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Conserved domains on  [gi|1622826298|ref|XP_028703189|]
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nucleoside diphosphate-linked moiety X motif 17 isoform X1 [Macaca mulatta]

Protein Classification

nucleoside diphosphate-linked moiety X motif 17( domain architecture ID 10140411)

nucleoside diphosphate-linked moiety X motif 17 (NUDT17) may mediate the hydrolysis of some nucleoside diphosphate derivatives

CATH:  3.90.79.10
EC:  3.6.1.-
Gene Ontology:  GO:0035529|GO:0019677|GO:0046872|GO:0006742|GO:0006734
PubMed:  15581572|16378245|27936487
SCOP:  3000098

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
 154-281 5.04e-49

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


:

Pssm-ID: 467576 [Multi-domain]  Cd Length: 135  Bit Score: 160.92  E-value: 5.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 154 VDLGVAVILQSSDKTVLLTRRARTLSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQfSWVPLGLWESAYPP 224
Cdd:cd04694     1 VDVGVVVLIEDSDDRVLLTRRAKHMRTFPGVWVPpgghvelgeSLLEAGLRELQEETGLEVSDIQ-SLSLLGLWESVYPT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622826298 225 RLSWGLPKYHHIVLYLLVISQESqQQLQARIQPNPSEVSALMWLTPDVAAAVAATED 281
Cdd:cd04694    80 LLSIGLPKRHHIVVYYLVKLSES-HENQEQLKLQEDEVDAAVWLPKSLLAKLLEAED 135
 
Name Accession Description Interval E-value
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
 154-281 5.04e-49

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467576 [Multi-domain]  Cd Length: 135  Bit Score: 160.92  E-value: 5.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 154 VDLGVAVILQSSDKTVLLTRRARTLSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQfSWVPLGLWESAYPP 224
Cdd:cd04694     1 VDVGVVVLIEDSDDRVLLTRRAKHMRTFPGVWVPpgghvelgeSLLEAGLRELQEETGLEVSDIQ-SLSLLGLWESVYPT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622826298 225 RLSWGLPKYHHIVLYLLVISQESqQQLQARIQPNPSEVSALMWLTPDVAAAVAATED 281
Cdd:cd04694    80 LLSIGLPKRHHIVVYYLVKLSES-HENQEQLKLQEDEVDAAVWLPKSLLAKLLEAED 135
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 158-281 5.83e-08

Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441052 [Multi-domain]  Cd Length: 162  Bit Score: 51.74  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 158 VAVILQSSDKTVLLTRRARTLSVSPNLW------YPR----LLDGGLRELWEECGLHLPQgqfSWVPLGlwesAYPPRLS 227
Cdd:COG1443    32 FSVFVFNSDGRLLLQRRALTKDHWPGLWdntvcgHPRagetYEEAAVRELEEELGITVDD---DLRPLG----TFRYRAV 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622826298 228 WGLPKYHHIVLYLLVIsqesqqQLQARIQPNPSEVSALMWLTP-DVAAAVAATED 281
Cdd:COG1443   105 DANGLVENEFCHVFVA------RLDGPLTPQPEEVAEVRWVTLeELLALLEAGPE 153
NUDIX pfam00293
NUDIX domain;
156-275 3.93e-05

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 42.86  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 156 LGVAVILQSSDKTVLLTRRARtlSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQFswvpLGLWESAYPPRL 226
Cdd:pfam00293   4 VAVGVVLLNEKGRVLLVRRSK--KPFPGWWSLpggkvepgeTPEEAARRELEEETGLEPELLEL----LGSLHYLAPFDG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622826298 227 SWGLPkyhHIVLYLLVISQESQQQLQAriqpnPSEVSALMWLTPDVAAA 275
Cdd:pfam00293  78 RFPDE---HEILYVFLAEVEGELEPDP-----DGEVEEVRWVPLEELLL 118
 
Name Accession Description Interval E-value
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
 154-281 5.04e-49

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467576 [Multi-domain]  Cd Length: 135  Bit Score: 160.92  E-value: 5.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 154 VDLGVAVILQSSDKTVLLTRRARTLSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQfSWVPLGLWESAYPP 224
Cdd:cd04694     1 VDVGVVVLIEDSDDRVLLTRRAKHMRTFPGVWVPpgghvelgeSLLEAGLRELQEETGLEVSDIQ-SLSLLGLWESVYPT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622826298 225 RLSWGLPKYHHIVLYLLVISQESqQQLQARIQPNPSEVSALMWLTPDVAAAVAATED 281
Cdd:cd04694    80 LLSIGLPKRHHIVVYYLVKLSES-HENQEQLKLQEDEVDAAVWLPKSLLAKLLEAED 135
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 158-281 5.83e-08

Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441052 [Multi-domain]  Cd Length: 162  Bit Score: 51.74  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 158 VAVILQSSDKTVLLTRRARTLSVSPNLW------YPR----LLDGGLRELWEECGLHLPQgqfSWVPLGlwesAYPPRLS 227
Cdd:COG1443    32 FSVFVFNSDGRLLLQRRALTKDHWPGLWdntvcgHPRagetYEEAAVRELEEELGITVDD---DLRPLG----TFRYRAV 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622826298 228 WGLPKYHHIVLYLLVIsqesqqQLQARIQPNPSEVSALMWLTP-DVAAAVAATED 281
Cdd:COG1443   105 DANGLVENEFCHVFVA------RLDGPLTPQPEEVAEVRWVTLeELLALLEAGPE 153
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 156-269 8.43e-07

NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467528 [Multi-domain]  Cd Length: 106  Bit Score: 47.01  E-value: 8.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 156 LGVAVILQSSDKTVLLTRRARTlsVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQfswvPLGLWESAYPPRl 226
Cdd:cd02883     1 VAVGAVVFDDEGRVLLVRRSDG--PGPGGWELpgggvepgeTPEEAAVREVREETGLDVEVLR----LLGVYEFPDPDE- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622826298 227 swglPKYHHIVLYLLVISQESQQQLQariqpnPSEVSALMWLT 269
Cdd:cd02883    74 ----GRHVVVLVFLARVVGGEPPPLD------DEEISEVRWVP 106
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 157-278 5.19e-06

8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];


Pssm-ID: 440260 [Multi-domain]  Cd Length: 143  Bit Score: 45.79  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 157 GVAVILQSSDKTVLLTRRARTlSVSPNLWYP---------RLLDGGLRELWEECGLHLPQgqfsWVPLGlwesayppRLS 227
Cdd:COG0494    15 AVVVVLLDDDGRVLLVRRYRY-GVGPGLWEFpggkiepgeSPEEAALRELREETGLTAED----LELLG--------ELP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622826298 228 WGLPKYHHIVLYLL-VISQESQQQLqariqPNPSEVSALMWLTPDVAAAVAA 278
Cdd:COG0494    82 SPGYTDEKVHVFLArGLGPGEEVGL-----DDEDEFIEVRWVPLDEALALVT 128
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 161-270 2.37e-05

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467574 [Multi-domain]  Cd Length: 142  Bit Score: 43.70  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 161 ILQSSDKTVLLTRRARTLSVSPNLW-------------YprlLDGGLRELWEECGLHLPQGQFswVPLGLWESaypprlS 227
Cdd:cd04692    33 LVNPEEGRLLLQKRSANKDDFPGLWdisaaghidagetY---EEAAVRELEEELGLTVSPEDL--IFLGVIRE------E 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622826298 228 WGLPKYH---HIVLYLLVISQESQQqlqarIQPNPSEVSALMWLTP 270
Cdd:cd04692   102 VIGGDFIdneFVHVYLYETDRPLEE-----FKLQPEEVAGVVFVDL 142
NUDIX pfam00293
NUDIX domain;
156-275 3.93e-05

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 42.86  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 156 LGVAVILQSSDKTVLLTRRARtlSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQFswvpLGLWESAYPPRL 226
Cdd:pfam00293   4 VAVGVVLLNEKGRVLLVRRSK--KPFPGWWSLpggkvepgeTPEEAARRELEEETGLEPELLEL----LGSLHYLAPFDG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622826298 227 SWGLPkyhHIVLYLLVISQESQQQLQAriqpnPSEVSALMWLTPDVAAA 275
Cdd:pfam00293  78 RFPDE---HEILYVFLAEVEGELEPDP-----DGEVEEVRWVPLEELLL 118
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
156-271 2.32e-04

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 40.35  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 156 LGVAVILQSSDKTVLLTRRARtlSVSPNLWYP---------RLLDGGLRELWEECGLHLPQGQFswvpLGLWESAYPprl 226
Cdd:COG1051     7 VAVDAVIFRKDGRVLLVRRAD--EPGKGLWALpggkvepgeTPEEAALRELREETGLEVEVLEL----LGVFDHPDR--- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622826298 227 swglpkYHHIVLYLLVISQESQQQLqariqpnPSEVSALMWLTPD 271
Cdd:COG1051    78 ------GHVVSVAFLAEVLSGEPRA-------DDEIDEARWFPLD 109
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 158-271 5.14e-04

uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467575 [Multi-domain]  Cd Length: 157  Bit Score: 40.20  E-value: 5.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622826298 158 VAVILQSSDKTVLLTRRARTLSVSPNLWYPRL----------LDGGLRELWEECGLHLPQGQfswvpLGLWESAYpprls 227
Cdd:cd04693    32 VHVWIFNSDGEILIQQRSPDKKGFPGMWEASTggsvlagetsLEAAIRELKEELGIDLDADE-----LRPILTIR----- 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622826298 228 wglpKYHHIV-LYLLVISQE-SQQQLQariqpnPSEVSALMWLTPD 271
Cdd:cd04693   102 ----FDNGFDdIYLFRKDVDiEDLTLQ------KEEVQDVKWVTLE 137
 
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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