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Conserved domains on  [gi|489188663|ref|WP_003098054|]
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MULTISPECIES: nitrite reductase small subunit NirD [Pseudomonas]

Protein Classification

nitrite reductase (NAD(P)H) small subunit( domain architecture ID 10131486)

NAD(P)H-dependent nitrite reductase small subunit NirD is required for nitrite assimilation and consists of a Rieske domain, which is a [2Fe-2S] cluster binding domain involved in electron transfer. Assimilatory nitrate and nitrite reductases convert nitrate through nitrite to ammonium.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 3-100 2.58e-56

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: 169.32  E-value: 2.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVAPDQ 82
Cdd:cd03530    1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPDE 80

                         90
                 ....*....|....*...
gi 489188663  83 GCAHRHPVRVENGRVLLG 100
Cdd:cd03530   81 GCVRTFPVKVEDGRVYLG 98
 
Name Accession Description Interval E-value
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 3-100 2.58e-56

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: 169.32  E-value: 2.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVAPDQ 82
Cdd:cd03530    1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPDE 80

                         90
                 ....*....|....*...
gi 489188663  83 GCAHRHPVRVENGRVLLG 100
Cdd:cd03530   81 GCVRTFPVKVEDGRVYLG 98
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 2-101 1.13e-42

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 135.14  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663    2 NWLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHK-GGPLSQGLIYGKR----VACPLHNWQIELESGE 76
Cdd:TIGR02378   1 TWQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKrAFVLSRGIVGDAQgelwVACPLHKRNFRLEDGR 80

                          90       100
                  ....*....|....*....|....*
gi 489188663   77 AVAPDQGCAHRHPVRVENGRVLLGL 101
Cdd:TIGR02378  81 CLEDDSGSVRTYEVRVEDGRVYVAL 105
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-102 5.51e-34

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: 113.01  E-value: 5.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   1 MNWLDICALDEINPLGSRVVAGPKGDIAIFRAaDDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAV-A 79
Cdd:COG2146    1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFRT-DGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLgG 79

                         90       100
                 ....*....|....*....|...
gi 489188663  80 PDQGCAHRHPVRVENGRVLLGLD 102
Cdd:COG2146   80 PATEPLKTYPVRVEDGDVYVDLP 102
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
3-97 1.17e-16

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


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 69.12  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663    3 WLDICALDEInPLGSRVVAGPKG-DIAIFRAADDQVFALDDRCPHKG-GPLSQGLIyGKR-----VACPLHNWQIELESG 75
Cdd:pfam13806   1 WTPVCALDDL-PPGTGVCALVGGrQVAVFRLEDGQVYAIDNRDPFSGaNVLSRGIV-GDLggelvVASPLYKQHFDLKTG 78

                          90       100
                  ....*....|....*....|..
gi 489188663   76 EAVAPDQGCAHRHPVRVENGRV 97
Cdd:pfam13806  79 ECLEDPEVSVPVYPVRVRDGNV 100
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 1-102 2.56e-13

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 60.56  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   1 MNWLDICALDEINPLGS-RVVAGPkgDIAIFRAaDDQVFALDDRCPHKGGPLSQGLIYGK-RVACPLHNWQIELESGEAV 78
Cdd:PRK09965   1 MNRIYACPVADLPEGEAlRVDTSP--VIALFNV-GGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGKAL 77

                         90       100
                 ....*....|....*....|....*
gi 489188663  79 APDQGCAHR-HPVRVENGRVLLGLD 102
Cdd:PRK09965  78 CLPATDPLRtYPVHVEGGDIFIDLP 102
 
Name Accession Description Interval E-value
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 3-100 2.58e-56

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: 169.32  E-value: 2.58e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVAPDQ 82
Cdd:cd03530    1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPDE 80

                         90
                 ....*....|....*...
gi 489188663  83 GCAHRHPVRVENGRVLLG 100
Cdd:cd03530   81 GCVRTFPVKVEDGRVYLG 98
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 2-101 1.13e-42

nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of nitrite reductase [NAD(P)H] (the assimilatory nitrite reductase), which associates with NirB, the large subunit (TIGR02374). In a few bacteria such as Klebsiella pneumoniae and in Fungi, the two regions are fused. [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 131431 [Multi-domain]  Cd Length: 105  Bit Score: 135.14  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663    2 NWLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHK-GGPLSQGLIYGKR----VACPLHNWQIELESGE 76
Cdd:TIGR02378   1 TWQDICAIDDIPEETGVCVLLGDTQIAIFRVPGDQVFAIQNMCPHKrAFVLSRGIVGDAQgelwVACPLHKRNFRLEDGR 80

                          90       100
                  ....*....|....*....|....*
gi 489188663   77 AVAPDQGCAHRHPVRVENGRVLLGL 101
Cdd:TIGR02378  81 CLEDDSGSVRTYEVRVEDGRVYVAL 105
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-102 5.51e-34

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: 113.01  E-value: 5.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   1 MNWLDICALDEINPLGSRVVAGPKGDIAIFRAaDDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAV-A 79
Cdd:COG2146    1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFRT-DGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLgG 79

                         90       100
                 ....*....|....*....|...
gi 489188663  80 PDQGCAHRHPVRVENGRVLLGLD 102
Cdd:COG2146   80 PATEPLKTYPVRVEDGDVYVDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 3-98 8.42e-21

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: 79.46  E-value: 8.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVA-PD 81
Cdd:cd03467    1 WVVVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSgPA 80

                         90
                 ....*....|....*...
gi 489188663  82 QGCAHRHPVRVE-NGRVL 98
Cdd:cd03467   81 PRPLPKYPVKVEgDGVVW 98
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 3-99 5.46e-20

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: 77.14  E-value: 5.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAaDDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVAPDQ 82
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRV-DGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPA 79

                         90
                 ....*....|....*...
gi 489188663  83 GCAHR-HPVRVENGRVLL 99
Cdd:cd03528   80 TEPLKtYPVKVEDGDVYV 97
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
3-97 1.17e-16

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


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 69.12  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663    3 WLDICALDEInPLGSRVVAGPKG-DIAIFRAADDQVFALDDRCPHKG-GPLSQGLIyGKR-----VACPLHNWQIELESG 75
Cdd:pfam13806   1 WTPVCALDDL-PPGTGVCALVGGrQVAVFRLEDGQVYAIDNRDPFSGaNVLSRGIV-GDLggelvVASPLYKQHFDLKTG 78

                          90       100
                  ....*....|....*....|..
gi 489188663   76 EAVAPDQGCAHRHPVRVENGRV 97
Cdd:pfam13806  79 ECLEDPEVSVPVYPVRVRDGNV 100
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 3-100 1.51e-16

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: 68.69  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEInPLGSRVVAGPKGD-IAIFRAADDQVFALDDRCPHKGGP-LSQGLIyGKR-----VACPLHNWQIELESG 75
Cdd:cd03529    1 WQTVCALDDL-PPGSGVAALVGDTqIAIFRLPGREVYAVQNMDPHSRANvLSRGIV-GDIggepvVASPLYKQHFSLKTG 78

                         90       100
                 ....*....|....*....|....*
gi 489188663  76 EAVAPDQGCAHRHPVRVENGRVLLG 100
Cdd:cd03529   79 RCLEDEDVSVATFPVRVEDGEVYVK 103
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 2-84 6.54e-16

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: 66.60  E-value: 6.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663    2 NWLDICALDEI--NPLGSRVVAGPkgDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGK-RVACPLHNWQIElESGEAV 78
Cdd:pfam00355   1 SWYPVCHSSELpeGEPKVVEVGGE--PLVVFRDEDGELYALEDRCPHRGAPLSEGKVNGGgRLECPYHGWRFD-GTGKVV 77


                  ....*..
gi 489188663   79 A-PDQGC 84
Cdd:pfam00355  78 KvPAPRP 84
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 3-104 9.25e-15

Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. T4mo is a four-protein complex that catalyzes the NADH- and O2-dependent hydroxylation of toluene to form p-cresol. T4mo consists of an NADH oxidoreductase (T4moF), a diiron hydroxylase (T4moH), a catalytic effector protein (T4moD), and a Rieske ferredoxin (T4moC). T4moC contains a Rieske domain and functions as an obligate electron carrier between T4moF and T4moH. 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: 239556 [Multi-domain]  Cd Length: 108  Bit Score: 64.28  E-value: 9.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLGSRVVAGPKGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAVAPDQ 82
Cdd:cd03474    1 FTKVCSLDDVWEGEMELVDVDGEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLNPRD 80

                         90       100
                 ....*....|....*....|..
gi 489188663  83 GCAHRHPVRVENGRVLLGLDSV 104
Cdd:cd03474   81 CRLARYPVKVEGGDILVDTEGV 102
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 1-102 2.56e-13

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 60.56  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   1 MNWLDICALDEINPLGS-RVVAGPkgDIAIFRAaDDQVFALDDRCPHKGGPLSQGLIYGK-RVACPLHNWQIELESGEAV 78
Cdd:PRK09965   1 MNRIYACPVADLPEGEAlRVDTSP--VIALFNV-GGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGKAL 77

                         90       100
                 ....*....|....*....|....*
gi 489188663  79 APDQGCAHR-HPVRVENGRVLLGLD 102
Cdd:PRK09965  78 CLPATDPLRtYPVHVEGGDIFIDLP 102
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
26-95 7.81e-13

Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 62.71  E-value: 7.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663  26 DIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIElESGEAVA-PDQG---------CAHRHPVRVENG 95
Cdd:COG5749   43 PLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFD-GDGKCVHiPQLPenqpipknaKVKSYPVQERYG 121
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 33-98 1.09e-11

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: 56.09  E-value: 1.09e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489188663  33 ADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELESGEAV-APDQGCAHRHPVRVENGRVL 98
Cdd:cd03478   29 QGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEdAPALDSLPCYEVEVEDGRVY 95
nirD PRK09511
nitrite reductase small subunit NirD;
1-99 2.55e-11

nitrite reductase small subunit NirD;


Pssm-ID: 181921  Cd Length: 108  Bit Score: 55.42  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   1 MNWLDICALDEINPlGSRVVAGPKGD-IAIFRA-ADDQVFALDDRCP-HKGGPLSQGLIYGKR----VACPLHNWQIELE 73
Cdd:PRK09511   2 SQWKDICKIDDILP-GTGVCALVGDEqVAIFRPyHDEQVFAISNIDPfFQASVLSRGLIAEHQgelwVASPLKKQRFRLS 80

                         90       100
                 ....*....|....*....|....*.
gi 489188663  74 SGEAVAPDQGCAHRHPVRVENGRVLL 99
Cdd:PRK09511  81 DGLCMEDEQFSVKHYDARVKDGVVQL 106
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 3-95 4.71e-11

Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 443676 [Multi-domain]  Cd Length: 298  Bit Score: 57.30  E-value: 4.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEINPLG---SRVVAGpkGDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIEL------- 72
Cdd:COG4638   27 WYYVGHSSELPEPGdylTRTILG--EPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDLdgrlvgi 104

                         90       100
                 ....*....|....*....|....*.
gi 489188663  73 ---ESGEAVAPDQGCAHRHPVRVENG 95
Cdd:COG4638  105 phmEGFPDFDPARAGLRSVPVEEWGG 130
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 26-94 1.79e-10

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: 53.36  E-value: 1.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489188663  26 DIAIFRAADDQVFALDDRCPHKGGPLSQGLIY-GKRVACPLHNWQIELE--------SGEAVAPDQGCAHRHPVRVEN 94
Cdd:cd03469   25 PLVLVRDRDGEVRAFHNVCPHRGARLCEGRGGnAGRLVCPYHGWTYDLDgklvgvprEEGFPGFDKEKLGLRTVPVEE 102
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 26-98 1.38e-09

Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and dicamba O-demethylase oxygenase (DdmC) 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. Vanillate-O-demethylase is a heterodimeric enzyme consisting of a terminal oxygenase (VanA) and reductase (VanB) components. This enzyme reductively catalyzes the conversion of vanillate into protocatechuate and formaldehyde. Protocatechuate and vanillate are important intermediate metabolites in the degradation pathway of lignin-derived compounds such as ferulic acid and vanillin by soil microbes. DDmC is the oxygenase component of a three-component dicamba O-demethylase found in Pseudomonas maltophila, that catalyzes the conversion of a widely used herbicide called herbicide dicamba (2-methoxy-3,6-dichlorobenzoic acid) to DCSA (3,6-dichlorosalicylic acid).


Pssm-ID: 239608 [Multi-domain]  Cd Length: 116  Bit Score: 51.21  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663  26 DIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQ-------IELESGEAVAPDQGCAHrHPVrVENGRVL 98
Cdd:cd03532   28 PVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEfdsdgrcVHMPGQERVPAKACVRS-YPV-VERDALI 105
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 3-97 1.60e-09

Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport through the plant inner chloroplast membrane. This domain represents the N-terminal Rieske domain of the Tic55 oxygenase alpha subunit. Tic55 is closely related to the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO), Ptc52, and ACD1 (accelerated cell death 1). 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.


Pssm-ID: 239830 [Multi-domain]  Cd Length: 134  Bit Score: 51.37  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663   3 WLDICALDEI---NPLGSRVVAGPkgdIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELE------ 73
Cdd:cd04338   18 WYPLYLLKDVptdAPLGLSVYDEP---FVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYHGWQFGGEgkcvki 94

                         90       100
                 ....*....|....*....|....*..
gi 489188663  74 ---SGEAVAPDQGCAHRHPVRVENGRV 97
Cdd:cd04338   95 pqlPADAKIPKNACVKSYEVRDSQGVV 121
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 27-69 1.54e-08

The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase component of 3-ketosteroid 9-alpha-hydroxylase (KSH). The terminal oxygenase component of KSH is a key enzyme in the microbial steroid degradation pathway, catalyzing the 9 alpha-hydroxylation of 4-androstene-3,17-dione (AD) and 1,4-androstadiene-3,17-dione (ADD). KSH is a two-component class IA monooxygenase, with terminal oxygenase (KshA) and oxygenase reductase (KshB) components. KSH activity has been found in many actino- and proteo- bacterial genera including Rhodococcus, Nocardia, Arthrobacter, Mycobacterium, and Burkholderia.


Pssm-ID: 239607 [Multi-domain]  Cd Length: 115  Bit Score: 48.56  E-value: 1.54e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489188663  27 IAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQ 69
Cdd:cd03531   26 LVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWR 68
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 26-95 1.73e-06

Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of a small subfamily of enzymes found in plants as well as oxygenic cyanobacterial photosynthesizers including LLS1 (lethal leaf spot 1, also known as PaO) and ACD1 (accelerated cell death 1). 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. PaO expression increases upon physical wounding of plant leaves and is thought to catalyze a key step in chlorophyll degradation. The Arabidopsis-accelerated cell death gene ACD1 is involved in oxygenation of PaO.


Pssm-ID: 239562 [Multi-domain]  Cd Length: 138  Bit Score: 43.47  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663  26 DIAI-FRAADDQVFALDDRCPHKGGPLSQGLIYGK-RVACPLHNWQIE-----------LESGEAVAPDQGCAHRHPVRV 92
Cdd:cd03480   41 DLVIwWDRNSQQWRAFDDQCPHRLAPLSEGRIDEEgCLECPYHGWSFDgsgscqripqaAEGGKAHTSPRACVASLPTAV 120


                 ...
gi 489188663  93 ENG 95
Cdd:cd03480  121 RQG 123
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 29-78 2.37e-06

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 44.28  E-value: 2.37e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489188663  29 IFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIElESGEAV 78
Cdd:PLN00095 100 LFRDADGEAGCIKDECAHRACPLSLGKLVDGKAQCPYHGWEYE-TGGECA 148
PLN02518 PLN02518
pheophorbide a oxygenase
 39-95 2.49e-05

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 41.39  E-value: 2.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489188663  39 ALDDRCPHKGGPLSQGLI-YGKRVACPLHNW------------QIELESGE--AVAPDQGCAHRHPVRVENG 95
Cdd:PLN02518 128 AFDDKCPHRLAPLSEGRIdENGHLQCSYHGWsfdgcgsctripQAAPEGPEarAVKSPRACAIKFPTMVSQG 199
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 25-99 5.42e-05

Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole 1,9a-dioxygenase (CARDO) 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. OMO catalyzes the NADH-dependent oxidation of the N-heterocyclic aromatic compound 2-oxoquinoline to 8-hydroxy-2-oxoquinoline, the second step in the bacterial degradation of quinoline. OMO consists of a reductase component (OMR) and an oxygenase component (OMO) that together function to shuttle electrons from the reduced pyridine nucleotide to the active site of OMO, where O2 activation and 2-oxoquinoline hydroxylation occurs. CARDO, which contains oxygenase (CARDO-O), ferredoxin (CARDO-F) and ferredoxin reductase (CARDO-R) components, catalyzes the dihydroxylation at the C1 and C9a positions of carbazole. The oxygenase component of OMO and CARDO contain only alpha subunits arranged in a trimeric structure.


Pssm-ID: 239617 [Multi-domain]  Cd Length: 136  Bit Score: 39.33  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663  25 GDIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKR--VACPLHNWQIELESGEAV----APDQGCAHRH-----PVRVE 93
Cdd:cd03548   36 GEPILLRRVDGKVYALKDRCLHRGVPLSKKPECFTKgtITCWYHGWTYRLDDGKLVtilaNPDDPLIGRTglktyPVEEA 115


                 ....*.
gi 489188663  94 NGRVLL 99
Cdd:cd03548  116 KGMIFV 121
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 29-69 1.04e-04

Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the plastid-envelope inner and thylakoid membranes, that catalyzes the conversion of chlorophyllide a to chlorophyllide b. CAO is found not only in plants but also in chlorophytes and prochlorophytes. This domain represents the 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. Cao is closely related to several other plant RO's including Tic 55, a 55 kDa protein associated with protein transport through the inner chloroplast membrane; Ptc 52, a novel 52 kDa protein isolated from chloroplasts; and LLS1/Pao (Lethal-leaf spot 1/pheophorbide a oxygenase).


Pssm-ID: 239829 [Multi-domain]  Cd Length: 129  Bit Score: 38.63  E-value: 1.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489188663  29 IFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQ 69
Cdd:cd04337   44 LFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWE 84
PLN02281 PLN02281
chlorophyllide a oxygenase
 29-69 4.73e-04

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 37.79  E-value: 4.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489188663  29 IFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQ 69
Cdd:PLN02281 247 IFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWE 287
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 26-97 1.19e-03

Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, N-terminal Rieske domain of the oxygenase alpha subunit; composed of the oxygenase alpha subunits of PhDO and similar proteins including 3-chlorobenzoate 3,4-dioxygenase (CBDO), phenoxybenzoate dioxygenase (POB-dioxygenase) and 3-nitrobenzoate oxygenase (MnbA). 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. PhDO and CBDO are two-component RO systems, containing oxygenase and reductase components. PhDO catalyzes the dihydroxylation of phthalate to form the 4,5-dihydro-cis-dihydrodiol of phthalate (DHD). CBDO, together with CbaC dehydrogenase, converts the environmental pollutant 3CBA to protocatechuate (PCA) and 5-Cl-PCA, which are then metabolized by the chromosomal PCA meta (extradiol) ring fission pathway. POB-dioxygenase catalyzes the initial catabolic step in the angular dioxygenation of phenoxybenzoate, converting mono- and dichlorinated phenoxybenzoates to protocatechuate and chlorophenols. These phenoxybenzoates are metabolic products formed during the degradation of pyrethroid insecticides.


Pssm-ID: 239561 [Multi-domain]  Cd Length: 144  Bit Score: 36.07  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188663  26 DIAIFRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIELEsGEAVA----PDQGCAHRH------PVRVENG 95
Cdd:cd03479   46 DLVAFRDTSGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFDVD-GQCLEmpsePPDSQLKQKvrqpayPVRERGG 124


                 ..
gi 489188663  96 RV 97
Cdd:cd03479  125 LV 126
Rieske_RO_Alpha_AntDO cd03538
Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) subfamily, ...
 26-80 2.16e-03

Rieske non-heme iron oxygenase (RO) family, Anthranilate 1,2-dioxygenase (AntDO) 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. AntDO converts anthranilate to catechol, a naturally occurring compound formed through tryptophan degradation and an important intermediate in the metabolism of many N-heterocyclic compounds such as indole, o-nitrobenzoate, carbazole, and quinaldine.


Pssm-ID: 239612 [Multi-domain]  Cd Length: 146  Bit Score: 35.13  E-value: 2.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489188663  26 DIAIFRAADDQVFALDDRCPHKGGPLSQ---GLIyGKRVACPLHNWQIELESGEAVAP 80
Cdd:cd03538   47 PVVMVRHTDGSVHVLYNRCPHKGTKIVSdgcGNT-GKFFRCPYHAWSFKTDGSLLAIP 103
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 30-78 2.98e-03

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of aminopyrrolnitrin oxygenase (PrnD). PrnD is a novel Rieske N-oxygenase that catalyzes the final step in the pyrrolnitrin biosynthetic pathway, the oxidation of the amino group in aminopyrrolnitrin to a nitro group, forming the antibiotic pyrrolnitrin. The biosynthesis of pyrrolnitrin is one of the best examples of enzyme-catalyzed arylamine oxidation. Although arylamine oxygenases are widely distributed within the microbial world and used in a variety of metabolic reactions, PrnD represents one of only two known examples of arylamine oxygenases or N-oxygenases involved in arylnitro group formation, the other being AurF involved in aureothin biosynthesis.


Pssm-ID: 239611 [Multi-domain]  Cd Length: 123  Bit Score: 34.52  E-value: 2.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489188663  30 FRAADDQVFALDDRCPHKGGPLSQGLIYGKRVACPLHNWQIElESGEAV 78
Cdd:cd03537   30 WRGATGRAVVMDRHCSHLGANLADGRVKDGCIQCPFHHWRYD-EQGQCV 77
 
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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