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Conserved domains on  [gi|442796439|ref|NP_001263194|]
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dual oxidase maturation factor 1 isoform 2 [Homo sapiens]

Protein Classification

DuoxA domain-containing protein( domain architecture ID 10562893)

DuoxA domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DuoxA pfam10204
Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential ...
10-242 4.17e-113

Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential protein necessary for the final release of DUOX2 (an NADPH:O2 oxidoreductase flavoprotein) from the endoplasmic reticulum. Dual oxidases (DUOX1 and DUOX2) constitute the catalytic core of the hydrogen peroxide generator, which generates H2O2 at the apical membrane of thyroid follicular cells, essential for iodination of thyroglobulin by thyroid peroxidases. DuoxA carries five membrane-integral regions including a reverse signal-anchor with external N-terminus (type III) and two N-glycosylation sites. It is conserved from nematodes to humans.


:

Pssm-ID: 462995  Cd Length: 277  Bit Score: 333.02  E-value: 4.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   10 FYAGPKPTFPMDTTLASIIMIFLTALATFIVILPGIRGKTRLFWLLRVVTSLFIGAAIL--------------------- 68
Cdd:pfam10204   1 FYPSNRTPVTFDVLLIVIILVFLTLAVSFLLILPGIRGKERLFWFLRVTLSLFIGAVILavnfgsewevgevttntsyka 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   69 ------------------------GTPVQQLNETINYNEEFTWRLGENYAEEYAKALEKGLPDPVLYLAEKFTPRSP-CG 123
Cdd:pfam10204  81 fsneeinadiglhiglrgvnvtlkGTPVGQLNETIDYNERFSWRFAGDMNEEYRAALEKGLPYPILYVAEYFTLDSEgCR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439  124 LYRQYRLAGHYTSAMLWVAFLCWLLANVMLsMPVLVYGGYMLLATGIFQLLALLFFSmatSLTSPCPLHL--GASVLHTH 201
Cdd:pfam10204 161 WGRQYRLAGYYASATLWTAFACWLLSNLLL-MPVPRYGGYMMLLTGAFMLFSNLIFS---SLLPPCPLVIpfGGASLTTH 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 442796439  202 HGPAFWITLTTGLLCVLLGLAMAVAHRMQPHRLKAFFNQSV 242
Cdd:pfam10204 237 YGWSFWLVLATGLLCLLLGLIIVILDLLFPHKLSTFFEVDY 277
 
Name Accession Description Interval E-value
DuoxA pfam10204
Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential ...
10-242 4.17e-113

Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential protein necessary for the final release of DUOX2 (an NADPH:O2 oxidoreductase flavoprotein) from the endoplasmic reticulum. Dual oxidases (DUOX1 and DUOX2) constitute the catalytic core of the hydrogen peroxide generator, which generates H2O2 at the apical membrane of thyroid follicular cells, essential for iodination of thyroglobulin by thyroid peroxidases. DuoxA carries five membrane-integral regions including a reverse signal-anchor with external N-terminus (type III) and two N-glycosylation sites. It is conserved from nematodes to humans.


Pssm-ID: 462995  Cd Length: 277  Bit Score: 333.02  E-value: 4.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   10 FYAGPKPTFPMDTTLASIIMIFLTALATFIVILPGIRGKTRLFWLLRVVTSLFIGAAIL--------------------- 68
Cdd:pfam10204   1 FYPSNRTPVTFDVLLIVIILVFLTLAVSFLLILPGIRGKERLFWFLRVTLSLFIGAVILavnfgsewevgevttntsyka 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   69 ------------------------GTPVQQLNETINYNEEFTWRLGENYAEEYAKALEKGLPDPVLYLAEKFTPRSP-CG 123
Cdd:pfam10204  81 fsneeinadiglhiglrgvnvtlkGTPVGQLNETIDYNERFSWRFAGDMNEEYRAALEKGLPYPILYVAEYFTLDSEgCR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439  124 LYRQYRLAGHYTSAMLWVAFLCWLLANVMLsMPVLVYGGYMLLATGIFQLLALLFFSmatSLTSPCPLHL--GASVLHTH 201
Cdd:pfam10204 161 WGRQYRLAGYYASATLWTAFACWLLSNLLL-MPVPRYGGYMMLLTGAFMLFSNLIFS---SLLPPCPLVIpfGGASLTTH 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 442796439  202 HGPAFWITLTTGLLCVLLGLAMAVAHRMQPHRLKAFFNQSV 242
Cdd:pfam10204 237 YGWSFWLVLATGLLCLLLGLIIVILDLLFPHKLSTFFEVDY 277
 
Name Accession Description Interval E-value
DuoxA pfam10204
Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential ...
10-242 4.17e-113

Dual oxidase maturation factor; DuoxA (Dual oxidase maturation factor) is the essential protein necessary for the final release of DUOX2 (an NADPH:O2 oxidoreductase flavoprotein) from the endoplasmic reticulum. Dual oxidases (DUOX1 and DUOX2) constitute the catalytic core of the hydrogen peroxide generator, which generates H2O2 at the apical membrane of thyroid follicular cells, essential for iodination of thyroglobulin by thyroid peroxidases. DuoxA carries five membrane-integral regions including a reverse signal-anchor with external N-terminus (type III) and two N-glycosylation sites. It is conserved from nematodes to humans.


Pssm-ID: 462995  Cd Length: 277  Bit Score: 333.02  E-value: 4.17e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   10 FYAGPKPTFPMDTTLASIIMIFLTALATFIVILPGIRGKTRLFWLLRVVTSLFIGAAIL--------------------- 68
Cdd:pfam10204   1 FYPSNRTPVTFDVLLIVIILVFLTLAVSFLLILPGIRGKERLFWFLRVTLSLFIGAVILavnfgsewevgevttntsyka 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439   69 ------------------------GTPVQQLNETINYNEEFTWRLGENYAEEYAKALEKGLPDPVLYLAEKFTPRSP-CG 123
Cdd:pfam10204  81 fsneeinadiglhiglrgvnvtlkGTPVGQLNETIDYNERFSWRFAGDMNEEYRAALEKGLPYPILYVAEYFTLDSEgCR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442796439  124 LYRQYRLAGHYTSAMLWVAFLCWLLANVMLsMPVLVYGGYMLLATGIFQLLALLFFSmatSLTSPCPLHL--GASVLHTH 201
Cdd:pfam10204 161 WGRQYRLAGYYASATLWTAFACWLLSNLLL-MPVPRYGGYMMLLTGAFMLFSNLIFS---SLLPPCPLVIpfGGASLTTH 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 442796439  202 HGPAFWITLTTGLLCVLLGLAMAVAHRMQPHRLKAFFNQSV 242
Cdd:pfam10204 237 YGWSFWLVLATGLLCLLLGLIIVILDLLFPHKLSTFFEVDY 277
 
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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