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Conserved domains on  [gi|2753127405|ref|WP_353738371|]
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nitrite reductase small subunit NirD [Limnobacter sp.]

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 ...
 13-111 2.22e-50

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: 154.69  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPaGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREPD 92
Cdd:cd03530     1 WIDIGALEDIPPRGARKVQTG-GGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPD 79

                          90
                  ....*....|....*....
gi 2753127405  93 EGCTAKFTVQVVDGRVQLS 111
Cdd:cd03530    80 EGCVRTFPVKVEDGRVYLG 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 ...
 13-111 2.22e-50

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: 154.69  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPaGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREPD 92
Cdd:cd03530     1 WIDIGALEDIPPRGARKVQTG-GGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPD 79

                          90
                  ....*....|....*....
gi 2753127405  93 EGCTAKFTVQVVDGRVQLS 111
Cdd:cd03530    80 EGCVRTFPVKVEDGRVYLG 98
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 12-110 1.22e-32

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: 110.10  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPVLGSRIVRRPAGQdIALFRNAEEQVFALLDECPHKKG-PLSQGIVHG----TTVTCPLHNWQIGLNDG 86
Cdd:TIGR02378   1 TWQDICAIDDIPEETGVCVLLGDTQ-IAIFRVPGDQVFAIQNMCPHKRAfVLSRGIVGDaqgeLWVACPLHKRNFRLEDG 79

                          90       100
                  ....*....|....*....|....
gi 2753127405  87 CAREPDEGCTAKFTVQVVDGRVQL 110
Cdd:TIGR02378  80 RCLEDDSGSVRTYEVRVEDGRVYV 103
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 11-114 2.32e-31

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: 106.85  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  11 MQWIEICGVEDIPVLGSRIVRrPAGQDIALFRNaEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDG-CAR 89
Cdd:COG2146     1 MSEVKVCALDDLPEGGGVVVE-VGGKQIAVFRT-DGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGeCLG 78

                          90       100
                  ....*....|....*....|....*
gi 2753127405  90 EPDEGCTAKFTVQVVDGRVQLSAEE 114
Cdd:COG2146    79 GPATEPLKTYPVRVEDGDVYVDLPE 103
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 12-99 2.87e-19

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: 75.85  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPvLGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVH-GTTVTCPLHNWQIGLNDGCARE 90
Cdd:pfam00355   1 SWYPVCHSSELP-EGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNgGGRLECPYHGWRFDGTGKVVKV 79


                  ....*....
gi 2753127405  91 PDEGCTAKF 99
Cdd:pfam00355  80 PAPRPLKSY 88
nirD PRK09511
nitrite reductase small subunit NirD;
11-112 4.16e-12

nitrite reductase small subunit NirD;


Pssm-ID: 181921  Cd Length: 108  Bit Score: 58.12  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  11 MQWIEICGVEDIpVLGSRIVRRPAGQDIALFR-NAEEQVFALLDECPHKKGP-LSQGIV---HGTT-VTCPLHNWQIGLN 84
Cdd:PRK09511    2 SQWKDICKIDDI-LPGTGVCALVGDEQVAIFRpYHDEQVFAISNIDPFFQASvLSRGLIaehQGELwVASPLKKQRFRLS 80

                          90       100
                  ....*....|....*....|....*...
gi 2753127405  85 DGCAREPDEGCTAKFTVQVVDGRVQLSA 112
Cdd:PRK09511   81 DGLCMEDEQFSVKHYDARVKDGVVQLRA 108
 
Name Accession Description Interval E-value
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 13-111 2.22e-50

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: 154.69  E-value: 2.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPaGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREPD 92
Cdd:cd03530     1 WIDIGALEDIPPRGARKVQTG-GGEIAVFRTADDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEAQGPD 79

                          90
                  ....*....|....*....
gi 2753127405  93 EGCTAKFTVQVVDGRVQLS 111
Cdd:cd03530    80 EGCVRTFPVKVEDGRVYLG 98
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 12-110 1.22e-32

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: 110.10  E-value: 1.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPVLGSRIVRRPAGQdIALFRNAEEQVFALLDECPHKKG-PLSQGIVHG----TTVTCPLHNWQIGLNDG 86
Cdd:TIGR02378   1 TWQDICAIDDIPEETGVCVLLGDTQ-IAIFRVPGDQVFAIQNMCPHKRAfVLSRGIVGDaqgeLWVACPLHKRNFRLEDG 79

                          90       100
                  ....*....|....*....|....
gi 2753127405  87 CAREPDEGCTAKFTVQVVDGRVQL 110
Cdd:TIGR02378  80 RCLEDDSGSVRTYEVRVEDGRVYV 103
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 11-114 2.32e-31

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: 106.85  E-value: 2.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  11 MQWIEICGVEDIPVLGSRIVRrPAGQDIALFRNaEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDG-CAR 89
Cdd:COG2146     1 MSEVKVCALDDLPEGGGVVVE-VGGKQIAVFRT-DGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGeCLG 78

                          90       100
                  ....*....|....*....|....*
gi 2753127405  90 EPDEGCTAKFTVQVVDGRVQLSAEE 114
Cdd:COG2146    79 GPATEPLKTYPVRVEDGDVYVDLPE 103
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 12-99 2.87e-19

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: 75.85  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPvLGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVH-GTTVTCPLHNWQIGLNDGCARE 90
Cdd:pfam00355   1 SWYPVCHSSELP-EGEPKVVEVGGEPLVVFRDEDGELYALEDRCPHRGAPLSEGKVNgGGRLECPYHGWRFDGTGKVVKV 79


                  ....*....
gi 2753127405  91 PDEGCTAKF 99
Cdd:pfam00355  80 PAPRPLKSY 88
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 13-106 1.05e-16

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: 69.44  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVlGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDG-CAREP 91
Cdd:cd03467     1 WVVVGALSELPP-GGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGeVVSGP 79

                          90
                  ....*....|....*
gi 2753127405  92 DEGCTAKFTVQVVDG 106
Cdd:cd03467    80 APRPLPKYPVKVEGD 94
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 13-111 1.37e-14

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: 64.05  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVlGSRIVRRPAGQDIALFRnAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDG-CAREP 91
Cdd:cd03528     1 WVRVCAVDELPE-GEPKRVDVGGRPIAVYR-VDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGkALSLP 78

                          90       100
                  ....*....|....*....|
gi 2753127405  92 DEGCTAKFTVQVVDGRVQLS 111
Cdd:cd03528    79 ATEPLKTYPVKVEDGDVYVD 98
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 13-110 2.89e-14

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: 63.30  E-value: 2.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVlGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGP-LSQGIVhGT-----TVTCPLHNWQIGLNDG 86
Cdd:cd03529     1 WQTVCALDDLPP-GSGVAALVGDTQIAIFRLPGREVYAVQNMDPHSRANvLSRGIV-GDiggepVVASPLYKQHFSLKTG 78

                          90       100
                  ....*....|....*....|....
gi 2753127405  87 CAREPDEGCTAKFTVQVVDGRVQL 110
Cdd:cd03529    79 RCLEDEDVSVATFPVRVEDGEVYV 102
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
13-111 9.90e-14

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


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 61.80  E-value: 9.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVlGSRIVRRPAGQDIALFRNAEEQVFALLDECP-HKKGPLSQGIV--HGT--TVTCPLHNWQIGLNDGC 87
Cdd:pfam13806   1 WTPVCALDDLPP-GTGVCALVGGRQVAVFRLEDGQVYAIDNRDPfSGANVLSRGIVgdLGGelVVASPLYKQHFDLKTGE 79

                          90       100
                  ....*....|....*....|....
gi 2753127405  88 AREPDEGCTAKFTVQVVDGRVQLS 111
Cdd:pfam13806  80 CLEDPEVSVPVYPVRVRDGNVEVQ 103
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 13-99 4.12e-13

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: 60.68  E-value: 4.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQG-IVHGTTVTCPLHNWQIGLNDGCAREP 91
Cdd:cd03469     1 WYFVGHSSELPEPGDYVTLELGGEPLVLVRDRDGEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYDLDGKLVGVP 80


                  ....*...
gi 2753127405  92 DEGCTAKF 99
Cdd:cd03469    81 REEGFPGF 88
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
12-103 4.17e-13

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 63.87  E-value: 4.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPVlgSRIVRRPA-GQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGlNDG-CAR 89
Cdd:COG5749    19 HWYPVAPSEDLKP--NKPKPVTLlGEPLVIWRDSDGKVVALEDRCPHRGAPLSEGRVEGGNLRCPYHGWQFD-GDGkCVH 95

                          90
                  ....*....|....*.
gi 2753127405  90 EP--DEGCTAKFTVQV 103
Cdd:COG5749    96 IPqlPENQPIPKNAKV 111
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 13-118 5.88e-13

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: 60.04  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVlGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREPD 92
Cdd:cd03474     1 FTKVCSLDDVWE-GEMELVDVDGEEVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGLNPR 79

                          90       100
                  ....*....|....*....|....*.
gi 2753127405  93 EGCTAKFTVQVVDGRVQLSAEEIKTL 118
Cdd:cd03474    80 DCRLARYPVKVEGGDILVDTEGVLPL 105
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 12-99 6.19e-13

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: 63.08  E-value: 6.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIPVLGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLnDG-CARE 90
Cdd:COG4638    26 GWYYVGHSSELPEPGDYLTRTILGEPVVLVRDKDGEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDL-DGrLVGI 104


                  ....*....
gi 2753127405  91 PDEGCTAKF 99
Cdd:COG4638   105 PHMEGFPDF 113
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 29-103 2.57e-12

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: 58.53  E-value: 2.57e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2753127405  29 IVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREP-DEGCTAKFTVQV 103
Cdd:cd03532    20 LARTLLGEPVVLYRTQDGRVAALEDRCPHRSAPLSKGSVEGGGLVCGYHGLEFDSDGRCVHMPgQERVPAKACVRS 95
nirD PRK09511
nitrite reductase small subunit NirD;
11-112 4.16e-12

nitrite reductase small subunit NirD;


Pssm-ID: 181921  Cd Length: 108  Bit Score: 58.12  E-value: 4.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  11 MQWIEICGVEDIpVLGSRIVRRPAGQDIALFR-NAEEQVFALLDECPHKKGP-LSQGIV---HGTT-VTCPLHNWQIGLN 84
Cdd:PRK09511    2 SQWKDICKIDDI-LPGTGVCALVGDEQVAIFRpYHDEQVFAISNIDPFFQASvLSRGLIaehQGELwVASPLKKQRFRLS 80

                          90       100
                  ....*....|....*....|....*...
gi 2753127405  85 DGCAREPDEGCTAKFTVQVVDGRVQLSA 112
Cdd:PRK09511   81 DGLCMEDEQFSVKHYDARVKDGVVQLRA 108
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 11-108 3.93e-10

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 52.86  E-value: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  11 MQWIEICGVEDIPVLGSRIVRRPAgqDIALFrNAEEQVFALLDECPHKKGPLSQGIVHGT-TVTCPLHNWQIGLNDG--- 86
Cdd:PRK09965    1 MNRIYACPVADLPEGEALRVDTSP--VIALF-NVGGEFYAIDDRCSHGNASLSEGYLEDDaTVECPLHAASFCLRTGkal 77

                          90       100
                  ....*....|....*....|....
gi 2753127405  87 C--AREPdegcTAKFTVQVVDGRV 108
Cdd:PRK09965   78 ClpATDP----LRTYPVHVEGGDI 97
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 35-108 1.28e-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: 48.95  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  35 GQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCA------REPDEGCTAKFTVQVVDGRV 108
Cdd:cd03531    23 GTKLVVFADSDGALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGDGRCKaipyarRVPPLARTRAWPTLERNGQL 102
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 43-108 2.35e-08

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: 48.00  E-value: 2.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2753127405  43 NAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDG-CAREPDEGCTAKFTVQVVDGRV 108
Cdd:cd03478    28 RQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGdIEDAPALDSLPCYEVEVEDGRV 94
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 12-98 3.67e-08

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: 48.29  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDIP---VLGSRIVRRPagqdIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCA 88
Cdd:cd04338    17 EWYPLYLLKDVPtdaPLGLSVYDEP----FVLFRDQNGQLRCLEDRCPHRLAKLSEGQLIDGKLECLYHGWQFGGEGKCV 92

                          90
                  ....*....|
gi 2753127405  89 REPDEGCTAK 98
Cdd:cd04338    93 KIPQLPADAK 102
PLN00095 PLN00095
chlorophyllide a oxygenase; Provisional
 40-91 1.49e-07

chlorophyllide a oxygenase; Provisional


Pssm-ID: 165668 [Multi-domain]  Cd Length: 394  Bit Score: 48.14  E-value: 1.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2753127405  40 LFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREP 91
Cdd:PLN00095  100 LFRDADGEAGCIKDECAHRACPLSLGKLVDGKAQCPYHGWEYETGGECAKMP 151
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 13-93 3.49e-07

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: 45.70  E-value: 3.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPAGQDIALFRNAEEQVfALLDE-CPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREP 91
Cdd:cd03479    22 WQPVALSSELTEDGQPVRVRLLGEDLVAFRDTSGRV-GLLDEhCPHRGASLVFGRVEECGLRCCYHGWKFDVDGQCLEMP 100


                  ..
gi 2753127405  92 DE 93
Cdd:cd03479   101 SE 102
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 35-95 3.28e-06

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: 42.86  E-value: 3.28e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753127405  35 GQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREPDEGC 95
Cdd:cd04337    39 GQPWVLFRDEDGTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYDGDGECTKMPSTKC 99
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 12-106 9.13e-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: 41.92  E-value: 9.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  12 QWIEICGVEDI-PvlgsrivRRPA-----GQDIALFRNAEEQ---VFAllDECPHKKGPLSQG-IVHGTTVTCPLHNWQI 81
Cdd:cd03480    17 VWYPVAYVEDLdP-------SRPTpftllGRDLVIWWDRNSQqwrAFD--DQCPHRLAPLSEGrIDEEGCLECPYHGWSF 87

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2753127405  82 GLNDGCAREP---DEG--------CTAKFTVQVVDG 106
Cdd:cd03480    88 DGSGSCQRIPqaaEGGkahtspraCVASLPTAVRQG 123
PLN02518 PLN02518
pheophorbide a oxygenase
 35-106 2.08e-05

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 42.16  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405  35 GQDIALFRNAEEQVF-ALLDECPHKKGPLSQG-IVHGTTVTCPLHNWQIGLNDGCAREPD---EG-----------CTAK 98
Cdd:PLN02518  112 GRDLVLWKDPNQGEWvAFDDKCPHRLAPLSEGrIDENGHLQCSYHGWSFDGCGSCTRIPQaapEGpearavkspraCAIK 191


                  ....*...
gi 2753127405  99 FTVQVVDG 106
Cdd:PLN02518  192 FPTMVSQG 199
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 7-86 2.75e-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: 40.48  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753127405   7 KEIQMQWIEICGVediPVLgsriVRRPAGQdialfrnaeeqVFALLDECPHKKGPLSQGIVHGT--TVTCPLHNWQIGLN 84
Cdd:cd03548    25 EEGEPKGIQLCGE---PIL----LRRVDGK-----------VYALKDRCLHRGVPLSKKPECFTkgTITCWYHGWTYRLD 86


                  ..
gi 2753127405  85 DG 86
Cdd:cd03548    87 DG 88
PLN02281 PLN02281
chlorophyllide a oxygenase
 36-91 5.93e-04

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 38.17  E-value: 5.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2753127405  36 QDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTVTCPLHNWQIGLNDGCAREP 91
Cdd:PLN02281  243 QPWVIFRGEDGKPGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWEYSTDGECKKMP 298
Rieske_RO_Alpha_DTDO cd03536
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit ...
 13-79 1.09e-03

This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit (DitA) of diterpenoid dioxygenase (DTDO). DTDO is a novel aromatic-ring-hydroxylating dioxygenase found in Pseudomonas and other proteobacteria that degrades dehydroabietic acid (DhA). Specifically, DitA hydroxylates 7-oxodehydroabietic acid to 7-oxo-11,12-dihydroxy-8, 13-abietadien acid. The ditA1 and ditA2 genes encode the alpha and beta subunits of the oxygenase component of DTDO while the ditA3 gene encodes the ferredoxin component of DTDO. The organization of the genes encoding the various diterpenoid dioxygenase components, the phylogenetic distinctiveness of both the alpha subunit and the ferredoxin component, and the unusual iron-sulfur cluster of the ferredoxin all suggest that this enzyme belongs to a new class of aromatic ring-hydroxylating dioxygenases.


Pssm-ID: 239610 [Multi-domain]  Cd Length: 123  Bit Score: 36.06  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2753127405  13 WIEICGVEDIPVLGSRIVRRPAGQDIALFRNAEEQVFALLDECPHKKGPLSQGIVHGTTV-TCPLHNW 79
Cdd:cd03536     1 WVLLGHESEIPNKGDFMVRDMGSDSVIVARDKDGEIHVSLNVCPHRGMRISTTDGGNTQIhVCIYHGW 68
 
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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