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Conserved domains on  [gi|446494623|ref|WP_000572477|]
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MULTISPECIES: molybdopterin-dependent oxidoreductase FAD-binding subunit [Escherichia]

Protein Classification

Se_sel_red_FAD family protein( domain architecture ID 11496598)

Se_sel_red_FAD family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Se_sel_red_FAD TIGR03312
probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., ...
2-258 2.74e-166

probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., to be the FAD-binding subunit of a molydbopterin-containing selenate reductase. Our comparative genomics suggests it to be a subunit of a selenium-dependent molybdenum hydroxylase for an unknown substrate.


:

Pssm-ID: 132355 [Multi-domain]  Cd Length: 257  Bit Score: 460.13  E-value: 2.74e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    2 IEQFFRPDSVEQALELKRRYQDEAVWFAGGSKLNATPTRTDKKIAISLQDLELDWVDWDNGALRIGAMSRLQTLRDARFI 81
Cdd:TIGR03312   1 IEQFFRPESTIQALELKKRHTGVAVWFAGGSKLNATPTRTDKKVAISLDKLALDKIELQGGALHIGAMCHLQSLIDNELT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   82 PAALREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVFGNGETLSIEEYLACPCDRLLTEIIIKDPYRTC 161
Cdd:TIGR03312  81 PAALKEALGFVYSRHIRNQATIGGEIAAFQSESLLLPVLLALKATVVLANASQMDIEDYLASEQRELIVEVIIPNPNLMC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  162 ATRKISRSQAGLTVVTAAVALTDHDGMRIALDGVASKALRLHDVEKQNLEGDALEQAVANAIFPQEDLRGSVAYKRYITG 241
Cdd:TIGR03312 161 ATRNISRSAAGLAVVTAAVAVDQKGNMRIALDGVSPVPVRLRDVEAQDLKGEALEQAVADAIHPVADLCGSVAYKRYIAG 240
                         250
                  ....*....|....*..
gi 446494623  242 VLVADLYADCQQAGEEA 258
Cdd:TIGR03312 241 VVVADLLAECQQLAQEA 257
 
Name Accession Description Interval E-value
Se_sel_red_FAD TIGR03312
probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., ...
2-258 2.74e-166

probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., to be the FAD-binding subunit of a molydbopterin-containing selenate reductase. Our comparative genomics suggests it to be a subunit of a selenium-dependent molybdenum hydroxylase for an unknown substrate.


Pssm-ID: 132355 [Multi-domain]  Cd Length: 257  Bit Score: 460.13  E-value: 2.74e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    2 IEQFFRPDSVEQALELKRRYQDEAVWFAGGSKLNATPTRTDKKIAISLQDLELDWVDWDNGALRIGAMSRLQTLRDARFI 81
Cdd:TIGR03312   1 IEQFFRPESTIQALELKKRHTGVAVWFAGGSKLNATPTRTDKKVAISLDKLALDKIELQGGALHIGAMCHLQSLIDNELT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   82 PAALREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVFGNGETLSIEEYLACPCDRLLTEIIIKDPYRTC 161
Cdd:TIGR03312  81 PAALKEALGFVYSRHIRNQATIGGEIAAFQSESLLLPVLLALKATVVLANASQMDIEDYLASEQRELIVEVIIPNPNLMC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  162 ATRKISRSQAGLTVVTAAVALTDHDGMRIALDGVASKALRLHDVEKQNLEGDALEQAVANAIFPQEDLRGSVAYKRYITG 241
Cdd:TIGR03312 161 ATRNISRSAAGLAVVTAAVAVDQKGNMRIALDGVSPVPVRLRDVEAQDLKGEALEQAVADAIHPVADLCGSVAYKRYIAG 240
                         250
                  ....*....|....*..
gi 446494623  242 VLVADLYADCQQAGEEA 258
Cdd:TIGR03312 241 VVVADLLAECQQLAQEA 257
CutB COG1319
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ...
4-246 2.54e-34

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


Pssm-ID: 440930 [Multi-domain]  Cd Length: 285  Bit Score: 124.85  E-value: 2.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   4 QFFRPDSVEQALELKRRYQDEAVWFAGGSKL-------NATPTRTdkkiaISLQDL-ELDWVDWDNGALRIGAMSRLQTL 75
Cdd:COG1319    5 EYHRPTSLEEALALLAEHGPDARVLAGGTDLlplmklrLARPEHL-----VDINRIpELRGIEEEGGGLRIGALVTHAEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  76 RDARFIPA---ALREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVF--GNGE-TLSIEEYLACPC---- 145
Cdd:COG1319   80 AASPLVRErypLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELagPDGErTIPAADFFLGPGetal 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623 146 --DRLLTEIII-KDPYRTCAT-RKIS-RSQAGLTVVTAAVALTDHDGM----RIALDGVASKALRLHDVEK----QNLEG 212
Cdd:COG1319  160 epGELITAVRLpAPPAGAGSAyLKVGrRASDAIALVSVAVALRLDGGTirdaRIALGGVAPTPWRAREAEAalagKPLSE 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446494623 213 DALEQA---VANAIFPQEDLRGSVAYKRYITGVLVAD 246
Cdd:COG1319  240 EAIEAAaeaAAAAADPIDDVRASAEYRRHLARVLVRR 276
FAD_binding_5 pfam00941
FAD binding domain in molybdopterin dehydrogenase;
4-154 9.41e-21

FAD binding domain in molybdopterin dehydrogenase;


Pssm-ID: 460007 [Multi-domain]  Cd Length: 170  Bit Score: 86.06  E-value: 9.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    4 QFFRPDSVEQALELKRRYQDeAVWFAGGSKL-------NATPtrtdkKIAISLQDL-ELDWVDWDNGALRIGAMSRLQTL 75
Cdd:pfam00941   4 GYYRPASLAEALELLAAGPD-AKLVAGGTSLgplmklrLARP-----DHLIDINGIpELRGIEETDGGLEIGAAVTLSEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   76 RD---ARFIPAaLREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVFGNGE---TLSIEEYL------AC 143
Cdd:pfam00941  78 AEpllREAYPA-LSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEgerTVPLEDFFlgygktAL 156
                         170
                  ....*....|.
gi 446494623  144 PCDRLLTEIII 154
Cdd:pfam00941 157 EPGELITAVII 167
CO_deh_flav_C smart01092
CO dehydrogenase flavoprotein C-terminal domain;
162-251 1.20e-10

CO dehydrogenase flavoprotein C-terminal domain;


Pssm-ID: 215021 [Multi-domain]  Cd Length: 102  Bit Score: 56.86  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   162 ATRKISRSQAGLTVVTAAVALTDHDG----MRIALDGVASKALRLHDVEK----QNLEGDALEQAVANAIF----PQEDL 229
Cdd:smart01092   1 AYKKSRRRDGDIALVSAAVALTLDGGrvteARIALGGVAPTPKRAAEAEAalvgKPLTDEALARAAAAALAqdftPLSDM 80
                           90       100
                   ....*....|....*....|..
gi 446494623   230 RGSVAYKRYITGVLVADLYADC 251
Cdd:smart01092  81 RASAEYRRQLAANLLRRALLEA 102
PRK09971 PRK09971
xanthine dehydrogenase subunit XdhB; Provisional
2-259 5.68e-09

xanthine dehydrogenase subunit XdhB; Provisional


Pssm-ID: 182175 [Multi-domain]  Cd Length: 291  Bit Score: 55.43  E-value: 5.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   2 IEQFFRPDSVEQALELkRRYQDEAVWFAGGS----KLNATPTRTDKKIAI----SLQDLELDwvdwDNGALRIGAMSRLQ 73
Cdd:PRK09971   4 IAEYHEAATLEEAIEL-LADNPQAKLIAGGTdvliQLHHHNDRYRHLVSIhniaELRGITLA----EDGSIRIGAATTFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  74 TLRDARFIPA---ALREALGFVYSRHIRNQSTIGGEI--AARQEESVllPVLLALDA--ELVFGNGETL-SIEEYLACPC 145
Cdd:PRK09971  79 QIIEDPIIQKhlpALAEAAVSIGGPQIRNVATIGGNIcnGATSADSA--PPLFALDAklEIHSPNGVRFvPINGFYTGPG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623 146 ------DRLLTEIII-KDPYRTCATRKI---SRSQAGLTVVTAAVALTDHDG----MRIALdGVASKA-LRLHDVE---- 206
Cdd:PRK09971 157 kvslehDEILVAFIIpPEPYEHAGGAYIkyaMRDAMDIATIGCAVLCRLDNGnfedLRLAF-GVAAPTpIRCQHAEqtak 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446494623 207 -----KQNLEgdALEQAVANAIFPQEDLRGSVAYKRYitgvLVADLyadCQQAGEEAV 259
Cdd:PRK09971 236 gaplnLETLE--AIGELVLQDVAPRSSWRASKEFRLH----LIQEL---TKRVIKEAV 284
 
Name Accession Description Interval E-value
Se_sel_red_FAD TIGR03312
probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., ...
2-258 2.74e-166

probable selenate reductase, FAD-binding subunit; This protein is suggested by Bebien, et al., to be the FAD-binding subunit of a molydbopterin-containing selenate reductase. Our comparative genomics suggests it to be a subunit of a selenium-dependent molybdenum hydroxylase for an unknown substrate.


Pssm-ID: 132355 [Multi-domain]  Cd Length: 257  Bit Score: 460.13  E-value: 2.74e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    2 IEQFFRPDSVEQALELKRRYQDEAVWFAGGSKLNATPTRTDKKIAISLQDLELDWVDWDNGALRIGAMSRLQTLRDARFI 81
Cdd:TIGR03312   1 IEQFFRPESTIQALELKKRHTGVAVWFAGGSKLNATPTRTDKKVAISLDKLALDKIELQGGALHIGAMCHLQSLIDNELT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   82 PAALREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVFGNGETLSIEEYLACPCDRLLTEIIIKDPYRTC 161
Cdd:TIGR03312  81 PAALKEALGFVYSRHIRNQATIGGEIAAFQSESLLLPVLLALKATVVLANASQMDIEDYLASEQRELIVEVIIPNPNLMC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  162 ATRKISRSQAGLTVVTAAVALTDHDGMRIALDGVASKALRLHDVEKQNLEGDALEQAVANAIFPQEDLRGSVAYKRYITG 241
Cdd:TIGR03312 161 ATRNISRSAAGLAVVTAAVAVDQKGNMRIALDGVSPVPVRLRDVEAQDLKGEALEQAVADAIHPVADLCGSVAYKRYIAG 240
                         250
                  ....*....|....*..
gi 446494623  242 VLVADLYADCQQAGEEA 258
Cdd:TIGR03312 241 VVVADLLAECQQLAQEA 257
CutB COG1319
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ...
4-246 2.54e-34

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


Pssm-ID: 440930 [Multi-domain]  Cd Length: 285  Bit Score: 124.85  E-value: 2.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   4 QFFRPDSVEQALELKRRYQDEAVWFAGGSKL-------NATPTRTdkkiaISLQDL-ELDWVDWDNGALRIGAMSRLQTL 75
Cdd:COG1319    5 EYHRPTSLEEALALLAEHGPDARVLAGGTDLlplmklrLARPEHL-----VDINRIpELRGIEEEGGGLRIGALVTHAEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  76 RDARFIPA---ALREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVF--GNGE-TLSIEEYLACPC---- 145
Cdd:COG1319   80 AASPLVRErypLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELagPDGErTIPAADFFLGPGetal 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623 146 --DRLLTEIII-KDPYRTCAT-RKIS-RSQAGLTVVTAAVALTDHDGM----RIALDGVASKALRLHDVEK----QNLEG 212
Cdd:COG1319  160 epGELITAVRLpAPPAGAGSAyLKVGrRASDAIALVSVAVALRLDGGTirdaRIALGGVAPTPWRAREAEAalagKPLSE 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446494623 213 DALEQA---VANAIFPQEDLRGSVAYKRYITGVLVAD 246
Cdd:COG1319  240 EAIEAAaeaAAAAADPIDDVRASAEYRRHLARVLVRR 276
FAD_binding_5 pfam00941
FAD binding domain in molybdopterin dehydrogenase;
4-154 9.41e-21

FAD binding domain in molybdopterin dehydrogenase;


Pssm-ID: 460007 [Multi-domain]  Cd Length: 170  Bit Score: 86.06  E-value: 9.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    4 QFFRPDSVEQALELKRRYQDeAVWFAGGSKL-------NATPtrtdkKIAISLQDL-ELDWVDWDNGALRIGAMSRLQTL 75
Cdd:pfam00941   4 GYYRPASLAEALELLAAGPD-AKLVAGGTSLgplmklrLARP-----DHLIDINGIpELRGIEETDGGLEIGAAVTLSEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   76 RD---ARFIPAaLREALGFVYSRHIRNQSTIGGEIAARQEESVLLPVLLALDAELVFGNGE---TLSIEEYL------AC 143
Cdd:pfam00941  78 AEpllREAYPA-LSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEgerTVPLEDFFlgygktAL 156
                         170
                  ....*....|.
gi 446494623  144 PCDRLLTEIII 154
Cdd:pfam00941 157 EPGELITAVII 167
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
4-258 3.60e-17

Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 80.18  E-value: 3.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   4 QFFRPDSVEQALELKRRYQDeAVWFAGGsklnatptrTD------KKIA-----ISLQDL-ELDWVDWDNGALRIGAMSR 71
Cdd:COG4630  193 RFLAPATLDELAALLAAHPD-ARLVAGA---------TDvglwvtKQLRdlppvIFLGRVaELRRIEETDDGLEIGAAVT 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  72 LQTLRDA--RFIPAaLREALGFVYSRHIRNQSTIGGEIA--------ArqeesvllPVLLALDAELVFGNGE---TLSIE 138
Cdd:COG4630  263 LSDAEAAlaAHFPE-LAELLRRFASRQIRNAGTLGGNIAngspigdsP--------PALIALGAELVLRSGDgrrTLPLE 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623 139 EY--------LAcPcDRLLTEIIIkdPYRTCATR----KIS-RSQAGLTVVTAAVALTDHDGM----RIALDGVASKALR 201
Cdd:COG4630  334 DFflgyrktdLQ-P-GEFVEAIRI--PLPAAGQRlrayKVSkRFDDDISAVCAAFALTLDDGTvteaRIAFGGMAATPKR 409
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446494623 202 LHDVEKQnLEG-----DALEQAVanAIFPQE-----DLRGSVAYKRYITGVLVADLYADCQQAGEEA 258
Cdd:COG4630  410 ARAAEAA-LLGqpwteATVAAAA--AALAQDftplsDMRASAEYRLAVAANLLRRFFLETQGEAPAT 473
CO_deh_flav_C smart01092
CO dehydrogenase flavoprotein C-terminal domain;
162-251 1.20e-10

CO dehydrogenase flavoprotein C-terminal domain;


Pssm-ID: 215021 [Multi-domain]  Cd Length: 102  Bit Score: 56.86  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   162 ATRKISRSQAGLTVVTAAVALTDHDG----MRIALDGVASKALRLHDVEK----QNLEGDALEQAVANAIF----PQEDL 229
Cdd:smart01092   1 AYKKSRRRDGDIALVSAAVALTLDGGrvteARIALGGVAPTPKRAAEAEAalvgKPLTDEALARAAAAALAqdftPLSDM 80
                           90       100
                   ....*....|....*....|..
gi 446494623   230 RGSVAYKRYITGVLVADLYADC 251
Cdd:smart01092  81 RASAEYRRQLAANLLRRALLEA 102
PRK09971 PRK09971
xanthine dehydrogenase subunit XdhB; Provisional
2-259 5.68e-09

xanthine dehydrogenase subunit XdhB; Provisional


Pssm-ID: 182175 [Multi-domain]  Cd Length: 291  Bit Score: 55.43  E-value: 5.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   2 IEQFFRPDSVEQALELkRRYQDEAVWFAGGS----KLNATPTRTDKKIAI----SLQDLELDwvdwDNGALRIGAMSRLQ 73
Cdd:PRK09971   4 IAEYHEAATLEEAIEL-LADNPQAKLIAGGTdvliQLHHHNDRYRHLVSIhniaELRGITLA----EDGSIRIGAATTFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  74 TLRDARFIPA---ALREALGFVYSRHIRNQSTIGGEI--AARQEESVllPVLLALDA--ELVFGNGETL-SIEEYLACPC 145
Cdd:PRK09971  79 QIIEDPIIQKhlpALAEAAVSIGGPQIRNVATIGGNIcnGATSADSA--PPLFALDAklEIHSPNGVRFvPINGFYTGPG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623 146 ------DRLLTEIII-KDPYRTCATRKI---SRSQAGLTVVTAAVALTDHDG----MRIALdGVASKA-LRLHDVE---- 206
Cdd:PRK09971 157 kvslehDEILVAFIIpPEPYEHAGGAYIkyaMRDAMDIATIGCAVLCRLDNGnfedLRLAF-GVAAPTpIRCQHAEqtak 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446494623 207 -----KQNLEgdALEQAVANAIFPQEDLRGSVAYKRYitgvLVADLyadCQQAGEEAV 259
Cdd:PRK09971 236 gaplnLETLE--AIGELVLQDVAPRSSWRASKEFRLH----LIQEL---TKRVIKEAV 284
PLN00192 PLN00192
aldehyde oxidase
6-156 6.03e-06

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 47.02  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623    6 FRPDSVEqalELKRRYqdEAVWFAGGS-KLNATPTRT---------DKKIAISlQDLELDWVDWDNGALRIGA---MSR- 71
Cdd:PLN00192  237 YTPVSVE---ELQSLL--ESNNFDGVSvKLVVGNTGTgyykdeelyDKYIDIR-HIPELSMIRRDEKGIEIGAvvtISKa 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623   72 LQTLRDAR---FIPAALREALGFVYSRHIRNQSTIGGEIAARQE---ESVLLPVLLALDAELVFGNG---ETLSIEEYLA 142
Cdd:PLN00192  311 IEALREESkseYVFKKIADHMEKIASRFVRNTGSIGGNLVMAQRkqfPSDIATILLAAGSTVNIQNAskrEKLTLEEFLE 390
                         170
                  ....*....|....*..
gi 446494623  143 -CPCD--RLLTEIIIKD 156
Cdd:PLN00192  391 rPPLDskSLLLSVEIPS 407
CO_deh_flav_C pfam03450
CO dehydrogenase flavoprotein C-terminal domain;
164-249 1.23e-05

CO dehydrogenase flavoprotein C-terminal domain;


Pssm-ID: 460921 [Multi-domain]  Cd Length: 102  Bit Score: 42.93  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446494623  164 RKISRSQAGLTVVTAAVALTDHDG----MRIALDGVASKALRLHDVEK----QNLEGDALEQA---VANAIFPQEDLRGS 232
Cdd:pfam03450   4 KQAKRRDDDIAIVNAAFRVRLDGGtvedARIAFGGVAPTPIRATEAEAaligKPWDEETLEAAaalLLEDLSPLSDPRGS 83
                          90
                  ....*....|....*..
gi 446494623  233 VAYKRYITGVLVADLYA 249
Cdd:pfam03450  84 AEYRRHLARSLLFRFLL 100
 
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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