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Conserved domains on  [gi|528478947|ref|XP_005165240|]
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D-amino-acid oxidase, tandem duplicate 1 isoform X1 [Danio rerio]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 12015107)

FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to D-amino acid oxidase

EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491
SCOP:  3000055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
2-329 2.44e-33

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


:

Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 125.97  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947    2 RVCIIGAGVIGLSTAqsiyqhFHSRVSPLTIEVY-ADIFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNyLLSFLN 80
Cdd:pfam01266   1 DVVVIGGGIVGLSTA------YELARRGLSVTLLeRGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALD-LWEELE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947   81 SPDSIKMGIFLESGYNLCFEPMPEP------SFKQAVLGFRQLSKREL-EMFP---GFSFGWFN-TALVIEGKSYLPWLM 149
Cdd:pfam01266  74 EELGIDCGFRRCGVLVLARDEEEEAlekllaALRRLGVPAELLDAEELrELEPllpGLRGGLFYpDGGHVDPARLLRALA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  150 DWLNQRGVKFFQR-KIDSFKE------LSDSG-ADMIINCSGVRSGDLQP---DPELQPARGQIIKVDAPWLKH----WV 214
Cdd:pfam01266 154 RAAEALGVRIIEGtEVTGIEEeggvwgVVTTGeADAVVNAAGAWADLLALpglRLPVRPVRGQVLVLEPLPEALlilpVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  215 ITHDSKLGTYNTPYiiPGSRLVtVGGVFQVGNWNRMNSSVEHKQ-IWEGACKLEPSLqhARIVEDWTGLRPARSKVRLER 293
Cdd:pfam01266 234 ITVDPGRGVYLRPR--ADGRLL-LGGTDEEDGFDDPTPDPEEIEeLLEAARRLFPAL--ADIERAWAGLRPLPDGLPIIG 308
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 528478947  294 ESIRCGghsfeVIHNYGHGGFGLTIHRGCAEEAARL 329
Cdd:pfam01266 309 RPGSPG-----LYLATGHGGHGLTLAPGIGKLLAEL 339
 
Name Accession Description Interval E-value
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
2-329 2.44e-33

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 125.97  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947    2 RVCIIGAGVIGLSTAqsiyqhFHSRVSPLTIEVY-ADIFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNyLLSFLN 80
Cdd:pfam01266   1 DVVVIGGGIVGLSTA------YELARRGLSVTLLeRGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALD-LWEELE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947   81 SPDSIKMGIFLESGYNLCFEPMPEP------SFKQAVLGFRQLSKREL-EMFP---GFSFGWFN-TALVIEGKSYLPWLM 149
Cdd:pfam01266  74 EELGIDCGFRRCGVLVLARDEEEEAlekllaALRRLGVPAELLDAEELrELEPllpGLRGGLFYpDGGHVDPARLLRALA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  150 DWLNQRGVKFFQR-KIDSFKE------LSDSG-ADMIINCSGVRSGDLQP---DPELQPARGQIIKVDAPWLKH----WV 214
Cdd:pfam01266 154 RAAEALGVRIIEGtEVTGIEEeggvwgVVTTGeADAVVNAAGAWADLLALpglRLPVRPVRGQVLVLEPLPEALlilpVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  215 ITHDSKLGTYNTPYiiPGSRLVtVGGVFQVGNWNRMNSSVEHKQ-IWEGACKLEPSLqhARIVEDWTGLRPARSKVRLER 293
Cdd:pfam01266 234 ITVDPGRGVYLRPR--ADGRLL-LGGTDEEDGFDDPTPDPEEIEeLLEAARRLFPAL--ADIERAWAGLRPLPDGLPIIG 308
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 528478947  294 ESIRCGghsfeVIHNYGHGGFGLTIHRGCAEEAARL 329
Cdd:pfam01266 309 RPGSPG-----LYLATGHGGHGLTLAPGIGKLLAEL 339
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-329 8.71e-20

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 89.19  E-value: 8.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947   1 MRVCIIGAGVIGLSTAQsiyqHFHSR-VSPLTIEvyADiFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNYLLSFL 79
Cdd:COG0665    3 ADVVVIGGGIAGLSTAY----HLARRgLDVTVLE--RG-RPGSGASGRNAGQLRPGLAALADRALVRLAREALDLWRELA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  80 NspdsiKMGI---FLESGY-NLCFEPMPEPSFKQAV-------LGFRQLSKREL-EMFPGFSFG------WFNTALVIEG 141
Cdd:COG0665   76 A-----ELGIdcdFRRTGVlYLARTEAELAALRAEAealralgLPVELLDAAELrEREPGLGSPdyagglYDPDDGHVDP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947 142 KSYLPWLMDWLNQRGVKFFQR-KIDSFKE--------LSDSG---ADMIINCSGVRSGDLQP----DPELQPARGQII-- 203
Cdd:COG0665  151 AKLVRALARAARAAGVRIREGtPVTGLEReggrvtgvRTERGtvrADAVVLAAGAWSARLLPmlglRLPLRPVRGYVLvt 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947 204 KVDAPWLKHWVITHDsklGTYNTPYiiPGSRLVtVGGVFQVGNWNRMNSSVEHKQIWEGACKLEPSLQHARIVEDWTGLR 283
Cdd:COG0665  231 EPLPDLPLRPVLDDT---GVYLRPT--ADGRLL-VGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLR 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528478947 284 PArSKVRLER--ESIRCGGhsfeVIHNYGHGGFGLTIHRGCAEEAARL 329
Cdd:COG0665  305 PM-TPDGLPIigRLPGAPG----LYVATGHGGHGVTLAPAAGRLLADL 347
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
175-329 1.67e-10

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 61.61  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  175 ADMIINCSGVRSGDLQPDPeLQPARGQIIKVDAPW-------LKHWVITHDSklgtyntpYIIP--GSRLVtVGGVFQVG 245
Cdd:TIGR02352 182 ADQVVLAAGAWAGELLPLP-LRPVRGQPLRLEAPAvpllnrpLRAVVYGRRV--------YIVPrrDGRLV-VGATMEES 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  246 NWNRMNSSVEHKQIWEGACKLEPSLQHARIVEDWTGLRPARSKvrlerESIRCGGHSFE--VIHNYGHGGFGLTIHRGCA 323
Cdd:TIGR02352 252 GFDTTPTLGGIKELLRDAYTILPALKEARLLETWAGLRPGTPD-----NLPYIGEHPEDrrLLIATGHYRNGILLAPATA 326

                  ....*.
gi 528478947  324 EEAARL 329
Cdd:TIGR02352 327 EVIADL 332
 
Name Accession Description Interval E-value
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
2-329 2.44e-33

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 125.97  E-value: 2.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947    2 RVCIIGAGVIGLSTAqsiyqhFHSRVSPLTIEVY-ADIFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNyLLSFLN 80
Cdd:pfam01266   1 DVVVIGGGIVGLSTA------YELARRGLSVTLLeRGDDPGSGASGRNAGLIHPGLRYLEPSELARLALEALD-LWEELE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947   81 SPDSIKMGIFLESGYNLCFEPMPEP------SFKQAVLGFRQLSKREL-EMFP---GFSFGWFN-TALVIEGKSYLPWLM 149
Cdd:pfam01266  74 EELGIDCGFRRCGVLVLARDEEEEAlekllaALRRLGVPAELLDAEELrELEPllpGLRGGLFYpDGGHVDPARLLRALA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  150 DWLNQRGVKFFQR-KIDSFKE------LSDSG-ADMIINCSGVRSGDLQP---DPELQPARGQIIKVDAPWLKH----WV 214
Cdd:pfam01266 154 RAAEALGVRIIEGtEVTGIEEeggvwgVVTTGeADAVVNAAGAWADLLALpglRLPVRPVRGQVLVLEPLPEALlilpVP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  215 ITHDSKLGTYNTPYiiPGSRLVtVGGVFQVGNWNRMNSSVEHKQ-IWEGACKLEPSLqhARIVEDWTGLRPARSKVRLER 293
Cdd:pfam01266 234 ITVDPGRGVYLRPR--ADGRLL-LGGTDEEDGFDDPTPDPEEIEeLLEAARRLFPAL--ADIERAWAGLRPLPDGLPIIG 308
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 528478947  294 ESIRCGghsfeVIHNYGHGGFGLTIHRGCAEEAARL 329
Cdd:pfam01266 309 RPGSPG-----LYLATGHGGHGLTLAPGIGKLLAEL 339
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-329 8.71e-20

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 89.19  E-value: 8.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947   1 MRVCIIGAGVIGLSTAQsiyqHFHSR-VSPLTIEvyADiFTPLTTSDGAAGFWQPYLYDKGNVKETQWNKETFNYLLSFL 79
Cdd:COG0665    3 ADVVVIGGGIAGLSTAY----HLARRgLDVTVLE--RG-RPGSGASGRNAGQLRPGLAALADRALVRLAREALDLWRELA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  80 NspdsiKMGI---FLESGY-NLCFEPMPEPSFKQAV-------LGFRQLSKREL-EMFPGFSFG------WFNTALVIEG 141
Cdd:COG0665   76 A-----ELGIdcdFRRTGVlYLARTEAELAALRAEAealralgLPVELLDAAELrEREPGLGSPdyagglYDPDDGHVDP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947 142 KSYLPWLMDWLNQRGVKFFQR-KIDSFKE--------LSDSG---ADMIINCSGVRSGDLQP----DPELQPARGQII-- 203
Cdd:COG0665  151 AKLVRALARAARAAGVRIREGtPVTGLEReggrvtgvRTERGtvrADAVVLAAGAWSARLLPmlglRLPLRPVRGYVLvt 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947 204 KVDAPWLKHWVITHDsklGTYNTPYiiPGSRLVtVGGVFQVGNWNRMNSSVEHKQIWEGACKLEPSLQHARIVEDWTGLR 283
Cdd:COG0665  231 EPLPDLPLRPVLDDT---GVYLRPT--ADGRLL-VGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLR 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 528478947 284 PArSKVRLER--ESIRCGGhsfeVIHNYGHGGFGLTIHRGCAEEAARL 329
Cdd:COG0665  305 PM-TPDGLPIigRLPGAPG----LYVATGHGGHGVTLAPAAGRLLADL 347
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
175-329 1.67e-10

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 61.61  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  175 ADMIINCSGVRSGDLQPDPeLQPARGQIIKVDAPW-------LKHWVITHDSklgtyntpYIIP--GSRLVtVGGVFQVG 245
Cdd:TIGR02352 182 ADQVVLAAGAWAGELLPLP-LRPVRGQPLRLEAPAvpllnrpLRAVVYGRRV--------YIVPrrDGRLV-VGATMEES 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528478947  246 NWNRMNSSVEHKQIWEGACKLEPSLQHARIVEDWTGLRPARSKvrlerESIRCGGHSFE--VIHNYGHGGFGLTIHRGCA 323
Cdd:TIGR02352 252 GFDTTPTLGGIKELLRDAYTILPALKEARLLETWAGLRPGTPD-----NLPYIGEHPEDrrLLIATGHYRNGILLAPATA 326

                  ....*.
gi 528478947  324 EEAARL 329
Cdd:TIGR02352 327 EVIADL 332
 
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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