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Conserved domains on  [gi|218521129|gb|ACK81714|]
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(2Fe-2S)-binding domain protein [Methylorubrum extorquens CM4]

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 ...
16-167 3.26e-76

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: 224.59  E-value: 3.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAglah 95
Cdd:COG2080    4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLA---- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218521129  96 reGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEEV 167
Cdd:COG2080   80 --EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
 
Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
16-167 3.26e-76

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: 224.59  E-value: 3.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAglah 95
Cdd:COG2080    4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLA---- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218521129  96 reGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEEV 167
Cdd:COG2080   80 --EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
7-167 3.61e-69

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 208.86  E-value: 3.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   7 SPGAVGTIGITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITT 86
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  87 VEGLAglahreGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNE------GHAK---------TRDEIREAMSGNI 151
Cdd:PRK11433 123 IEGLG------SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEikdgipSHVTvdltaapelTADEIRERMSGNI 196
                        170
                 ....*....|....*.
gi 218521129 152 CRCGAYTNIVDAIEEV 167
Cdd:PRK11433 197 CRCGAYSNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
13-166 8.23e-49

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 155.34  E-value: 8.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  13 TIGITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAg 92
Cdd:NF041020   8 KVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS- 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218521129  93 lahREGKnsLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEE 166
Cdd:NF041020  87 ---KDGK--LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKE 155
4hydroxCoAred TIGR03193
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ...
16-165 4.57e-36

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: 122.29  E-value: 4.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAGlah 95
Cdd:TIGR03193   2 LRLTVNGRWREDAVADNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKVETVEGLAT--- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   96 regKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIE 165
Cdd:TIGR03193  79 ---NGRLSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVE 145
Fer2_2 pfam01799
[2Fe-2S] binding domain;
86-164 4.24e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.53  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   86 TVEGLAGLAHregknslHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRD-EIREAMSGNICRCGAYTNIVDAI 164
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 ...
16-167 3.26e-76

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: 224.59  E-value: 3.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAglah 95
Cdd:COG2080    4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLA---- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218521129  96 reGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEEV 167
Cdd:COG2080   80 --EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
7-167 3.61e-69

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 208.86  E-value: 3.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   7 SPGAVGTIGITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITT 86
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  87 VEGLAglahreGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNE------GHAK---------TRDEIREAMSGNI 151
Cdd:PRK11433 123 IEGLG------SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEikdgipSHVTvdltaapelTADEIRERMSGNI 196
                        170
                 ....*....|....*.
gi 218521129 152 CRCGAYTNIVDAIEEV 167
Cdd:PRK11433 197 CRCGAYSNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
13-166 8.23e-49

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 155.34  E-value: 8.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  13 TIGITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAg 92
Cdd:NF041020   8 KVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS- 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218521129  93 lahREGKnsLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEE 166
Cdd:NF041020  87 ---KDGK--LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKE 155
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
16-173 1.98e-42

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


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 147.21  E-value: 1.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  16 ITLTINGERRALQ-VAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLV-----NGTR---INSCLTLAVMKDGAEITT 86
Cdd:COG4630    1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgelddGGLRyraVNACILFLPQLDGKALVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  87 VEGLAGlahreGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIEE 166
Cdd:COG4630   81 VEGLAG-----PDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARA 155

                 ....*..
gi 218521129 167 VMHQGDA 173
Cdd:COG4630  156 MAEAPAP 162
4hydroxCoAred TIGR03193
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ...
16-165 4.57e-36

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: 122.29  E-value: 4.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAGlah 95
Cdd:TIGR03193   2 LRLTVNGRWREDAVADNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKVETVEGLAT--- 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   96 regKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIE 165
Cdd:TIGR03193  79 ---NGRLSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVE 145
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
17-164 4.86e-36

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: 122.65  E-value: 4.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   17 TLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAglahr 96
Cdd:TIGR03198   5 RFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIA----- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 218521129   97 egKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAI 164
Cdd:TIGR03198  80 --ENELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSA 145
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
13-164 3.91e-35

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 120.41  E-value: 3.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  13 TIGITLTINGERRALQVAPwTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAg 92
Cdd:PRK09908   6 TITIECTINGMPFQLHAAP-GTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEA- 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218521129  93 lahreGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAK--TRDEIREAMSGNICRCGAYTNIVDAI 164
Cdd:PRK09908  84 -----KGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKplTITEIRRGLAGNLCRCTGYQMIVNTV 152
Fer2_2 pfam01799
[2Fe-2S] binding domain;
86-164 4.24e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.53  E-value: 4.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   86 TVEGLAGLAHregknslHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRD-EIREAMSGNICRCGAYTNIVDAI 164
Cdd:pfam01799   1 TIEGLAESGG-------EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTEaEIREALSGNLCRCTGYRRIVDAV 73
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
16-173 1.12e-34

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: 126.23  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   16 ITLTINGERRALQ-VAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLV----NGTRI-----NSCLTLAVMKDGAEIT 85
Cdd:TIGR02963   1 IRFFLNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKLryrsvNACIQFLPSLDGKAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   86 TVEGLaglahREGKNSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIE 165
Cdd:TIGR02963  81 TVEDL-----RQPDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAE 155

                  ....*...
gi 218521129  166 EVMHQGDA 173
Cdd:TIGR02963 156 AAFDYPCS 163
Se_dep_XDH TIGR03311
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ...
46-165 3.61e-29

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: 112.63  E-value: 3.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   46 TGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLAglaHREGKNSLHpiqeAFVEHDAFQCGYCTPGQL 125
Cdd:TIGR03311  29 TGVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTVEGLT---EREKDVYAW----AFAKAGAVQCGFCIPGMV 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 218521129  126 CSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIE 165
Cdd:TIGR03311 102 ISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVR 141
PLN02906 PLN02906
xanthine dehydrogenase
46-163 9.26e-29

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 111.33  E-value: 9.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   46 TGTKKGCDHGQCGACTVLV----NGTR------INSCLTLAVMKDGAEITTVEGLAglaHRegKNSLHPIQEAFVEHDAF 115
Cdd:PLN02906   14 TGTKLGCGEGGCGACTVMVshydRKTGkcvhyaVNACLAPLYSVEGMHVITVEGIG---NR--RDGLHPVQEALASMHGS 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 218521129  116 QCGYCTPGQLCSSVGLM-NEGHAKTRDEIREAMSGNICRCGAYTNIVDA 163
Cdd:PLN02906   89 QCGFCTPGFIMSMYALLrSSKTPPTEEQIEECLAGNLCRCTGYRPILDA 137
PLN00192 PLN00192
aldehyde oxidase
18-163 3.81e-27

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 106.72  E-value: 3.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   18 LTINGER-RALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVL----------VNGTRINSCLTLAVMKDGAEITT 86
Cdd:PLN00192    8 FAVNGERfELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLlskydpvldqVEDFTVSSCLTLLCSVNGCSITT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129   87 VEGLAGlahreGKNSLHPIQEAFVEHDAFQCGYCTPGqLCSSV--GLMN----------EGHAK-TRDEIREAMSGNICR 153
Cdd:PLN00192   88 SEGLGN-----SKDGFHPIHKRFAGFHASQCGFCTPG-MCISLfsALVNadktdrpeppSGFSKlTVVEAEKAVSGNLCR 161
                         170
                  ....*....|
gi 218521129  154 CGAYTNIVDA 163
Cdd:PLN00192  162 CTGYRPIVDA 171
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
46-163 1.44e-26

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: 105.09  E-value: 1.44e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129    46 TGTKKGCDHGQCGACTVLVNGTR----------INSCLTLAVMKDGAEITTVEGLAGLAHRegknsLHPIQEAFVEHDAF 115
Cdd:TIGR02969   34 TGTKYGCGGGGCGACTVMISRYNpstksirhhpVNACLTPICSLYGAAVTTVEGIGSTRTR-----LHPVQERIAKCHGT 108
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 218521129   116 QCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDA 163
Cdd:TIGR02969  109 QCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDA 156
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
16-165 6.58e-11

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 59.85  E-value: 6.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218521129  16 ITLTINGERRALQVAPWTTLLDLLRERLDLTGTKKGCDHGQCGACTVLVNGTRINSCLTLAVMKDGAEITTVEGLaglah 95
Cdd:PRK09800   3 IHFTLNGAPQELTVNPGENVQKLLFNMGMHSVRNSDDGFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESL----- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218521129  96 reGK-NSLHPIQEAFVEHDAFQCGYCTPGQLCSSVGLMNEGHAKTRDEIREAMSGNICRCGAYTNIVDAIE 165
Cdd:PRK09800  78 --GKwNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIE 146
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
51-93 1.28e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 36.83  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 218521129   51 GCDHGQCGACTVLVNGTRINSCLTLaVMKDGAEITTVEGLAGL 93
Cdd:pfam13085  51 SCREGICGSCAMNINGKPRLACKTL-IDDLLGQDITLEPLPGF 92
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
52-90 1.63e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 37.81  E-value: 1.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 218521129  52 CDHGQCGACTVLVNGTRINSCLTLA--VMKDGAEITTVEGL 90
Cdd:PRK12576  58 CHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPM 98
 
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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