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Conserved domains on  [gi|501385687|ref|WP_012417253|]
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non-heme iron oxygenase ferredoxin subunit [Bordetella avium]

Protein Classification

non-heme iron oxygenase ferredoxin subunit( domain architecture ID 10131475)

Rieske non-heme iron oxygenase ferredoxin subunit is part of a multicomponent enzyme system such as biphenyl dioxygenase, toluene 1,2-dioxygenase, anthranilate 1,2-dioxygenase, and naphthalene 1,2-dioxygenase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 3-100 1.45e-41

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: 131.84  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPAT 82
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPAT 80

                         90
                 ....*....|....*...
gi 501385687  83 QPIRVYPVRTQGDEVQAD 100
Cdd:cd03528   81 EPLKTYPVKVEDGDVYVD 98
 
Name Accession Description Interval E-value
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 3-100 1.45e-41

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: 131.84  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPAT 82
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPAT 80

                         90
                 ....*....|....*...
gi 501385687  83 QPIRVYPVRTQGDEVQAD 100
Cdd:cd03528   81 EPLKTYPVKVEDGDVYVD 98
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-102 1.04e-38

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: 124.57  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   1 MTWKTIANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAP 80
Cdd:COG2146    1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 501385687  81 ATQPIRVYPVRTQGDEVQADLP 102
Cdd:COG2146   81 ATEPLKTYPVRVEDGDVYVDLP 102
MocE_fam_FeS TIGR02377
Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the ...
 2-101 2.06e-23

Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the Rieske-like [2Fe-2S] family of ferredoxins that includes MocE, part of the rhizopine (3-O-methyl-scyllo-inosamine) catabolic cluster in Rhizobium. Members of this family are related to, yet distinct from, the small subunit of nitrite reductase [NAD(P)H].


Pssm-ID: 131430 [Multi-domain]  Cd Length: 101  Bit Score: 86.08  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    2 TWKTIANINDIGEDEALAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAP 80
Cdd:TIGR02377   1 NWVKACDADDIGREDVARFDHGGRTFAIYRTPDdQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFDYRTGEALNPP 80

                          90       100
                  ....*....|....*....|.
gi 501385687   81 ATQPIRVYPVRTQGDEVQADL 101
Cdd:TIGR02377  81 VCVNLKTYPVKVVDGAVYVDI 101
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 1-102 4.02e-23

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 85.21  E-value: 4.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   1 MTWKTIANINDIGEDEALAFEHDgAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGC-VECPLHQGTFDLVSGEAKCA 79
Cdd:PRK09965   1 MNRIYACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEDDAtVECPLHAASFCLRTGKALCL 79

                         90       100
                 ....*....|....*....|...
gi 501385687  80 PATQPIRVYPVRTQGDEVQADLP 102
Cdd:PRK09965  80 PATDPLRTYPVHVEGGDIFIDLP 102
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 2-89 1.05e-20

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: 78.54  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    2 TWKTIANINDIGEDEALAFEHDGAKLALFKSADA-FHVTDNICTHQYALLSEGYI-EDGCVECPLHQGTFDLvSGEAKCA 79
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGeLYALEDRCPHRGAPLSEGKVnGGGRLECPYHGWRFDG-TGKVVKV 79

                          90
                  ....*....|
gi 501385687   80 PATQPIRVYP 89
Cdd:pfam00355  80 PAPRPLKSYP 89
 
Name Accession Description Interval E-value
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 3-100 1.45e-41

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: 131.84  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPAT 82
Cdd:cd03528    1 WVRVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLSEGYVEGGVIECPLHGGRFDLRTGKALSLPAT 80

                         90
                 ....*....|....*...
gi 501385687  83 QPIRVYPVRTQGDEVQAD 100
Cdd:cd03528   81 EPLKTYPVKVEDGDVYVD 98
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 1-102 1.04e-38

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: 124.57  E-value: 1.04e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   1 MTWKTIANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAP 80
Cdd:COG2146    1 MSEVKVCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLSEGIVDGGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 501385687  81 ATQPIRVYPVRTQGDEVQADLP 102
Cdd:COG2146   81 ATEPLKTYPVRVEDGDVYVDLP 102
MocE_fam_FeS TIGR02377
Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the ...
 2-101 2.06e-23

Rieske [2Fe-2S] domain protein, MocE subfamily; This model describes a subfamily of the Rieske-like [2Fe-2S] family of ferredoxins that includes MocE, part of the rhizopine (3-O-methyl-scyllo-inosamine) catabolic cluster in Rhizobium. Members of this family are related to, yet distinct from, the small subunit of nitrite reductase [NAD(P)H].


Pssm-ID: 131430 [Multi-domain]  Cd Length: 101  Bit Score: 86.08  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    2 TWKTIANINDIGEDEALAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAP 80
Cdd:TIGR02377   1 NWVKACDADDIGREDVARFDHGGRTFAIYRTPDdQYYATDGLCTHEYAHLADGLVMDTTVECPKHAGCFDYRTGEALNPP 80

                          90       100
                  ....*....|....*....|.
gi 501385687   81 ATQPIRVYPVRTQGDEVQADL 101
Cdd:TIGR02377  81 VCVNLKTYPVKVVDGAVYVDI 101
PRK09965 PRK09965
3-phenylpropionate dioxygenase ferredoxin subunit; Provisional
 1-102 4.02e-23

3-phenylpropionate dioxygenase ferredoxin subunit; Provisional


Pssm-ID: 170182 [Multi-domain]  Cd Length: 106  Bit Score: 85.21  E-value: 4.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   1 MTWKTIANINDIGEDEALAFEHDgAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGC-VECPLHQGTFDLVSGEAKCA 79
Cdd:PRK09965   1 MNRIYACPVADLPEGEALRVDTS-PVIALFNVGGEFYAIDDRCSHGNASLSEGYLEDDAtVECPLHAASFCLRTGKALCL 79

                         90       100
                 ....*....|....*....|...
gi 501385687  80 PATQPIRVYPVRTQGDEVQADLP 102
Cdd:PRK09965  80 PATDPLRTYPVHVEGGDIFIDLP 102
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 3-97 1.73e-22

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: 83.69  E-value: 1.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALF-KSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPA 81
Cdd:cd03467    1 WVVVGALSELPPGGGRVVVVGGGPVVVVrREGGEVYALSNRCTHQGCPLSEGEGEDGCIVCPCHGSRFDLRTGEVVSGPA 80

                         90
                 ....*....|....*.
gi 501385687  82 TQPIRVYPVRTQGDEV 97
Cdd:cd03467   81 PRPLPKYPVKVEGDGV 96
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 2-89 1.05e-20

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: 78.54  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    2 TWKTIANINDIGEDEALAFEHDGAKLALFKSADA-FHVTDNICTHQYALLSEGYI-EDGCVECPLHQGTFDLvSGEAKCA 79
Cdd:pfam00355   1 SWYPVCHSSELPEGEPKVVEVGGEPLVVFRDEDGeLYALEDRCPHRGAPLSEGKVnGGGRLECPYHGWRFDG-TGKVVKV 79

                          90
                  ....*....|
gi 501385687   80 PATQPIRVYP 89
Cdd:pfam00355  80 PAPRPLKSYP 89
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 7-97 1.58e-17

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: 70.73  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   7 ANINDIGEDEALAFEHDGAKLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPATQPIR 86
Cdd:cd03478    4 CRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLAKGVLTDGRIRCPWHGACFNLRTGDIEDAPALDSLP 83

                         90
                 ....*....|.
gi 501385687  87 VYPVRTQGDEV 97
Cdd:cd03478   84 CYEVEVEDGRV 94
Rieske_NirD_small_Bacillus cd03530
Small subunit of nitrite reductase (NirD) family, Rieske domain; composed of proteins similar ...
 3-97 4.28e-16

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: 67.25  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSA-DAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAkCAPA 81
Cdd:cd03530    1 WIDIGALEDIPPRGARKVQTGGGEIAVFRTAdDEVFALENRCPHKGGPLSEGIVHGEYVTCPLHNWVIDLETGEA-QGPD 79

                         90
                 ....*....|....*.
gi 501385687  82 TQPIRVYPVRTQGDEV 97
Cdd:cd03530   80 EGCVRTFPVKVEDGRV 95
nirD_assim_sml TIGR02378
nitrite reductase [NAD(P)H], small subunit; This model describes NirD, the small subunit of ...
 2-98 4.61e-15

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: 64.65  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    2 TWKTIANINDIGEDEALAFEHDGAKLALFK-SADAFHVTDNICTHQYA-LLSEGYIED----GCVECPLHQGTFDLVSGE 75
Cdd:TIGR02378   1 TWQDICAIDDIPEETGVCVLLGDTQIAIFRvPGDQVFAIQNMCPHKRAfVLSRGIVGDaqgeLWVACPLHKRNFRLEDGR 80

                          90       100
                  ....*....|....*....|...
gi 501385687   76 AkCAPATQPIRVYPVRTQGDEVQ 98
Cdd:TIGR02378  81 C-LEDDSGSVRTYEVRVEDGRVY 102
Rieske_2 pfam13806
Rieske-like [2Fe-2S] domain;
3-98 1.30e-12

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


Pssm-ID: 433491 [Multi-domain]  Cd Length: 103  Bit Score: 58.34  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687    3 WKTIANINDIGEDEALAFEHDGAKLALFK-SADAFHVTDNICTHQYA-LLSEGYI----EDGCVECPLHQGTFDLVSGEA 76
Cdd:pfam13806   1 WTPVCALDDLPPGTGVCALVGGRQVAVFRlEDGQVYAIDNRDPFSGAnVLSRGIVgdlgGELVVASPLYKQHFDLKTGEC 80

                          90       100
                  ....*....|....*....|..
gi 501385687   77 KCAPAtQPIRVYPVRTQGDEVQ 98
Cdd:pfam13806  81 LEDPE-VSVPVYPVRVRDGNVE 101
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 3-102 4.60e-12

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: 57.35  E-value: 4.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGA-KLALFKSADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKcAPA 81
Cdd:cd03474    1 FTKVCSLDDVWEGEMELVDVDGEeVLLVAPEGGEFRAFQGICPHQEIPLAEGGFDGGVLTCRAHLWQFDADTGEGL-NPR 79

                         90       100
                 ....*....|....*....|.
gi 501385687  82 TQPIRVYPVRTQGDEVQADLP 102
Cdd:cd03474   80 DCRLARYPVKVEGGDILVDTE 100
Rieske_NirD cd03529
Assimilatory nitrite reductase (NirD) family, Rieske domain; Assimilatory nitrate and nitrite ...
 3-98 9.86e-11

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: 53.67  E-value: 9.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFK-SADAFHVTDNICTHQYA-LLSEGYI-EDG---CVECPLHQGTFDLVSGEA 76
Cdd:cd03529    1 WQTVCALDDLPPGSGVAALVGDTQIAIFRlPGREVYAVQNMDPHSRAnVLSRGIVgDIGgepVVASPLYKQHFSLKTGRC 80

                         90       100
                 ....*....|....*....|..
gi 501385687  77 KCAPATQpIRVYPVRTQGDEVQ 98
Cdd:cd03529   81 LEDEDVS-VATFPVRVEDGEVY 101
QcrA/PetC COG0723
Rieske Fe-S protein [Energy production and conversion];
9-102 6.25e-10

Rieske Fe-S protein [Energy production and conversion];


Pssm-ID: 440487 [Multi-domain]  Cd Length: 118  Bit Score: 51.93  E-value: 6.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   9 INDIGEDEALAFEHDGAKLALFK----SADAFHVTDNICTHQyallsegyiedGCV----------ECPLHQGTFDLvSG 74
Cdd:COG0723   23 LSDLPPGEGKVVEWRGKPVFVVRtpvrGDGEIVAVSAICTHL-----------GCPvtwnadeggfDCPCHGSRFDP-DG 90

                         90       100
                 ....*....|....*....|....*...
gi 501385687  75 EAKCAPATQPIRVYPVRTQGDEVQADLP 102
Cdd:COG0723   91 RVLKGPAPRPLPVPPLEVDDDKLLIGVG 118
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 24-100 3.15e-07

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: 45.05  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687  24 GAKLALFKSAD----AFHvtdNICTHQYALLSEGYIEDGCVECPLHQGTFDlvsGEAKCA--------PATQPIRVYPVR 91
Cdd:cd03532   26 GEPVVLYRTQDgrvaALE---DRCPHRSAPLSKGSVEGGGLVCGYHGLEFD---SDGRCVhmpgqervPAKACVRSYPVV 99

                         90
                 ....*....|....*..
gi 501385687  92 TQ--------GDEVQAD 100
Cdd:cd03532  100 ERdaliwiwmGDAALAD 116
Rieske_RO_Alpha_Tic55 cd04338
Tic55 is a 55kDa LLS1-related non-heme iron oxygenase associated with protein transport ...
 3-78 7.93e-07

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: 44.05  E-value: 7.93e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSADA-FHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDlvsGEAKC 78
Cdd:cd04338   18 WYPLYLLKDVPTDAPLGLSVYDEPFVLFRDQNGqLRCLEDRCPHRLAKLSEGQLIDGKLECLYHGWQFG---GEGKC 91
Rieske_RO_Alpha_PaO cd03480
Rieske non-heme iron oxygenase (RO) family, Pheophorbide a oxygenase (PaO) subfamily, ...
 38-93 9.99e-07

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: 43.85  E-value: 9.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687  38 VTDNICTHQYALLSEGYI-EDGCVECPLHQGTFDlvsGEAKC-----APATQP--------IRVYPVRTQ 93
Cdd:cd03480   55 AFDDQCPHRLAPLSEGRIdEEGCLECPYHGWSFD---GSGSCqripqAAEGGKahtspracVASLPTAVR 121
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 18-81 1.92e-06

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: 42.96  E-value: 1.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501385687  18 LAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEG-YIEDGCVECPLHQGTFDLvSGEAKCAPA 81
Cdd:cd03469   17 VTLELGGEPLVLVRDRDgEVRAFHNVCPHRGARLCEGrGGNAGRLVCPYHGWTYDL-DGKLVGVPR 81
Rieske_RO_Alpha_PrnD cd03537
This alignment model represents the N-terminal rieske domain of the oxygenase alpha subunit of ...
 38-85 4.33e-06

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: 42.23  E-value: 4.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501385687  38 VTDNICTHQYALLSEGYIEDGCVECPLH------QGTFDLVSGEAKCAPATQPI 85
Cdd:cd03537   39 VMDRHCSHLGANLADGRVKDGCIQCPFHhwrydeQGQCVHIPGHSTAVRRLEPV 92
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 18-94 6.68e-06

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: 42.67  E-value: 6.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687  18 LAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDL---------VSGEAKCAPATQPIRV 87
Cdd:COG4638   43 LTRTILGEPVVLVRDKDgEVRAFHNVCPHRGAPLSEGRGNGGRLVCPYHGWTYDLdgrlvgiphMEGFPDFDPARAGLRS 122


                 ....*..
gi 501385687  88 YPVRTQG 94
Cdd:COG4638  123 VPVEEWG 129
Rieske_RO_Alpha_Cao cd04337
Cao (chlorophyll a oxygenase) is a rieske non-heme iron-sulfur protein located within the ...
 3-102 1.54e-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: 37.85  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDlVSGEAKCAPA 81
Cdd:cd04337   18 WYPVEFSKDLKMDTMVPFELFGQPWVLFRDEDgTPGCIRDECAHRACPLSLGKVIEGRIQCPYHGWEYD-GDGECTKMPS 96

                         90       100       110
                 ....*....|....*....|....*....|...
gi 501385687  82 TQ----PIRVYPVRTQ--------GDEVQADLP 102
Cdd:cd04337   97 TKclnvGIAALPCMEQdgmiwvwpGDDPPAALP 129
PLN02518 PLN02518
pheophorbide a oxygenase
 3-99 2.94e-04

pheophorbide a oxygenase


Pssm-ID: 215283 [Multi-domain]  Cd Length: 539  Bit Score: 38.31  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFK--SADAFHVTDNICTHQYALLSEGYI-EDGCVECPLHQGTFDlvsGEAKCA 79
Cdd:PLN02518  91 WYPVSLVEDLDPSVPTPFQLLGRDLVLWKdpNQGEWVAFDDKCPHRLAPLSEGRIdENGHLQCSYHGWSFD---GCGSCT 167

                         90       100
                 ....*....|....*....|
gi 501385687  80 PATQPIrvypvrTQGDEVQA 99
Cdd:PLN02518 168 RIPQAA------PEGPEARA 181
Rieske_RO_Alpha_CMO cd03541
Rieske non-heme iron oxygenase (RO) family, Choline monooxygenase (CMO) subfamily, N-terminal ...
 35-82 3.15e-04

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: 37.15  E-value: 3.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 501385687  35 AFHvtdNICTHQYALLSEGYIEDGCVECPLHQGTFDLVSGEAKCAPAT 82
Cdd:cd03541   39 AFH---NVCTHRASILACGSGKKSCFVCPYHGWVYGLDGSLTKATQAT 83
PLN02281 PLN02281
chlorophyllide a oxygenase
 3-87 1.54e-03

chlorophyllide a oxygenase


Pssm-ID: 177920 [Multi-domain]  Cd Length: 536  Bit Score: 36.25  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSADAF-HVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDlVSGEAKCAPA 81
Cdd:PLN02281 221 WYPVAFTADLKHDTMVPIECFEQPWVIFRGEDGKpGCVRNTCAHRACPLDLGTVNEGRIQCPYHGWEYS-TDGECKKMPS 299


                 ....*.
gi 501385687  82 TQPIRV 87
Cdd:PLN02281 300 TKLLKV 305
Rieske_RO_Alpha_KSH cd03531
The alignment model represents the N-terminal rieske iron-sulfur domain of KshA, the oxygenase ...
 3-79 1.70e-03

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: 35.08  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501385687   3 WKTIANINDIGEDEALAFEHDGAKLALFKSAD-AFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFdlvSGEAKCA 79
Cdd:cd03531    2 WHCLGLARDFRDGKPHGVEAFGTKLVVFADSDgALNVLDAYCRHMGGDLSQGTVKGDEIACPFHDWRW---GGDGRCK 76
Rieske_RO_Alpha_PhDO_like cd03479
Rieske non-heme iron oxygenase (RO) family, Phthalate 4,5-dioxygenase (PhDO)-like subfamily, ...
 24-97 8.58e-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: 33.37  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501385687  24 GAKLALFK-SADAFHVTDNICTHQYALLSEGYIEDGCVECPLHQGTFDlVSG---EAKCAPATQP------IRVYPVRTQ 93
Cdd:cd03479   44 GEDLVAFRdTSGRVGLLDEHCPHRGASLVFGRVEECGLRCCYHGWKFD-VDGqclEMPSEPPDSQlkqkvrQPAYPVRER 122


                 ....
gi 501385687  94 GDEV 97
Cdd:cd03479  123 GGLV 126
 
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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