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Conserved domains on  [gi|1229266194|gb|OYC99671|]
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flavin reductase-like protein (plasmid) [Rhizobium sp. N4311]

Protein Classification

NUDIX hydrolase; bifunctional NUDIX hydrolase family protein/GNAT family N-acetyltransferase( domain architecture ID 10658198)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg2+ or Mn2+ for its activity| bifunctional GNAT family N-acetyltransferase/NUDIX hydrolase which contains an N-terminal domain which may catalyze the transfer of an acetyl group from acetyl-CoA to a substrate and a C-terminal domain which may catalyze the hydrolysis of nucleoside diphosphates linked to other moieties and require a divalent cation, such as Mg2+ or Mn2+ for its activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 13-164 2.47e-54

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


:

Pssm-ID: 441458  Cd Length: 160  Bit Score: 175.02  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  13 DPIALRRAFGTFVTGVTVITTRDEDGTPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISG 92
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  93 TFASKSP---DKFQSVTHDHI--HTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSPT---APLGFCRGRYAS 164
Cdd:COG1853    81 RFAGRSGrgvDKFAGAGLTTAsgEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVHVDEDvdgRPLLYLGGRYRR 160
NUDIX_Hydrolase super family cl00447
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 179-291 1.17e-04

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.


The actual alignment was detected with superfamily member cd04511:

Pssm-ID: 469772 [Multi-domain]  Cd Length: 123  Bit Score: 41.02  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194 179 MIIGYLIEAGDGLLL-------RsdgRGGWVLPSARRRKADSqlVVEGgdALRLVPEET-------FLYSVFDVADSDPG 244
Cdd:cd04511     3 IVVGCLPEWEGKVLLcrraiepR---KGYWTLPAGFMELGET--TEQG--AARETREEAgarveigSLYAVYSLPHISQV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229266194 245 YLVYRARLA----GEGEEvnlPADLRFFGIDDLPYEAIATHELRSMLRRYV 291
Cdd:cd04511    76 YIIFRARLLspdfSPGPE---SLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 13-164 2.47e-54

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 175.02  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  13 DPIALRRAFGTFVTGVTVITTRDEDGTPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISG 92
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  93 TFASKSP---DKFQSVTHDHI--HTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSPT---APLGFCRGRYAS 164
Cdd:COG1853    81 RFAGRSGrgvDKFAGAGLTTAsgEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVHVDEDvdgRPLLYLGGRYRR 160
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 21-162 1.32e-53

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 172.73  E-value: 1.32e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194   21 FGTFVTGVTVITTRDEDGTPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFASKS-P 99
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKSgA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229266194  100 DKFQSV---THDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSP-TAPLGFCRGRY 162
Cdd:smart00903  81 DRFEGVawgLTEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDdGEPLVYHRGGY 147
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 21-166 1.58e-46

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 154.36  E-value: 1.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  21 FGTFVTGVTVITTRDEDGtPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFASKSP- 99
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGE-PNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRSGr 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194 100 DKFQSVTHDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGT---SPTAPLGFCRGRYASVK 166
Cdd:pfam01613  80 DKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVdedADGEPLLYYRRRYRSLG 149
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 17-151 3.83e-06

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 46.57  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  17 LRRAFGTFVTGVTVITTRDEDGTPrGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFAS 96
Cdd:PRK15486   10 FRDAMASLSAAVNIVTTAGDAGRC-GITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHFAG 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229266194  97 KS----PDKFQSVTHDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSP 151
Cdd:PRK15486   89 MTgmamEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSA 147
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 179-291 1.17e-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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 41.02  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194 179 MIIGYLIEAGDGLLL-------RsdgRGGWVLPSARRRKADSqlVVEGgdALRLVPEET-------FLYSVFDVADSDPG 244
Cdd:cd04511     3 IVVGCLPEWEGKVLLcrraiepR---KGYWTLPAGFMELGET--TEQG--AARETREEAgarveigSLYAVYSLPHISQV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229266194 245 YLVYRARLA----GEGEEvnlPADLRFFGIDDLPYEAIATHELRSMLRRYV 291
Cdd:cd04511    76 YIIFRARLLspdfSPGPE---SLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
 
Name Accession Description Interval E-value
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 13-164 2.47e-54

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 175.02  E-value: 2.47e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  13 DPIALRRAFGTFVTGVTVITTRDEDGTPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISG 92
Cdd:COG1853     1 MPDAFRDALGRLAPGVAVVTTRDADGRPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  93 TFASKSP---DKFQSVTHDHI--HTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSPT---APLGFCRGRYAS 164
Cdd:COG1853    81 RFAGRSGrgvDKFAGAGLTTAsgEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVHVDEDvdgRPLLYLGGRYRR 160
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 21-162 1.32e-53

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 172.73  E-value: 1.32e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194   21 FGTFVTGVTVITTRDEDGTPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFASKS-P 99
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGGRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKSgA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1229266194  100 DKFQSV---THDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSP-TAPLGFCRGRY 162
Cdd:smart00903  81 DRFEGVawgLTEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDdGEPLVYHRGGY 147
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 21-166 1.58e-46

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 154.36  E-value: 1.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  21 FGTFVTGVTVITTRDEDGtPRGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFASKSP- 99
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGE-PNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRSGr 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194 100 DKFQSVTHDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGT---SPTAPLGFCRGRYASVK 166
Cdd:pfam01613  80 DKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVdedADGEPLLYYRRRYRSLG 149
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 17-151 3.83e-06

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 46.57  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194  17 LRRAFGTFVTGVTVITTRDEDGTPrGMTANSFTSVSLDPPLLLVCVAKAASSYRAFTNAGCFAVNILHEGQVDISGTFAS 96
Cdd:PRK15486   10 FRDAMASLSAAVNIVTTAGDAGRC-GITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQELMARHFAG 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1229266194  97 KS----PDKFQSVTHDHIHTGAPVLTDSLTWFDCTTYSAVDAGDHTVLIGQVRAFGTSP 151
Cdd:PRK15486   89 MTgmamEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSA 147
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 179-291 1.17e-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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 41.02  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1229266194 179 MIIGYLIEAGDGLLL-------RsdgRGGWVLPSARRRKADSqlVVEGgdALRLVPEET-------FLYSVFDVADSDPG 244
Cdd:cd04511     3 IVVGCLPEWEGKVLLcrraiepR---KGYWTLPAGFMELGET--TEQG--AARETREEAgarveigSLYAVYSLPHISQV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1229266194 245 YLVYRARLA----GEGEEvnlPADLRFFGIDDLPYEAIATHELRSMLRRYV 291
Cdd:cd04511    76 YIIFRARLLspdfSPGPE---SLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
 
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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