NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1771861168|ref|WP_153003945|]
View 

xanthine dehydrogenase family protein molybdopterin-binding subunit, partial [Aureimonas ureilytica]

Protein Classification

xanthine dehydrogenase family protein molybdopterin-binding subunit( domain architecture ID 11445946)

xanthine dehydrogenase family protein molybdopterin-binding subunit is part of an oxidase/dehydrogenase complex acting on one or more of a variety of substrates

EC:  1.-.-.-
Gene Ontology:  GO:0043546
PubMed:  27537049

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CoxL COG1529
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
5-255 1.39e-83

Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


:

Pssm-ID: 441138 [Multi-domain]  Cd Length: 741  Bit Score: 264.40  E-value: 1.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   5 GFGARVLRKEDRRFITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIgnlicgw 84
Cdd:COG1529     9 IIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDLPGLKF------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  85 avtskdGSPMKMGEWPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPEAPGNL 164
Cdd:COG1529    82 ------GLPGPDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAALAPGAPLVHEELPGNV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168 165 CFDWELGDArATEEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGVYDPaDDHYTVWTTSQNPHVARLVMSAFYNVaPEHK 244
Cdd:COG1529   156 AAEWRGERG-DVDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDG-DGRLTVWASTQGPHLVRRALARALGL-PPEK 232
                         250
                  ....*....|.
gi 1771861168 245 LRVIAPDVGGG 255
Cdd:COG1529   233 VRVIAPDVGGG 243
 
Name Accession Description Interval E-value
CoxL COG1529
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
5-255 1.39e-83

Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441138 [Multi-domain]  Cd Length: 741  Bit Score: 264.40  E-value: 1.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   5 GFGARVLRKEDRRFITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIgnlicgw 84
Cdd:COG1529     9 IIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDLPGLKF------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  85 avtskdGSPMKMGEWPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPEAPGNL 164
Cdd:COG1529    82 ------GLPGPDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAALAPGAPLVHEELPGNV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168 165 CFDWELGDArATEEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGVYDPaDDHYTVWTTSQNPHVARLVMSAFYNVaPEHK 244
Cdd:COG1529   156 AAEWRGERG-DVDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDG-DGRLTVWASTQGPHLVRRALARALGL-PPEK 232
                         250
                  ....*....|.
gi 1771861168 245 LRVIAPDVGGG 255
Cdd:COG1529   233 VRVIAPDVGGG 243
Ald_Xan_dh_C smart01008
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ...
20-140 4.43e-35

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.


Pssm-ID: 214971 [Multi-domain]  Cd Length: 107  Bit Score: 121.09  E-value: 4.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   20 TGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGignlicgwavtskdGSPMKMGEW 99
Cdd:smart01008   1 TGEARYGDDIRLPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLN--------------DFGPLGPDE 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1771861168  100 PALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLD 140
Cdd:smart01008  67 PVLADDKVRYVGQPVAAVVAETEEAARDAAEAVKVEYEELP 107
MoCoBD_1 pfam02738
Molybdopterin cofactor-binding domain;
156-255 2.47e-33

Molybdopterin cofactor-binding domain;


Pssm-ID: 460671 [Multi-domain]  Cd Length: 244  Bit Score: 121.02  E-value: 2.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168 156 IHPEAPGNLCFDWELGDAratEEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGVYDPADDHYTVWTTSQNPHVARLVMSA 235
Cdd:pfam02738   1 LHEEPPNNVAFHREKGDV---EAAFAEADHVVEGEYRTGRQEHFYMETRAALAVPDDEDGRLTVYSSTQGPHLVRRLVAR 77
                          90       100
                  ....*....|....*....|
gi 1771861168 236 FYNVaPEHKLRVIAPDVGGG 255
Cdd:pfam02738  78 VLGI-PENKVRVIVPRVGGG 96
PRK09970 PRK09970
xanthine dehydrogenase subunit XdhA; Provisional
19-255 8.52e-31

xanthine dehydrogenase subunit XdhA; Provisional


Pssm-ID: 236637 [Multi-domain]  Cd Length: 759  Bit Score: 120.19  E-value: 8.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  19 ITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIGNLICGWavtSKDGSPMKMGE 98
Cdd:PRK09970   16 VTGRAKYTDDYVMAGMLYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDVPDIPFPTAGHPW---SLDPNHRDIAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  99 WpALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPEApGNLC--FDWELGDaraT 176
Cdd:PRK09970   93 R-ALLTRHVRHHGDAVAAVVARDELTAEKALKLIKVEYEELPVITDPEAALAEGAPPIHNGR-GNLLkqSTMSTGN---V 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771861168 177 EEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGvYDPADDHYTVWTTSQNPHVARLVMSAFYNVaPEHKLRVIAPDVGGG 255
Cdd:PRK09970  168 QQTIKAADYQVQGHYETPIVQHCHMENVTSYA-YMEDDGRITIVSSTQIPHIVRRVVGQALGI-PWGKVRVIKPYVGGG 244
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
20-143 1.99e-13

aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.


Pssm-ID: 132014 [Multi-domain]  Cd Length: 1330  Bit Score: 69.65  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   20 TGRGRYTDDM-VVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLkadgignlicgwavtsKDGSpmKMGE 98
Cdd:TIGR02969  590 TGEAIYCDDMpAVDQELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAEHL----------------QDAN--TFGT 651
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1771861168   99 WPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVV 143
Cdd:TIGR02969  652 EKLLATDKVHCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLI 696
 
Name Accession Description Interval E-value
CoxL COG1529
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
5-255 1.39e-83

Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441138 [Multi-domain]  Cd Length: 741  Bit Score: 264.40  E-value: 1.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   5 GFGARVLRKEDRRFITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIgnlicgw 84
Cdd:COG1529     9 IIGKPVPRVDGPAKVTGRARYTDDIRLPGMLYAAVVRSPHAHARIKSIDTSAALALPGVVAVLTGEDLPGLKF------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  85 avtskdGSPMKMGEWPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPEAPGNL 164
Cdd:COG1529    82 ------GLPGPDPDQPPLADDKVRYVGEPVAAVVAETREAARDAAELIKVEYEPLPAVVDPEAALAPGAPLVHEELPGNV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168 165 CFDWELGDArATEEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGVYDPaDDHYTVWTTSQNPHVARLVMSAFYNVaPEHK 244
Cdd:COG1529   156 AAEWRGERG-DVDAAFAEADVVVEATYTTPRLAHAPMEPRAAVAEWDG-DGRLTVWASTQGPHLVRRALARALGL-PPEK 232
                         250
                  ....*....|.
gi 1771861168 245 LRVIAPDVGGG 255
Cdd:COG1529   233 VRVIAPDVGGG 243
Ald_Xan_dh_C smart01008
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses ...
20-140 4.43e-35

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.


Pssm-ID: 214971 [Multi-domain]  Cd Length: 107  Bit Score: 121.09  E-value: 4.43e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   20 TGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGignlicgwavtskdGSPMKMGEW 99
Cdd:smart01008   1 TGEARYGDDIRLPGMLHAAVVRSPVAHARIKSIDTSAARAMPGVVAVLTAKDVPGLN--------------DFGPLGPDE 66
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1771861168  100 PALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLD 140
Cdd:smart01008  67 PVLADDKVRYVGQPVAAVVAETEEAARDAAEAVKVEYEELP 107
MoCoBD_1 pfam02738
Molybdopterin cofactor-binding domain;
156-255 2.47e-33

Molybdopterin cofactor-binding domain;


Pssm-ID: 460671 [Multi-domain]  Cd Length: 244  Bit Score: 121.02  E-value: 2.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168 156 IHPEAPGNLCFDWELGDAratEEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGVYDPADDHYTVWTTSQNPHVARLVMSA 235
Cdd:pfam02738   1 LHEEPPNNVAFHREKGDV---EAAFAEADHVVEGEYRTGRQEHFYMETRAALAVPDDEDGRLTVYSSTQGPHLVRRLVAR 77
                          90       100
                  ....*....|....*....|
gi 1771861168 236 FYNVaPEHKLRVIAPDVGGG 255
Cdd:pfam02738  78 VLGI-PENKVRVIVPRVGGG 96
PRK09970 PRK09970
xanthine dehydrogenase subunit XdhA; Provisional
19-255 8.52e-31

xanthine dehydrogenase subunit XdhA; Provisional


Pssm-ID: 236637 [Multi-domain]  Cd Length: 759  Bit Score: 120.19  E-value: 8.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  19 ITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIGNLICGWavtSKDGSPMKMGE 98
Cdd:PRK09970   16 VTGRAKYTDDYVMAGMLYAKYVRSPIAHGKVKSIDTEEARSLPGVEAVFTWEDVPDIPFPTAGHPW---SLDPNHRDIAD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  99 WpALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPEApGNLC--FDWELGDaraT 176
Cdd:PRK09970   93 R-ALLTRHVRHHGDAVAAVVARDELTAEKALKLIKVEYEELPVITDPEAALAEGAPPIHNGR-GNLLkqSTMSTGN---V 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1771861168 177 EEAFSRAAHVTRLDIVNNRLVPNAMEPRAALGvYDPADDHYTVWTTSQNPHVARLVMSAFYNVaPEHKLRVIAPDVGGG 255
Cdd:PRK09970  168 QQTIKAADYQVQGHYETPIVQHCHMENVTSYA-YMEDDGRITIVSSTQIPHIVRRVVGQALGI-PWGKVRVIKPYVGGG 244
Ald_Xan_dh_C pfam01315
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain;
20-140 1.74e-30

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain;


Pssm-ID: 426197 [Multi-domain]  Cd Length: 107  Bit Score: 109.63  E-value: 1.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  20 TGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGIGnlicgwavtskdgsPMKMGEW 99
Cdd:pfam01315   1 TGEAVYVDDIPAPGNLYGAFVRSTIAHAKIVSIDTSAALALPGVVAVITAKDLPGGNYN--------------IGPIPLD 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1771861168 100 PALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLD 140
Cdd:pfam01315  67 PLFATDKVRHVGQPIAAVVADDEETARRAAKLVKVEYEELP 107
PLN02906 PLN02906
xanthine dehydrogenase
19-255 2.46e-15

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 75.12  E-value: 2.46e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   19 ITGRGRYTDDMVVP-GMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADgigNLIcGWAVTSKDgspmkmg 97
Cdd:PLN02906   578 VTGEAEYADDIPMPpNTLHAALVLSTKPHARILSIDDSEAKSSPGFAGIFLAKDVPGD---NMI-GPVVHDEE------- 646
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   98 ewpALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGApeIHPEAPGNLcfdwELGDAratE 177
Cdd:PLN02906   647 ---LFATDVVTCVGQVIGVVVADTQENAKAAARKVKVEYEELPAILSIEEAIEAGS--FHPNTERRL----EKGDV---E 714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  178 EAFSRAAHVtrlDIVNNRLVPNA-----MEPRAALGVYDPADDHYTVWTTSQNPHVARLVMSAFYNVaPEHKLRVIAPDV 252
Cdd:PLN02906   715 LCFASGQCD---RIIEGEVQMGGqehfyLEPNSSLVWTSDSGNEVHMISSTQAPQKHQKYVAHVLGL-PMSKVVCKTKRI 790

                   ...
gi 1771861168  253 GGG 255
Cdd:PLN02906   791 GGG 793
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
20-143 1.99e-13

aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.


Pssm-ID: 132014 [Multi-domain]  Cd Length: 1330  Bit Score: 69.65  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   20 TGRGRYTDDM-VVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLkadgignlicgwavtsKDGSpmKMGE 98
Cdd:TIGR02969  590 TGEAIYCDDMpAVDQELFLTFVTSSRAHAKIVSIDLSEALSLPGVVDIITAEHL----------------QDAN--TFGT 651
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1771861168   99 WPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVV 143
Cdd:TIGR02969  652 EKLLATDKVHCVGQLVCAVIADSEVQAKQAAKHVKIVYRDLEPLI 696
PLN00192 PLN00192
aldehyde oxidase
20-255 5.61e-10

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 59.34  E-value: 5.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   20 TGRGRYTDDmvVPGMK---FAAFVRSPHAHARIKGIDASAAREMPGVIDILSGDQLKADGignlicgwavtSKDGSPMKM 96
Cdd:PLN00192   593 SGEAVYVDD--IPSPKnclYGAFIYSTKPLARVKGIKFKSNLVPQGVLAVITFKDIPKGG-----------QNIGSKTIF 659
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168   97 GEWPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYEL---------LDAVVEGPAALEAgAPEIHPEapgnlcfd 167
Cdd:PLN00192   660 GPEPLFADEVTRCAGQRIALVVADTQKHADMAANLAVVEYDTenleppiltVEDAVKRSSLFEV-PPFLYPK-------- 730
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  168 wELGDaraTEEAFSRAAHvtrlDIVNNRLVPNA-----MEPRAALGVYDpADDHYTVWTTSQNPHVARLVMSAFYNVaPE 242
Cdd:PLN00192   731 -PVGD---ISKGMAEADH----KILSAEIKLGSqyyfyMETQTALALPD-EDNCIVVYSSTQCPEYVHSVIARCLGI-PE 800
                          250
                   ....*....|...
gi 1771861168  243 HKLRVIAPDVGGG 255
Cdd:PLN00192   801 HNVRVITRRVGGG 813
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
17-159 4.19e-08

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 53.68  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1771861168  17 RFITGRGRYTDDMVVPGMKFAAFVRSPHAHARIKGIDASAAREMPGVIDIlsgdqlkadgIGNLICG--WAVTSKDGSPM 94
Cdd:PRK09800  183 KMVQAKPCYVEDRVTADACVIKMLRSPHAHALITHLDVSKAEALPGVVHV----------ITHLNCPdiYYTPGGQSAPE 252
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1771861168  95 KMGEWPALAVGTVRHVGQAVAVVVADSKLQARDAAEAVEVDYELLDAVVEGPAALEAGAPEIHPE 159
Cdd:PRK09800  253 PSPLDRRMFGKKMRHVGDRVAAVVAESEEIALEALKLIDVEYEVLKPVMSIDEAMAEDAPVVHDE 317
 
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