGKNPEQ 182

                  ....
gi 1387244676 306 AFHY 309
Cdd:PRK13145  183 AVYH 186
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
165-308 6.45e-05

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 44.79  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 165 ISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDqGSTNLKIDHAgfsPHAAIYSTRPDVKCVIHIH-TLATA-AVSS 242
Cdd:PRK12348   31 IDRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVE-GEYRPSSDTA---THLELYRRYPSLGGIVHTHsTHATAwAQAG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 243 MKCGILPISQESLILGDVAyydYQGSLDDQEERIQLQKVLGpscKVL---------------VLRNHGVVALGETVEEAF 307
Cdd:PRK12348  107 LAIPALGTTHADYFFGDIP---CTRGLSEEEVQGEYELNTG---KVIietlgnaeplhtpgiVVYQHGPFAWGKDAHDAV 180

                  .
gi 1387244676 308 H 308
Cdd:PRK12348  181 H 181
PRK06357 PRK06357
hypothetical protein; Provisional
161-233 1.68e-04

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 43.61  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387244676 161 ISVRIS--KEQDHIIIIPRGLSfsEATASNLVKVNIIgeVVDQgSTNLKIDHAG-----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.
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