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Conserved domains on  [gi|221042188|dbj|BAH12771|]
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unnamed protein product [Homo sapiens]

Protein Classification

ferric reductase family protein( domain architecture ID 10484952)

ferric reductase family protein functions as an oxidoreductase, such as human NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

EC:  1.-.-.-
Gene Ontology:  GO:0050661|GO:0016491|GO:0016020

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 145-390 1.52e-42

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


:

Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 147.84  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 145 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 220
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 221 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKPRRLYFIWFwqe 299
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWV--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 300 nGPDYVNIQLYLSQTDGIQKIigekYHALNSRLFIGRprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQNNsy 379
Cdd:cd06186  147 -VRDREDLEWFLDELRAAQEL----EVDGEIEIYVTR--------------------VVVCGPPGLVDDVRNAVAKKG-- 199

                        250
                 ....*....|.
gi 221042188 380 GTRFEYNKESF 390
Cdd:cd06186  200 GTGVEFHEESF 210
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 1-39 4.25e-06

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


:

Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 45.34  E-value: 4.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 221042188    1 MVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 39
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 145-390 1.52e-42

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 147.84  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 145 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 220
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 221 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKPRRLYFIWFwqe 299
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWV--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 300 nGPDYVNIQLYLSQTDGIQKIigekYHALNSRLFIGRprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQNNsy 379
Cdd:cd06186  147 -VRDREDLEWFLDELRAAQEL----EVDGEIEIYVTR--------------------VVVCGPPGLVDDVRNAVAKKG-- 199

                        250
                 ....*....|.
gi 221042188 380 GTRFEYNKESF 390
Cdd:cd06186  200 GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
257-373 5.41e-17

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 77.38  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  257 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKPRRLYFIWF--------W--------QENGPDYVNIQLYLSQTD----- 315
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVvrdlssleWfkdvlnelEELKELNIEIHIYLTGEYeaeda 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042188  316 -----------GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 373
Cdd:pfam08030  81 sdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
108-296 9.73e-16

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 78.40  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 108 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 176
Cdd:COG4097  178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 177 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 254
Cdd:COG4097  256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 221042188 255 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKPRRLYFIWF 296
Cdd:COG4097  316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYC 355
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 1-279 3.23e-15

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 77.19  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188   1 MVVVLFLMITaSTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrtssqnislpeyfSEH 80
Cdd:PLN02844 244 LVTGLVIWIT-SLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG----------------------------------DRH 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  81 FHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRM 160
Cdd:PLN02844 289 FYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKAIELVL 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 161 VKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRnyp 239
Cdd:PLN02844 332 PKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVA--- 408

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 221042188 240 klyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTL 279
Cdd:PLN02844 409 ---IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 1-39 4.25e-06

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 45.34  E-value: 4.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 221042188    1 MVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 39
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 145-390 1.52e-42

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 147.84  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 145 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 220
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 221 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKPRRLYFIWFwqe 299
Cdd:cd06186   81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWV--- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 300 nGPDYVNIQLYLSQTDGIQKIigekYHALNSRLFIGRprwkllfdeiakynrgktvgVFCCGPNSLSKTLHKLSNQNNsy 379
Cdd:cd06186  147 -VRDREDLEWFLDELRAAQEL----EVDGEIEIYVTR--------------------VVVCGPPGLVDDVRNAVAKKG-- 199

                        250
                 ....*....|.
gi 221042188 380 GTRFEYNKESF 390
Cdd:cd06186  200 GTGVEFHEESF 210
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
257-373 5.41e-17

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 77.38  E-value: 5.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  257 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKPRRLYFIWF--------W--------QENGPDYVNIQLYLSQTD----- 315
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVvrdlssleWfkdvlnelEELKELNIEIHIYLTGEYeaeda 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042188  316 -----------GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 373
Cdd:pfam08030  81 sdqsdssirseNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
108-296 9.73e-16

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 78.40  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 108 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 176
Cdd:COG4097  178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 177 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 254
Cdd:COG4097  256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 221042188 255 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKPRRLYFIWF 296
Cdd:COG4097  316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYC 355
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 1-279 3.23e-15

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 77.19  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188   1 MVVVLFLMITaSTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrtssqnislpeyfSEH 80
Cdd:PLN02844 244 LVTGLVIWIT-SLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG----------------------------------DRH 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  81 FHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRM 160
Cdd:PLN02844 289 FYMVFPGIF-------------------------------------LFGLDKLLRIVQSRPETCILSARLFPCKAIELVL 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 161 VKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLLPPSSQDSEILPFIQSRnyp 239
Cdd:PLN02844 332 PKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQAELDSETNQMNCIPVA--- 408

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 221042188 240 klyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTL 279
Cdd:PLN02844 409 ---IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
FAD_binding_8 pfam08022
FAD-binding domain;
141-250 3.43e-15

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 70.83  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  141 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 217
Cdd:pfam08022   2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 221042188  218 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 250
Cdd:pfam08022  80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 144-295 2.49e-14

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 72.20  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 144 TIISVISHPSDV--MEIRMVKENFKARPGQYITLHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 221
Cdd:COG0543    1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221042188 222 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKPRRLYFIW 295
Cdd:COG0543   75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYL 129
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 154-362 3.63e-13

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 68.24  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 154 DVMEIRMVKEN-FKARPGQYITLHCPSVSALENHPFTLTMCPTETKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 231
Cdd:cd00322    9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 232 fiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP------Y---KPRRLYFIWFWQENGP 302
Cdd:cd00322   83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGgeitllYgarTPADLLFLDELEELAK 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221042188 303 DYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKY-NRGKTVGVFCCGP 362
Cdd:cd00322  152 EGPNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
PLN02292 PLN02292
ferric-chelate reductase
 7-280 9.26e-11

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 63.35  E-value: 9.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188   7 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 85
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188  86 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 164
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 165 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 244
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 221042188 245 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 280
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 151-391 1.04e-10

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 60.73  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 151 HPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 229
Cdd:cd06198    7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 230 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwKPYKPRRLyfiwFWQENGPDYvniQL 309
Cdd:cd06198   79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAAR-GDARPVTL----FYCVRDPED---AV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 310 YLSQTDGIQKIIGEKYHALNSRLfIGRPRWKLLFDEIAKynRGKTVGVFCCGPNSLSKTLHKLSNQNNSYGTRFEYnkES 389
Cdd:cd06198  140 FLDELRALAAAAGVVLHVIDSPS-DGRLTLEQLVRALVP--DLADADVWFCGPPGMADALEKGLRALGVPARRFHY--ER 214


                 ..
gi 221042188 390 FS 391
Cdd:cd06198  215 FE 216
PLN02631 PLN02631
ferric-chelate reductase
 127-280 1.86e-10

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 62.75  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 127 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 205
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042188 206 KIVGDWTERFRDLLlpPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 280
Cdd:PLN02631 374 RRQGSWTQKLYTHL--SSSIDS-----------LEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELI 435
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 143-362 5.90e-07

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 49.94  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 143 VTIISVIshpsdvMEIRMVK-----ENFKARPGQYITLHCPSVSALenhPFTLTMCPTEtkatFGVHLKIVGDWTERFRD 217
Cdd:cd06220    1 VTIKEVI------DETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 218 LllppssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKPYK--------PR 289
Cdd:cd06220   68 L-----------------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKKAAdvtvllgaRT 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221042188 290 RLYFIWFWQENGPDyvniQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKYNRgktvgVFCCGP 362
Cdd:cd06220  125 KEELLFLDRLRKSD----ELIVTTDDG-------------SYGFKGFVTDLLKELDLEEYDA-----IYVCGP 175
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
142-281 9.48e-07

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 49.40  E-value: 9.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 142 PVTIISVISHPSDVMEIRMV----KENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGV-------------- 203
Cdd:COG1018    5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 204 HLKiVGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLL 280
Cdd:COG1018   85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131


                 .
gi 221042188 281 D 281
Cdd:COG1018  132 A 132
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 143-275 1.57e-06

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 49.10  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 143 VTIISVISHPSDVMEIRM-VKENFKARPGQYITLHCPSVSALENHPFTLTMCPTEtKATFGVhlKIVGDWTERFRDLllp 221
Cdd:PRK00054   7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 221042188 222 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 275
Cdd:PRK00054  81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 1-39 4.25e-06

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 45.34  E-value: 4.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 221042188    1 MVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 39
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 155-276 1.72e-05

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 45.78  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 155 VMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLtMCPTETKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 234
Cdd:cd06192   13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 221042188 235 srnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASIL 276
Cdd:cd06192   80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 240-362 2.09e-04

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 42.55  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 240 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKPRRLYFIWF---------------WQENGPD 303
Cdd:cd06183   86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYAnrteedillreeldeLAKKHPD 163

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 221042188 304 YVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPRWKLLFDEIAKYNRGKTVgVFCCGP 362
Cdd:cd06183  164 RFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 240-293 9.32e-04

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 40.67  E-value: 9.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221042188 240 KLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKPRRLYF 293
Cdd:cd06221   80 TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYGKVTLLY 134
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 143-295 2.98e-03

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 38.68  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042188 143 VTIISVISHpsDVMEIR-MVKENFKARPGQYITLHCPSVSALenhPFTLTMCPTETkATFGVHLKIVGDWteRFRDlllp 221
Cdd:cd06189    3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042188 222 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKPRR-LYFIW 295
Cdd:cd06189   71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYW 133
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 240-295 4.54e-03

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 38.39  E-value: 4.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 221042188 240 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKpRRLYFIW 295
Cdd:cd06190   80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFY 134
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 263-294 9.88e-03

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 37.15  E-value: 9.88e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 221042188 263 VAGGIGVTPFASILNTLLDDwkpYKPRRLYFI 294
Cdd:cd06184  119 ISAGVGITPMLSMLEALAAE---GPGRPVTFI 147
 
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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