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Conserved domains on  [gi|15597127|ref|NP_250621|]
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ferredoxin [Pseudomonas aeruginosa PAO1]

Protein Classification

(2Fe-2S)-binding protein( domain architecture ID 11449880)

(2Fe-2S)-binding protein is the small subunit of a dehydrogenase or oxidoreductase enzyme complex such as carbon monoxide dehydrogenase and isoquinoline 1-oxidoreductase; contains a a 2Fe-2S ferredoxin-type domain which binds 2Fe-2S clusters

Gene Ontology:  GO:0046872|GO:0051536|GO:0051537
PubMed:  11734195
SCOP:  3000113

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
10-156 1.74e-72

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


:

Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 214.96  E-value: 1.74e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127  10 PISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGD 89
Cdd:COG2080   3 MITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597127  90 RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:COG2080  83 ELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
 
Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
10-156 1.74e-72

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


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 214.96  E-value: 1.74e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127  10 PISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGD 89
Cdd:COG2080   3 MITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597127  90 RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:COG2080  83 ELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
2-156 6.31e-68

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 205.78  E-value: 6.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    2 TNPEPADLPISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTT 81
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   82 IEGLAEGDRLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRAR---------------SRAEIREGMSGNLCRCGAY 146
Cdd:PRK11433 123 IEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGipshvtvdltaapelTADEIRERMSGNICRCGAY 202
                        170
                 ....*....|
gi 15597127  147 GNILDAVEDA 156
Cdd:PRK11433 203 SNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
11-156 5.58e-47

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 150.72  E-value: 5.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   11 ISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGDR 90
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597127   91 LHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEA 156
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
10-153 8.21e-37

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 124.19  E-value: 8.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    10 PISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEgD 89
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-N 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597127    90 RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAV 153
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSA 145
Fer2_2 pfam01799
[2Fe-2S] binding domain;
81-153 9.27e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 116.38  E-value: 9.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597127    81 TIEGLAEGDRlHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSR-AEIREGMSGNLCRCGAYGNILDAV 153
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTeAEIREALSGNLCRCTGYRRIVDAV 73
 
Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
10-156 1.74e-72

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


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 214.96  E-value: 1.74e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127  10 PISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGD 89
Cdd:COG2080   3 MITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597127  90 RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:COG2080  83 ELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
2-156 6.31e-68

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 205.78  E-value: 6.31e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    2 TNPEPADLPISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTT 81
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   82 IEGLAEGDRLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRAR---------------SRAEIREGMSGNLCRCGAY 146
Cdd:PRK11433 123 IEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGipshvtvdltaapelTADEIRERMSGNICRCGAY 202
                        170
                 ....*....|
gi 15597127  147 GNILDAVEDA 156
Cdd:PRK11433 203 SNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
11-156 5.58e-47

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 150.72  E-value: 5.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   11 ISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGDR 90
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597127   91 LHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEA 156
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
11-163 6.00e-40

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


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 140.27  E-value: 6.00e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127  11 ISLLINGQRRELR-VPP------WLTLLDLLrerldlVGSKKGCDHGQCGACTV----LRNGRR----INACLTLAVMCD 75
Cdd:COG4630   1 IRFLLNGELVELSdVPPtttlldWLREDRGL------TGTKEGCAEGDCGACTVvvgeLDDGGLryraVNACILFLPQLD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127  76 GDALTTIEGLAEGD-RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVE 154
Cdd:COG4630  75 GKALVTVEGLAGPDgALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAAR 154

                ....*....
gi 15597127 155 DALPLLDRD 163
Cdd:COG4630 155 AMAEAPAPD 163
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
10-153 8.21e-37

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 124.19  E-value: 8.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    10 PISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEgD 89
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-N 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597127    90 RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAV 153
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSA 145
4hydroxCoAred TIGR03193
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ...
11-156 9.91e-37

4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.


Pssm-ID: 132237 [Multi-domain]  Cd Length: 148  Bit Score: 123.83  E-value: 9.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    11 ISLLINGQRRELRVPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGDR 90
Cdd:TIGR03193   2 LRLTVNGRWREDAVADNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKVETVEGLATNGR 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597127    91 LHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:TIGR03193  82 LSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVEAA 147
Fer2_2 pfam01799
[2Fe-2S] binding domain;
81-153 9.27e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 116.38  E-value: 9.27e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597127    81 TIEGLAEGDRlHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSR-AEIREGMSGNLCRCGAYGNILDAV 153
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTeAEIREALSGNLCRCTGYRRIVDAV 73
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
44-155 1.38e-34

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 118.87  E-value: 1.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   44 KKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGDRLHPLQQAFIRHDAFQCGYCTPGQICSALGLASE 123
Cdd:PRK09908  41 KQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAK 120
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15597127  124 GRAR--SRAEIREGMSGNLCRCGAYGNILDAVED 155
Cdd:PRK09908 121 PREKplTITEIRRGLAGNLCRCTGYQMIVNTVLD 154
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
11-154 1.66e-31

xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274365 [Multi-domain]  Cd Length: 467  Bit Score: 117.76  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    11 ISLLINGQRRELR-VPPWLTLLDLLRERLDLVGSKKGCDHGQCGACTV----LRNGRRI-----NACLTLAVMCDGDALT 80
Cdd:TIGR02963   1 IRFFLNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVvvgeLVDGGKLryrsvNACIQFLPSLDGKAVV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597127    81 TIEGLAEGD-RLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVE 154
Cdd:TIGR02963  81 TVEDLRQPDgRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAE 155
PLN02906 PLN02906
xanthine dehydrogenase
42-152 9.99e-29

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 110.94  E-value: 9.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    42 GSKKGCDHGQCGACTVLR----------NGRRINACLTLAVMCDGDALTTIEGLA-EGDRLHPLQQAFIRHDAFQCGYCT 110
Cdd:PLN02906   15 GTKLGCGEGGCGACTVMVshydrktgkcVHYAVNACLAPLYSVEGMHVITVEGIGnRRDGLHPVQEALASMHGSQCGFCT 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15597127   111 PGQICS--ALgLASEGRARSRAEIREGMSGNLCRCGAYGNILDA 152
Cdd:PLN02906   95 PGFIMSmyAL-LRSSKTPPTEEQIEECLAGNLCRCTGYRPILDA 137
Se_dep_XDH TIGR03311
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ...
42-156 5.75e-27

selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132354 [Multi-domain]  Cd Length: 848  Bit Score: 106.08  E-value: 5.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    42 GSKKGCDHGQCGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEGDRlHPLQQAFIRHDAFQCGYCTPGQICSALGLA 121
Cdd:TIGR03311  30 GVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTVEGLTEREK-DVYAWAFAKAGAVQCGFCIPGMVISAKALL 108
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15597127   122 SEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:TIGR03311 109 DKNPNPTEAEIKKALKGNICRCTGYVKIIKAVRLA 143
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
42-152 3.29e-23

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: 95.46  E-value: 3.29e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127     42 GSKKGCDHGQCGACTVL-----RNGRRI-----NACLTLAVMCDGDALTTIEGLAEG-DRLHPLQQAFIRHDAFQCGYCT 110
Cdd:TIGR02969   35 GTKYGCGGGGCGACTVMisrynPSTKSIrhhpvNACLTPICSLYGAAVTTVEGIGSTrTRLHPVQERIAKCHGTQCGFCT 114
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 15597127    111 PGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDA 152
Cdd:TIGR02969  115 PGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDA 156
PLN00192 PLN00192
aldehyde oxidase
42-152 6.72e-21

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 88.62  E-value: 6.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127    42 GSKKGCDHGQCGACTVLRNGR----------RINACLTLAVMCDGDALTTIEGLAEG-DRLHPLQQAFIRHDAFQCGYCT 110
Cdd:PLN00192   38 SVKLGCGEGGCGACVVLLSKYdpvldqvedfTVSSCLTLLCSVNGCSITTSEGLGNSkDGFHPIHKRFAGFHASQCGFCT 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597127   111 PG---QICSALGLA--------SEGRAR-SRAEIREGMSGNLCRCGAYGNILDA 152
Cdd:PLN00192  118 PGmciSLFSALVNAdktdrpepPSGFSKlTVVEAEKAVSGNLCRCTGYRPIVDA 171
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
11-156 5.09e-10

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 57.15  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597127   11 ISLLINGQRRELRVPPwlTLLDLLRERLDLVGSKKGCDHGQ--CGACTVLRNGRRINACLTLAVMCDGDALTTIEGLAEG 88
Cdd:PRK09800   3 IHFTLNGAPQELTVNP--GENVQKLLFNMGMHSVRNSDDGFgfAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKW 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597127   89 DRLHPLQQAFIRHDAFQCGYCTPGQICSALGLASEGRARSRAEIREGMSGNLCRCGAYGNILDAVEDA 156
Cdd:PRK09800  81 NELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELA 148
 
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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