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Conserved domains on  [gi|197100700|ref|NP_001124541|]
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Rieske domain-containing protein [Mus musculus]

Protein Classification

Rieske (2Fe-2S) protein( domain architecture ID 10005408)

Rieske (2Fe-2S) protein similar to Sulfolobus tokodaii sulredoxin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 16-134 1.67e-21

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 82.97  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  16 TSVCVGREEDIRKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGL 95
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDG----GVVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100700  96 yqsinpKDPSAKPkwcskgvkQRIHTVKVDNGNIYVTLS 134
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 16-134 1.67e-21

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 82.97  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  16 TSVCVGREEDIRKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGL 95
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDG----GVVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100700  96 yqsinpKDPSAKPkwcskgvkQRIHTVKVDNGNIYVTLS 134
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 18-96 2.00e-19

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 77.91  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  18 VCVGREEDIRKSERMTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGLY 96
Cdd:cd03467    2 VVVGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGED----GCIVCPCHGSRFDLRTGEVVS 77
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
15-131 5.12e-10

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 53.33  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700   15 YTSVCvgREEDIRKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSG-GPLHLGEIEDFNGQSCIVCPWHKYKITLATG 92
Cdd:pfam13806   1 WTPVC--ALDDLPPGTGVCALVGGRQVAVFrLEDGQVYAIDNRDPFSGaNVLSRGIVGDLGGELVVASPLYKQHFDLKTG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 197100700   93 EGLyqsinpKDPSakpkwcskgVKQRIHTVKVDNGNIYV 131
Cdd:pfam13806  79 ECL------EDPE---------VSVPVYPVRVRDGNVEV 102
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 16-136 1.78e-08

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 49.39  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  16 TSVCVGREEDIRKSERMTaVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIV-CPWHKYKITLATGEg 94
Cdd:PRK09965   2 NRIYACPVADLPEGEALR-VDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLED----DATVeCPLHAASFCLRTGK- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 197100700  95 lyqsinPKDPSAKpkwcskgVKQRIHTVKVDNGNIYVTLSKE 136
Cdd:PRK09965  76 ------ALCLPAT-------DPLRTYPVHVEGGDIFIDLPEA 104
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 16-134 1.67e-21

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441749 [Multi-domain]  Cd Length: 103  Bit Score: 82.97  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  16 TSVCVGREEDIRKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGL 95
Cdd:COG2146    2 SEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDG----GVVTCPLHGARFDLRTGECL 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100700  96 yqsinpKDPSAKPkwcskgvkQRIHTVKVDNGNIYVTLS 134
Cdd:COG2146   78 ------GGPATEP--------LKTYPVRVEDGDVYVDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 18-96 2.00e-19

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.


Pssm-ID: 239550 [Multi-domain]  Cd Length: 98  Bit Score: 77.91  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  18 VCVGREEDIRKSERMTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGLY 96
Cdd:cd03467    2 VVVGALSELPPGGGRVVVVGGGPVVVVRREgGEVYALSNRCTHQGCPLSEGEGED----GCIVCPCHGSRFDLRTGEVVS 77
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 20-131 5.29e-15

Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar to the Bacillus subtilis small subunit of assimilatory nitrite reductase containing a Rieske domain. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.


Pssm-ID: 239606 [Multi-domain]  Cd Length: 98  Bit Score: 66.48  E-value: 5.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  20 VGREEDIRKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGEGLYqs 98
Cdd:cd03530    4 IGALEDIPPRGARKVQTGGGEIAVFrTADDEVFALENRCPHKGGPLSEGIVHG----EYVTCPLHNWVIDLETGEAQG-- 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 197100700  99 inPKDPSAKPkwcskgvkqriHTVKVDNGNIYV 131
Cdd:cd03530   78 --PDEGCVRT-----------FPVKVEDGRVYL 97
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
15-131 5.12e-10

Rieske-like [2Fe-2S] domain;


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 53.33  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700   15 YTSVCvgREEDIRKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSG-GPLHLGEIEDFNGQSCIVCPWHKYKITLATG 92
Cdd:pfam13806   1 WTPVC--ALDDLPPGTGVCALVGGRQVAVFrLEDGQVYAIDNRDPFSGaNVLSRGIVGDLGGELVVASPLYKQHFDLKTG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 197100700   93 EGLyqsinpKDPSakpkwcskgVKQRIHTVKVDNGNIYV 131
Cdd:pfam13806  79 ECL------EDPE---------VSVPVYPVRVRDGNVEV 102
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 18-131 2.73e-09

Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 51.33  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  18 VCVGREEDIrKSERMTAVVHD-REVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDFngqsCIVCPWHKYKITLATGEgly 96
Cdd:cd03528    2 VRVCAVDEL-PEGEPKRVDVGgRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGG----VIECPLHGGRFDLRTGK--- 73

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 197100700  97 qsinpkdPSAKPkwCSKGVKqrIHTVKVDNGNIYV 131
Cdd:cd03528   74 -------ALSLP--ATEPLK--TYPVKVEDGDVYV 97
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 18-84 4.24e-09

Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines coordinate one Fe ion, while the other Fe ion is coordinated by two conserved histidines. In hyperthermophilic archaea there is a SKTPCX(2-3)C motif at the C-terminus. The cysteines in this motif form a disulphide bridge, which stabilizes the protein.


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 50.81  E-value: 4.24e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197100700   18 VCVGREEDIRKSERMTAVVHDREVVIF-YHKGEYHAMDIRCYHSGGPLHLGEIedfNGQSCIVCPWHK 84
Cdd:pfam00355   3 YPVCHSSELPEGEPKVVEVGGEPLVVFrDEDGELYALEDRCPHRGAPLSEGKV---NGGGRLECPYHG 67
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 20-93 5.95e-09

AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family show similarity to human AIFL, containing an N-terminal Rieske domain and a C-terminal pyridine nucleotide-disulfide oxidoreductase domain (Pyr_redox). The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. AIFL shares 35% homology with human AIF (apoptosis-inducing factor), mainly in the Pyr_redox domain. AIFL is predominantly localized to the mitochondria. AIFL induces apoptosis in a caspase-dependent manner.


Pssm-ID: 239560 [Multi-domain]  Cd Length: 95  Bit Score: 50.31  E-value: 5.95e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 197100700  20 VGREEDIRKSERMTAVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIVCPWHKYKITLATGE 93
Cdd:cd03478    3 VCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTD----GRIRCPWHGACFNLRTGD 72
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 16-136 1.78e-08

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 49.39  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  16 TSVCVGREEDIRKSERMTaVVHDREVVIFYHKGEYHAMDIRCYHSGGPLHLGEIEDfngqSCIV-CPWHKYKITLATGEg 94
Cdd:PRK09965   2 NRIYACPVADLPEGEALR-VDTSPVIALFNVGGEFYAIDDRCSHGNASLSEGYLED----DATVeCPLHAASFCLRTGK- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 197100700  95 lyqsinPKDPSAKpkwcskgVKQRIHTVKVDNGNIYVTLSKE 136
Cdd:PRK09965  76 ------ALCLPAT-------DPLRTYPVHVEGGDIFIDLPEA 104
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 18-137 2.46e-04

Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha subunit; The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The oxygenase component may contain alpha and beta subunits, with the beta subunit having a purely structural function. Some oxygenase components contain only an alpha subunit. The oxygenase alpha subunit has two domains, an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from the reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. Reduced pyridine nucleotide is used as the initial source of two electrons for dioxygen activation.


Pssm-ID: 239551 [Multi-domain]  Cd Length: 118  Bit Score: 38.72  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  18 VCVGREEDIRKSER-MTAVVHDREVVIFYHK-GEYHAMDIRCYHSGGPLHLGEIedfNGQSCIVCPWH--KYKitlATGE 93
Cdd:cd03469    2 YFVGHSSELPEPGDyVTLELGGEPLVLVRDRdGEVRAFHNVCPHRGARLCEGRG---GNAGRLVCPYHgwTYD---LDGK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 197100700  94 GLYQSINPKDPSAKPKwcskgvKQRIHTVKVD--NGNIYVTLSKEP 137
Cdd:cd03469   76 LVGVPREEGFPGFDKE------KLGLRTVPVEewGGLIFVNLDPDA 115
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 15-131 4.01e-04

Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium. Members include bacterial and fungal proteins. The bacterial NirD contains a single Rieske domain while fungal proteins have a C-terminal Rieske domain in addition to several other domains. The fungal NirD is involved in nutrient acquisition, functioning at the soil/fungus interface to control nutrient exchange between the fungus and the host plant. The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. The Rieske [2Fe-2S] cluster is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In this family, only a few members contain these residues. Other members may have lost the ability to bind the Rieske [2Fe-2S] cluster.


Pssm-ID: 239605 [Multi-domain]  Cd Length: 103  Bit Score: 37.88  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197100700  15 YTSVCvgREEDIRKSERMTAVVHDREVVIFY-HKGEYHAMDIRCYHSGGP-LHLGEIEDFNGQSCIVCPWHKYKITLATG 92
Cdd:cd03529    1 WQTVC--ALDDLPPGSGVAALVGDTQIAIFRlPGREVYAVQNMDPHSRANvLSRGIVGDIGGEPVVASPLYKQHFSLKTG 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 197100700  93 EGLyqsinpKDPSAKPKWcskgvkqriHTVKVDNGNIYV 131
Cdd:cd03529   79 RCL------EDEDVSVAT---------FPVRVEDGEVYV 102
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 48-108 8.05e-03

Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; ROs comprise a large class of aromatic ring-hydroxylating dioxygenases that enable microorganisms to tolerate and utilize aromatic compounds for growth. The oxygenase alpha subunit contains an N-terminal Rieske domain with an [2Fe-2S] cluster and a C-terminal catalytic domain with a mononuclear Fe(II) binding site. The Rieske [2Fe-2S] cluster accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron for catalysis. CMO is a novel RO found in certain plants which catalyzes the first step in betaine synthesis. CMO is not found in animals or bacteria. In these organisms, the first step in betaine synthesis is catalyzed by either the membrane-bound choline dehydrogenase (CDH) or the soluble choline oxidase (COX).


Pssm-ID: 239614 [Multi-domain]  Cd Length: 118  Bit Score: 34.45  E-value: 8.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197100700  48 GEYHAMDIRCYHSGGPLHLGeiedfNGQ-SCIVCPWHKY---------KITLATGEglyQSINPKDPSAKP 108
Cdd:cd03541   35 GKLHAFHNVCTHRASILACG-----SGKkSCFVCPYHGWvygldgsltKATQATGI---QNFNPKELGLVP 97
 
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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