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Conserved domains on  [gi|1243057515|ref|NP_001342403|]
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methylthioribulose-1-phosphate dehydratase isoform 3 [Mus musculus]

Protein Classification

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

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

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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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 ...
1-154 3.63e-72

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 TIGR03328:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 192  Bit Score: 215.59  E-value: 3.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   1 MFVCDINEQDISGppaskKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgG 79
Cdd:TIGR03328  47 FLVVDLQGKPVSG-----GLKPSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----G 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243057515  80 YYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 154
Cdd:TIGR03328 117 ITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
1-154 3.63e-72

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: 215.59  E-value: 3.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   1 MFVCDINEQDISGppaskKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgG 79
Cdd:TIGR03328  47 FLVVDLQGKPVSG-----GLKPSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----G 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243057515  80 YYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 154
Cdd:TIGR03328 117 ITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
5-150 3.11e-28

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: 103.01  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   5 DINEQDISGPPASKKLKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGqeFKITHQEMIKgirkctsggyYRY 83
Cdd:pfam00596  48 DLVVVDLDGNVVEGGLKPSSETPLHLAIYRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLG 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243057515  84 DDmlvVPIIEN-TPEEKDLKERMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 150
Cdd:pfam00596 116 GD---IPIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
1-150 1.31e-27

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: 101.56  E-value: 1.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515    1 MFVCDINEQDISGPPAskkLKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMIKGIrkctSGG 79
Cdd:smart01007  48 LVVVDLDGNVVEGGGG---PKPSSETPLHLAIYRARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGG 118
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243057515   80 YYRYDDmLVVPIIENTPEEKDLKERMAHAMNEYPdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 150
Cdd:smart01007 119 EIPYAP-YAGPGTELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
10-146 1.56e-21

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 86.64  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  10 DISGPPASK-KLKKSQCTPLFMNAYTMRGAGAVIHTHSKAA-VMATLLFPGQEFKITHQEMIKGIrkctsgGYYRYDDML 87
Cdd:PRK06754   63 DHDGKPVEEtELKPSAETLLHTHIYNNTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEI 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1243057515  88 VVPIIENTPEEKDLKERMAHAMNeyPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 146
Cdd:PRK06754  137 HIPIIENHADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
37-163 6.78e-16

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: 71.78  E-value: 6.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  37 GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMikgirkctsgGYYRYDDmlvVPIIE-NTPEEKDLKERMAHAMNEYPds 115
Cdd:COG0235    88 DVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP-- 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1243057515 116 cAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMGlDPTQLP 163
Cdd:COG0235   151 -AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
1-166 5.24e-15

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: 69.32  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   1 MFVCDINEQDISGPpaskklKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGQ--EFKITHqemikgirkcts 77
Cdd:cd00398    54 LVVVDAQGKVVEGK------KPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEGLipAGHTAC------------ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  78 gGYYRYDDmlvVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMG- 156
Cdd:cd00398   116 -AVYFTGD---IPCTPYMTPETGEDEIGTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGg 191
                         170
                  ....*....|....
gi 1243057515 157 ----LDPTQLPVGE 166
Cdd:cd00398   192 qlppISLELLNKEY 205
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
1-154 3.63e-72

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: 215.59  E-value: 3.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   1 MFVCDINEQDISGppaskKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGQE-FKITHQEMIKGIRkctsgG 79
Cdd:TIGR03328  47 FLVVDLQGKPVSG-----GLKPSAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----G 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243057515  80 YYRYDDMLVVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKK 154
Cdd:TIGR03328 117 ITTHEDTLVVPIIENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
5-150 3.11e-28

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: 103.01  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   5 DINEQDISGPPASKKLKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGqeFKITHQEMIKgirkctsggyYRY 83
Cdd:pfam00596  48 DLVVVDLDGNVVEGGLKPSSETPLHLAIYRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLG 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243057515  84 DDmlvVPIIEN-TPEEKDLKERMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 150
Cdd:pfam00596 116 GD---IPIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
1-150 1.31e-27

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: 101.56  E-value: 1.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515    1 MFVCDINEQDISGPPAskkLKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMIKGIrkctSGG 79
Cdd:smart01007  48 LVVVDLDGNVVEGGGG---PKPSSETPLHLAIYRARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGG 118
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243057515   80 YYRYDDmLVVPIIENTPEEKDLKERMAHAMNEYPdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 150
Cdd:smart01007 119 EIPYAP-YAGPGTELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
10-146 1.56e-21

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 86.64  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  10 DISGPPASK-KLKKSQCTPLFMNAYTMRGAGAVIHTHSKAA-VMATLLFPGQEFKITHQEMIKGIrkctsgGYYRYDDML 87
Cdd:PRK06754   63 DHDGKPVEEtELKPSAETLLHTHIYNNTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEI 136
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1243057515  88 VVPIIENTPEEKDLKERMAHAMNeyPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 146
Cdd:PRK06754  137 HIPIIENHADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
37-163 6.78e-16

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: 71.78  E-value: 6.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  37 GAGAVIHTHSKAAVMATLLfpGQEFKITHQEMikgirkctsgGYYRYDDmlvVPIIE-NTPEEKDLKERMAHAMNEYPds 115
Cdd:COG0235    88 DVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP-- 150
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1243057515 116 cAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMGlDPTQLP 163
Cdd:COG0235   151 -AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
1-166 5.24e-15

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: 69.32  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   1 MFVCDINEQDISGPpaskklKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGQ--EFKITHqemikgirkcts 77
Cdd:cd00398    54 LVVVDAQGKVVEGK------KPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEGLipAGHTAC------------ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  78 gGYYRYDDmlvVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKMG- 156
Cdd:cd00398   116 -AVYFTGD---IPCTPYMTPETGEDEIGTQRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGg 191
                         170
                  ....*....|....
gi 1243057515 157 ----LDPTQLPVGE 166
Cdd:cd00398   192 qlppISLELLNKEY 205
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
5-155 1.14e-13

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 65.73  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515   5 DINEQDISGPPASKKLKKSQCTPLFMNAYTMR-GAGAVIHTHSKAAVMATLLFPGQEFKITHQEMIKgirkcTSGGYYRY 83
Cdd:PRK09220   55 DFLQVDIAGNAVPSGRKPSAETLLHTQLYRLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQK-----AFAGQTTH 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243057515  84 DDMLVVPIIENTPEEKDLKERMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKM 155
Cdd:PRK09220  130 ETAVVVPIFDNDQDIARLAARVAPYLDAQPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLL 201
PRK06755 PRK06755
hypothetical protein; Validated
87-152 2.22e-05

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 43.10  E-value: 2.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243057515  87 LVVPIIENTPEEKDLKERMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSM 152
Cdd:PRK06755  135 MTIPIVEDEKKFADLLENNVPNFIE--GGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
PRK08660 PRK08660
aldolase;
33-135 2.33e-04

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 39.55  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243057515  33 YTMRGAGAVIHTHSKAAVMATLLfpgqefkithQEMIKGIrkCTSGGYYryddMLVVPIIENTPEEKDLKERMAHAMNEY 112
Cdd:PRK08660   76 YRRTSAKAIVHAHPPYAVALSLL----------EDEIVPL--DSEGLYF----LGTIPVVGGDIGSGELAENVARALSEH 139
                          90       100
                  ....*....|....*....|...
gi 1243057515 113 PdscAVLVRRHGVYVWGETWEKA 135
Cdd:PRK08660  140 K---GVVVRGHGTFAIGKTLEEA 159
 
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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