NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498248543|ref|WP_010562699|]
View 

MULTISPECIES: Rieske (2Fe-2S) protein [Pseudomonas]

Protein Classification

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

Rieske (2Fe-2S) protein 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

CATH:  2.102.10.10
Gene Ontology:  GO:0051537|GO:0046872

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 4.49e-23

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: 85.28  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   4 LCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLDtsASLIQCATHGALFLIETGECIAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 498248543  84 CAGqSLKALPGREDEQGLWVQL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 4.49e-23

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: 85.28  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   4 LCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLDtsASLIQCATHGALFLIETGECIAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 498248543  84 CAGqSLKALPGREDEQGLWVQL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 3-100 3.17e-17

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: 70.21  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYF-YINRCPHRGIPLEWQpdsflDTSASLIQCATHGALFLIETGECIA 81
Cdd:cd03467    3 VVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYaLSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVS 77

                         90
                 ....*....|....*....
gi 498248543  82 GPCaGQSLKALPGREDEQG 100
Cdd:cd03467   78 GPA-PRPLPKYPVKVEGDG 95
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 4-93 9.62e-10

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


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 50.81  E-value: 9.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543    4 LCPSDALAPNSSLGFEVDGIKLLAVR-RDGIVYFYINRCPHRGIPLewqpDSFLDTSASLIQCATHGALFlIETGECIAG 82
Cdd:pfam00355   5 VCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPL----SEGKVNGGGRLECPYHGWRF-DGTGKVVKV 79

                          90
                  ....*....|.
gi 498248543   83 PCAGQsLKALP 93
Cdd:pfam00355  80 PAPRP-LKSYP 89
 
Name Accession Description Interval E-value
NirD COG2146
Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion ...
 4-105 4.49e-23

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: 85.28  E-value: 4.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   4 LCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLDtsASLIQCATHGALFLIETGECIAGP 83
Cdd:COG2146    6 VCALDDLPEGGGVVVEVGGKQIAVFRTDGEVYAYDNRCPHQGAPLS---EGIVD--GGVVTCPLHGARFDLRTGECLGGP 80

                         90       100
                 ....*....|....*....|..
gi 498248543  84 CAGqSLKALPGREDEQGLWVQL 105
Cdd:COG2146   81 ATE-PLKTYPVRVEDGDVYVDL 101
Rieske cd03467
Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron ...
 3-100 3.17e-17

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: 70.21  E-value: 3.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYF-YINRCPHRGIPLEWQpdsflDTSASLIQCATHGALFLIETGECIA 81
Cdd:cd03467    3 VVGALSELPPGGGRVVVVGGGPVVVVRREGGEVYaLSNRCTHQGCPLSEG-----EGEDGCIVCPCHGSRFDLRTGEVVS 77

                         90
                 ....*....|....*....
gi 498248543  82 GPCaGQSLKALPGREDEQG 100
Cdd:cd03467   78 GPA-PRPLPKYPVKVEGDG 95
Rieske_AIFL_N cd03478
AIFL (apoptosis-inducing factor like) family, N-terminal Rieske domain; members of this family ...
 3-93 4.05e-10

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: 51.85  E-value: 4.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLdtSASLIQCATHGALFLIETGECIAG 82
Cdd:cd03478    2 VVCRLSDLGDGEMKEVDVGDGKVLLVRQGGEVHAIGAKCPHYGAPLA---KGVL--TDGRIRCPWHGACFNLRTGDIEDA 76

                         90
                 ....*....|.
gi 498248543  83 PCagqsLKALP 93
Cdd:cd03478   77 PA----LDSLP 83
Rieske pfam00355
Rieske [2Fe-2S] domain; The rieske domain has a [2Fe-2S] centre. Two conserved cysteines ...
 4-93 9.62e-10

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


Pssm-ID: 425632 [Multi-domain]  Cd Length: 89  Bit Score: 50.81  E-value: 9.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543    4 LCPSDALAPNSSLGFEVDGIKLLAVR-RDGIVYFYINRCPHRGIPLewqpDSFLDTSASLIQCATHGALFlIETGECIAG 82
Cdd:pfam00355   5 VCHSSELPEGEPKVVEVGGEPLVVFRdEDGELYALEDRCPHRGAPL----SEGKVNGGGRLECPYHGWRF-DGTGKVVKV 79

                          90
                  ....*....|.
gi 498248543   83 PCAGQsLKALP 93
Cdd:pfam00355  80 PAPRP-LKSYP 89
Rieske_RO_ferredoxin cd03528
Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the ...
 3-84 2.36e-09

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


Pssm-ID: 239604 [Multi-domain]  Cd Length: 98  Bit Score: 50.18  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLDTSAslIQCATHGALFLIETGECIAG 82
Cdd:cd03528    3 RVCAVDELPEGEPKRVDVGGRPIAVYRVDGEFYATDDLCTHGDASLS---EGYVEGGV--IECPLHGGRFDLRTGKALSL 77


                 ..
gi 498248543  83 PC 84
Cdd:cd03528   78 PA 79
Rieske_RO_Alpha_N cd03469
Rieske non-heme iron oxygenase (RO) family, N-terminal Rieske domain of the oxygenase alpha ...
 3-86 8.10e-07

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: 43.73  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALA-PNSSLGFEVDGIKLLAVR-RDGIVYFYINRCPHRGIPLEWQPdsflDTSASLIQCATHGALF-LieTGEC 79
Cdd:cd03469    3 FVGHSSELPePGDYVTLELGGEPLVLVRdRDGEVRAFHNVCPHRGARLCEGR----GGNAGRLVCPYHGWTYdL--DGKL 76


                 ....*..
gi 498248543  80 IAGPCAG 86
Cdd:cd03469   77 VGVPREE 83
Rieske_RO_Alpha_OMO_CARDO cd03548
Rieske non-heme iron oxygenase (RO) family, 2-Oxoquinoline 8-monooxygenase (OMO) and Carbazole ...
 7-103 1.17e-06

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: 43.95  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   7 SDALAPNSSLGFEVDGIKLLAVRRDGIVYFYINRCPHRGIPLEWQPDSFldtSASLIQCATHGALFLIETGE---CIAGP 83
Cdd:cd03548   21 SHELEEGEPKGIQLCGEPILLRRVDGKVYALKDRCLHRGVPLSKKPECF---TKGTITCWYHGWTYRLDDGKlvtILANP 97

                         90       100
                 ....*....|....*....|....
gi 498248543  84 CAGQ----SLKALPGREDEQGLWV 103
Cdd:cd03548   98 DDPLigrtGLKTYPVEEAKGMIFV 121
HcaE COG4638
Phenylpropionate dioxygenase or related ring-hydroxylating dioxygenase, large terminal subunit ...
 3-103 1.81e-05

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: 41.51  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   3 FLCPSDALA-PNSSLGFEVDGIKLLAVR-RDGIVYFYINRCPHRGIPLewqpdSFLDTSASLIQCATHG---ALflieTG 77
Cdd:COG4638   29 YVGHSSELPePGDYLTRTILGEPVVLVRdKDGEVRAFHNVCPHRGAPL-----SEGRGNGGRLVCPYHGwtyDL----DG 99

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 498248543  78 ECIAGPCAGQ---------SLKALPGREdEQGL-WV 103
Cdd:COG4638  100 RLVGIPHMEGfpdfdparaGLRSVPVEE-WGGLiFV 134
Rieske_RO_Alpha_VanA_DdmC cd03532
Rieske non-heme iron oxygenase (RO) family, Vanillate-O-demethylase oxygenase (VanA) and ...
 30-103 5.65e-04

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: 36.19  E-value: 5.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498248543  30 RDGIVYFYINRCPHRGIPLEwqpDSFLdtSASLIQCATHGALFLIEtGECIAGPC-----AGQSLKALPGREDEQGLWV 103
Cdd:cd03532   35 QDGRVAALEDRCPHRSAPLS---KGSV--EGGGLVCGYHGLEFDSD-GRCVHMPGqervpAKACVRSYPVVERDALIWI 107
Rieske_T4moC cd03474
Toluene-4-monooxygenase effector protein complex (T4mo), Rieske ferredoxin subunit; The Rieske ...
 4-80 4.61e-03

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: 33.85  E-value: 4.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498248543   4 LCPSDALAPNSSLGFEVDG-IKLLAVRRDGIVYFYINRCPHRGIPLEwqpDSFLDtsASLIQCATHGALFLIETGECI 80
Cdd:cd03474    4 VCSLDDVWEGEMELVDVDGeEVLLVAPEGGEFRAFQGICPHQEIPLA---EGGFD--GGVLTCRAHLWQFDADTGEGL 76
PobA COG5749
Chlorophyllide a oxygenase/letal leaf spot protein [Coenzyme transport and metabolism];
5-103 5.10e-03

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


Pssm-ID: 444459 [Multi-domain]  Cd Length: 349  Bit Score: 34.59  E-value: 5.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498248543   5 CPSDALAPNSSLGFEVDGIKLLAVR-RDGIVYFYINRCPHRGIPLewqpdsfldtsaSL-------IQCATHGALFlIET 76
Cdd:COG5749   24 APSEDLKPNKPKPVTLLGEPLVIWRdSDGKVVALEDRCPHRGAPL------------SEgrveggnLRCPYHGWQF-DGD 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 498248543  77 GECIAGPCAGQS--------LKALPGREdEQG-LWV 103
Cdd:COG5749   91 GKCVHIPQLPENqpipknakVKSYPVQE-RYGlIWV 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH