NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1052537219|gb|AOD23764|]
View 

(2Fe-2S)-binding protein [Rhodococcus sp. p52]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11433 super family cl36021
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
18-178 3.14e-79

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


The actual alignment was detected with superfamily member PRK11433:

Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 235.82  E-value: 3.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGD-GE 96
Cdd:PRK11433   52 VTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSpDN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEFADGAPSHVTADLEQAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:PRK11433  132 LHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIED 211

                  ..
gi 1052537219 177 VA 178
Cdd:PRK11433  212 VA 213
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
18-178 3.14e-79

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 235.82  E-value: 3.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGD-GE 96
Cdd:PRK11433   52 VTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSpDN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEFADGAPSHVTADLEQAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:PRK11433  132 LHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIED 211

                  ..
gi 1052537219 177 VA 178
Cdd:PRK11433  212 VA 213
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
18-178 2.14e-75

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: 223.82  E-value: 2.14e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLG-DGE 96
Cdd:COG2080     4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAeDGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadleqAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:COG2080    84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDE---------------NPNPTEEEIREALSGNLCRCTGYVRIVRAVKR 148

                  ..
gi 1052537219 177 VA 178
Cdd:COG2080   149 AA 150
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
18-178 1.10e-48

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 156.11  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLG-DGE 96
Cdd:NF041020   11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSkDGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadleqAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:NF041020   91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKE 155

                  ..
gi 1052537219 177 VA 178
Cdd:NF041020  156 AS 157
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
22-180 7.84e-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: 125.73  E-value: 7.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  22 VDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGDGEMHPLQ 101
Cdd:TIGR03198   8 VNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAENELDPCQ 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052537219 102 AQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadlEQAPEldDDEIRERMSGNLCRCAAYPNIVSAIRTVATG 180
Cdd:TIGR03198  88 TAFLEEGGFQCGYCTPGMVVALKALFRE-------------TPQPS--DEDMEEGLSGNLCRCTGYGGIIRSACRIRRG 151
Fer2_2 pfam01799
[2Fe-2S] binding domain;
88-174 3.04e-31

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 108.67  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  88 TAAGLGDGEMHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDefadgapshvtadlEQAPELDDDEIRERMSGNLCRCAAY 167
Cdd:pfam01799   1 TIEGLAESGGEPVQQAFAEAGAVQCGYCTPGMIMSAYALLE--------------RNPPPPTEAEIREALSGNLCRCTGY 66

                  ....*..
gi 1052537219 168 PNIVSAI 174
Cdd:pfam01799  67 RRIVDAV 73
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
18-80 4.76e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.15  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRdRLGITSPKkGCDLGQCGACTVLID------------------GRRTLSCLALAA 79
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAR-EAGIDIPY-SCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRVT 78

                  .
gi 1052537219  80 S 80
Cdd:cd00207    79 D 79
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
18-178 3.14e-79

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 235.82  E-value: 3.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGD-GE 96
Cdd:PRK11433   52 VTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSpDN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEFADGAPSHVTADLEQAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:PRK11433  132 LHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIED 211

                  ..
gi 1052537219 177 VA 178
Cdd:PRK11433  212 VA 213
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
18-178 2.14e-75

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: 223.82  E-value: 2.14e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLG-DGE 96
Cdd:COG2080     4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAeDGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadleqAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:COG2080    84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDE---------------NPNPTEEEIREALSGNLCRCTGYVRIVRAVKR 148

                  ..
gi 1052537219 177 VA 178
Cdd:COG2080   149 AA 150
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
18-178 1.10e-48

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 156.11  E-value: 1.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLG-DGE 96
Cdd:NF041020   11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSkDGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  97 MHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadleqAPELDDDEIRERMSGNLCRCAAYPNIVSAIRT 176
Cdd:NF041020   91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKE 155

                  ..
gi 1052537219 177 VA 178
Cdd:NF041020  156 AS 157
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
22-180 7.84e-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: 125.73  E-value: 7.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  22 VDGVERRVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGDGEMHPLQ 101
Cdd:TIGR03198   8 VNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAENELDPCQ 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052537219 102 AQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadlEQAPEldDDEIRERMSGNLCRCAAYPNIVSAIRTVATG 180
Cdd:TIGR03198  88 TAFLEEGGFQCGYCTPGMVVALKALFRE-------------TPQPS--DEDMEEGLSGNLCRCTGYGGIIRSACRIRRG 151
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
12-174 4.70e-34

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 118.87  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  12 HRPDLDIVLHVDGVERRVPIDVRTTVLDALRDRlGITSPKKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAG 91
Cdd:PRK09908    3 HSETITIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  92 LGDG-EMHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDEfadgapshvtadLEQAPeLDDDEIRERMSGNLCRCAAYPNI 170
Cdd:PRK09908   82 EAKGgKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAK------------PREKP-LTITEIRRGLAGNLCRCTGYQMI 148

                  ....
gi 1052537219 171 VSAI 174
Cdd:PRK09908  149 VNTV 152
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
18-179 6.46e-32

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


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 120.24  E-value: 6.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVP-IDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLI----DGRRTL----SCLALAASHDGAEIVT 88
Cdd:COG4630     1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgeldDGGLRYravnACILFLPQLDGKALVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  89 AAGLG--DGEMHPLQAQFIEDDAFQCGYCTPGQICSAVGMldefadgapshvtadLEQAPELDDDEIRERMSGNLCRCAA 166
Cdd:COG4630    81 VEGLAgpDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFAL---------------YERGPAPDRADIEDALSGNLCRCTG 145
                         170
                  ....*....|...
gi 1052537219 167 YPNIVSAIRTVAT 179
Cdd:COG4630   146 YRPIIDAARAMAE 158
Fer2_2 pfam01799
[2Fe-2S] binding domain;
88-174 3.04e-31

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 108.67  E-value: 3.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  88 TAAGLGDGEMHPLQAQFIEDDAFQCGYCTPGQICSAVGMLDefadgapshvtadlEQAPELDDDEIRERMSGNLCRCAAY 167
Cdd:pfam01799   1 TIEGLAESGGEPVQQAFAEAGAVQCGYCTPGMIMSAYALLE--------------RNPPPPTEAEIREALSGNLCRCTGY 66

                  ....*..
gi 1052537219 168 PNIVSAI 174
Cdd:pfam01799  67 RRIVDAV 73
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
32-173 4.57e-25

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: 101.20  E-value: 4.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  32 DVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLI----DGRRTL-----SCLALAASHDGAEIVTAAGLG--DGEMHPL 100
Cdd:TIGR02963  16 DPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKLRyrsvnACIQFLPSLDGKAVVTVEDLRqpDGRLHPV 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052537219 101 QAQFIEDDAFQCGYCTPGQICSAVGMldefadgapshvtadLEQAPELDDDEIRERMSGNLCRCAAYPNIVSA 173
Cdd:TIGR02963  96 QQAMVECHGSQCGFCTPGFVMSLYAL---------------YKNSPAPSRADIEDALQGNLCRCTGYRPILDA 153
PLN00192 PLN00192
aldehyde oxidase
17-179 8.26e-25

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 101.33  E-value: 8.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219   17 DIVLHVDGvER--RVPIDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTL----------SCLALAASHDGA 84
Cdd:PLN00192     5 SLVFAVNG-ERfeLSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYDPVldqvedftvsSCLTLLCSVNGC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219   85 EIVTAAGLGDGE--MHPLQAQFIEDDAFQCGYCTPGQICSAVGML---DEFADGAPSHVTADLEQApeldddEIRERMSG 159
Cdd:PLN00192    84 SITTSEGLGNSKdgFHPIHKRFAGFHASQCGFCTPGMCISLFSALvnaDKTDRPEPPSGFSKLTVV------EAEKAVSG 157
                          170       180
                   ....*....|....*....|
gi 1052537219  160 NLCRCAAYPNIVSAIRTVAT 179
Cdd:PLN00192   158 NLCRCTGYRPIVDACKSFAA 177
PLN02906 PLN02906
xanthine dehydrogenase
36-203 9.77e-23

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 95.15  E-value: 9.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219   36 TVLDALRDrLGITSPKKGCDLGQCGACTVL----------IDGRRTLSCLALAASHDGAEIVTAAGLG---DGeMHPLQA 102
Cdd:PLN02906     3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMvshydrktgkCVHYAVNACLAPLYSVEGMHVITVEGIGnrrDG-LHPVQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  103 QFIEDDAFQCGYCTPGQICSAVGMLdefadgapshvtADLEQAPEldDDEIRERMSGNLCRCAAYPNIVSAIRTVATGDS 182
Cdd:PLN02906    81 ALASMHGSQCGFCTPGFIMSMYALL------------RSSKTPPT--EEQIEECLAGNLCRCTGYRPILDAFRVFAKTDD 146
                          170       180
                   ....*....|....*....|.
gi 1052537219  183 RIGAGDSRIGVGDSRLDTEET 203
Cdd:PLN02906   147 ALYTGVSSLSLQDGEPICPST 167
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
17-176 3.80e-22

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: 93.54  E-value: 3.80e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219   17 DIVLHVDG---VERRVpiDVRTTVLDALRDRLGITSPKKGCDLGQCGACTVLIDGRRTLS----------CLALAASHDG 83
Cdd:TIGR02969    2 ELLFYVNGrkvVEKNV--DPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNPSTksirhhpvnaCLTPICSLYG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219   84 AEIVTAAGLGD--GEMHPLQAQFIEDDAFQCGYCTPGQICSavgmldefadgapshVTADLEQAPELDDDEIRERMSGNL 161
Cdd:TIGR02969   80 AAVTTVEGIGStrTRLHPVQERIAKCHGTQCGFCTPGMVMS---------------MYALLRNHPEPTLDQLTDALGGNL 144
                          170
                   ....*....|....*
gi 1052537219  162 CRCAAYPNIVSAIRT 176
Cdd:TIGR02969  145 CRCTGYRPIIDACKT 159
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
18-80 4.76e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.15  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  18 IVLHVDGVERRVPIDVRTTVLDALRdRLGITSPKkGCDLGQCGACTVLID------------------GRRTLSCLALAA 79
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAR-EAGIDIPY-SCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRVT 78

                  .
gi 1052537219  80 S 80
Cdd:cd00207    79 D 79
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
28-87 1.16e-05

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: 42.61  E-value: 1.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052537219  28 RVPIDVRTTVLDAL---RDRlgITSP---KKGCDLGQCGACTVLIDGRRTLSCLALAASHDGAEIV 87
Cdd:pfam13085  22 EVPYEEGMTVLDALnkiKEE--QDPTlafRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQDIT 85
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
16-174 1.03e-04

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 42.51  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  16 LDIVLHVDGVERRVPIDVRTTVLDALRdRLGITSPKKGCD-LGQCGACTVLIDGRRTLSCLALAASHDGAEIVTAAGLGD 94
Cdd:PRK09800    1 MIIHFTLNGAPQELTVNPGENVQKLLF-NMGMHSVRNSDDgFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052537219  95 G-EMHPLQAQFIEDDAFQCGYCTPgqicsAVGMLdefadgapshVTADLEQAPELDDDEIRERMSGNLCRCAAYPNIVSA 173
Cdd:PRK09800   80 WnELSLVQQAMVDVGVVQSGYNDP-----AAALI----------ITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQV 144

                  .
gi 1052537219 174 I 174
Cdd:PRK09800  145 I 145
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
26-88 1.04e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 42.04  E-value: 1.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052537219  26 ERRVPIDVRTTVLDALR---DRLGIT-SPKKGCDLGQCGACTVLIDGRRTLSC--LALAASHDGAEIVT 88
Cdd:PRK12576   26 EYKVKVDRFTQVTEALRrikEEQDPTlSYRASCHMAVCGSCGMKINGEPRLACktLVLDVAKKYNSVIT 94
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
29-86 1.50e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 38.83  E-value: 1.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052537219  29 VPIDVRTTVLDALR---DRLGIT-SPKKGCDLGQCGACTVLIDGRRTLSCLALAasHDGAEI 86
Cdd:PRK06259   25 VPVKEGMTVLDALEyinKTYDANiAFRSSCRAGQCGSCAVTINGEPVLACKTEV--EDGMII 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
20-74 2.28e-03

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 35.58  E-value: 2.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1052537219  20 LHVDGVERRVPIDV-RTTVLDALRdRLGITSPKkGCDLGQCGACTVLIDGRRTLSC 74
Cdd:pfam00111   1 VTINGKGVTIEVPDgETTLLDAAE-EAGIDIPY-SCRGGGCGTCAVKVLEGEDQSD 54
 
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