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Conserved domains on  [gi|2136496089|gb|UEQ04018|]
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2Fe-2S iron-sulfur cluster-binding protein [Halomonas profundus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11433 super family cl36021
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-188 4.95e-108

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: 307.85  E-value: 4.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   1 MNPPNSAERHRETAQNGAERSNVSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACL 80
Cdd:PRK11433   30 AYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  81 TLAVMHEGDDVATIEGLGEADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADLPSHVTKDLTAPIEMTDAEIC 160
Cdd:PRK11433  110 TLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIR 189

                         170       180
                  ....*....|....*....|....*...
gi 2136496089 161 ERMSGNLCRCGAYANILKAIKQVAEARA 188
Cdd:PRK11433  190 ERMSGNICRCGAYSNILEAIEDVAGEIA 217
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-188 4.95e-108

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 307.85  E-value: 4.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   1 MNPPNSAERHRETAQNGAERSNVSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACL 80
Cdd:PRK11433   30 AYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  81 TLAVMHEGDDVATIEGLGEADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADLPSHVTKDLTAPIEMTDAEIC 160
Cdd:PRK11433  110 TLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIR 189

                         170       180
                  ....*....|....*....|....*...
gi 2136496089 161 ERMSGNLCRCGAYANILKAIKQVAEARA 188
Cdd:PRK11433  190 ERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 23-188 4.74e-84

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: 245.00  E-value: 4.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLGEADH 102
Cdd:COG2080     4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089 103 LNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRAdlPshvtkdltapiemTDAEICERMSGNLCRCGAYANILKAIKQ 182
Cdd:COG2080    84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPN--P-------------TEEEIREALSGNLCRCTGYVRIVRAVKR 148


                  ....*.
gi 2136496089 183 VAEARA 188
Cdd:COG2080   149 AAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
19-185 1.27e-48

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 155.34  E-value: 1.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  19 ERSNVSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLG 98
Cdd:NF041020    7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  99 EADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRadlpshvtkdltapiEMTDAEICERMSGNLCRCGAYANILK 178
Cdd:NF041020   87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENP---------------NPTEEEIRDGIHGNLCRCTGYQNIVK 151


                  ....*..
gi 2136496089 179 AIKQVAE 185
Cdd:NF041020  152 AVKEASQ 158
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 27-185 1.66e-41

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: 136.90  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  27 VNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLGEaDHLNPM 106
Cdd:TIGR03198   8 VNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NELDPC 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136496089 107 QQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADlpshvtkdltapiemTDAEICERMSGNLCRCGAYANILKAIKQVAE 185
Cdd:TIGR03198  87 QTAFLEEGGFQCGYCTPGMVVALKALFRETPQP---------------SDEDMEEGLSGNLCRCTGYGGIIRSACRIRR 150
Fer2_2 pfam01799
[2Fe-2S] binding domain;
93-180 4.77e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 115.22  E-value: 4.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  93 TIEGLGEADHlNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEvradlpshvtkdltAPIEMTDAEICERMSGNLCRCGA 172
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 2136496089 173 YANILKAI 180
Cdd:pfam01799  66 YRRIVDAV 73
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 23-72 1.28e-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: 44.69  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLELDNRTTLLDALREHLKltGTKKGCDHGQCGACTVSVN 72
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAREAGI--DIPYSCRAGACGTCKVEVV 48
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-188 4.95e-108

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 307.85  E-value: 4.95e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   1 MNPPNSAERHRETAQNGAERSNVSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACL 80
Cdd:PRK11433   30 AYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  81 TLAVMHEGDDVATIEGLGEADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADLPSHVTKDLTAPIEMTDAEIC 160
Cdd:PRK11433  110 TLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIR 189

                         170       180
                  ....*....|....*....|....*...
gi 2136496089 161 ERMSGNLCRCGAYANILKAIKQVAEARA 188
Cdd:PRK11433  190 ERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 23-188 4.74e-84

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: 245.00  E-value: 4.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLGEADH 102
Cdd:COG2080     4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089 103 LNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRAdlPshvtkdltapiemTDAEICERMSGNLCRCGAYANILKAIKQ 182
Cdd:COG2080    84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPN--P-------------TEEEIREALSGNLCRCTGYVRIVRAVKR 148


                  ....*.
gi 2136496089 183 VAEARA 188
Cdd:COG2080   149 AAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
19-185 1.27e-48

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 155.34  E-value: 1.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  19 ERSNVSLVVNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLG 98
Cdd:NF041020    7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  99 EADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRadlpshvtkdltapiEMTDAEICERMSGNLCRCGAYANILK 178
Cdd:NF041020   87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENP---------------NPTEEEIRDGIHGNLCRCTGYQNIVK 151


                  ....*..
gi 2136496089 179 AIKQVAE 185
Cdd:NF041020  152 AVKEASQ 158
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
 23-188 8.85e-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: 146.05  E-value: 8.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLE-LDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVnGER---------INACLTLAVMHEGDDVA 92
Cdd:COG4630     1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVV-GELddgglryraVNACILFLPQLDGKALV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  93 TIEGLGEAD-HLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEevRADLPshvtkdltapiemTDAEICERMSGNLCRCG 171
Cdd:COG4630    80 TVEGLAGPDgALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYE--RGPAP-------------DRADIEDALSGNLCRCT 144

                         170
                  ....*....|....*..
gi 2136496089 172 AYANILKAIKQVAEARA 188
Cdd:COG4630   145 GYRPIIDAARAMAEAPA 161
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 27-185 1.66e-41

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: 136.90  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  27 VNGAKHQLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIEGLGEaDHLNPM 106
Cdd:TIGR03198   8 VNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NELDPC 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136496089 107 QQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADlpshvtkdltapiemTDAEICERMSGNLCRCGAYANILKAIKQVAE 185
Cdd:TIGR03198  87 QTAFLEEGGFQCGYCTPGMVVALKALFRETPQP---------------SDEDMEEGLSGNLCRCTGYGGIIRSACRIRR 150
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
16-181 3.13e-37

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 126.18  E-value: 3.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  16 NGAERSNVSLVVNGAKHQLELDNRTTLLDALREHlKLTGTKKGCDHGQCGACTVSVNGERINACLTLAVMHEGDDVATIE 95
Cdd:PRK09908    2 NHSETITIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  96 GLGEADHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEVRADlpshvtkdltapiEMTDAEICERMSGNLCRCGAYAN 175
Cdd:PRK09908   81 GEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREK-------------PLTITEIRRGLAGNLCRCTGYQM 147


                  ....*.
gi 2136496089 176 ILKAIK 181
Cdd:PRK09908  148 IVNTVL 153
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
 27-188 4.14e-36

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: 130.86  E-value: 4.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  27 VNGAKHQLE-LDNRTTLLDALREHLKLTGTKKGCDHGQCGACTVSV----NGERI-----NACLT-LAVMHeGDDVATIE 95
Cdd:TIGR02963   5 LNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKLryrsvNACIQfLPSLD-GKAVVTVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  96 GLGEAD-HLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEevRADLPShvtkdltapiemtDAEICERMSGNLCRCGAYA 174
Cdd:TIGR02963  84 DLRQPDgRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYK--NSPAPS-------------RADIEDALQGNLCRCTGYR 148

                         170
                  ....*....|....
gi 2136496089 175 NILKAIKQVAEARA 188
Cdd:TIGR02963 149 PILDAAEAAFDYPC 162
Fer2_2 pfam01799
[2Fe-2S] binding domain;
93-180 4.77e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 115.22  E-value: 4.77e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  93 TIEGLGEADHlNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEEvradlpshvtkdltAPIEMTDAEICERMSGNLCRCGA 172
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 2136496089 173 YANILKAI 180
Cdd:pfam01799  66 YRRIVDAV 73
PLN02906 PLN02906
xanthine dehydrogenase
 41-184 1.08e-27

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 109.02  E-value: 1.08e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   41 TLLDALREhLKLTGTKKGCDHGQCGACTV----------SVNGERINACLTLAVMHEGDDVATIEGLG-EADHLNPMQQA 109
Cdd:PLN02906     3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVmvshydrktgKCVHYAVNACLAPLYSVEGMHVITVEGIGnRRDGLHPVQEA 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2136496089  110 FLDHDAFQCGYCTPGQICSAKAVLEEVRadlpshvtkdlTAPiemTDAEICERMSGNLCRCGAYANILKAIKQVA 184
Cdd:PLN02906    82 LASMHGSQCGFCTPGFIMSMYALLRSSK-----------TPP---TEEQIEECLAGNLCRCTGYRPILDAFRVFA 142
PLN00192 PLN00192
aldehyde oxidase
 18-184 2.23e-26

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 105.18  E-value: 2.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   18 AERSNVSLVVNGAKHQLE-LDNRTTLLDALREHLKLTGTKKGCDHGQCGACTV----------SVNGERINACLTLAVMH 86
Cdd:PLN00192     1 SSNMSLVFAVNGERFELSsVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVllskydpvldQVEDFTVSSCLTLLCSV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   87 EGDDVATIEGLGEA-DHLNPMQQAFLDHDAFQCGYCTPG---QICSAKAVLEEVRADLPSHVTKDLTApiemTDAEicER 162
Cdd:PLN00192    81 NGCSITTSEGLGNSkDGFHPIHKRFAGFHASQCGFCTPGmciSLFSALVNADKTDRPEPPSGFSKLTV----VEAE--KA 154

                          170       180
                   ....*....|....*....|..
gi 2136496089  163 MSGNLCRCGAYANILKAIKQVA 184
Cdd:PLN00192   155 VSGNLCRCTGYRPIVDACKSFA 176
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 27-186 6.00e-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: 103.94  E-value: 6.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   27 VNGAKH-QLELDNRTTLLDALREHLKLTGTKKGCDHGQCGACTV----------SVNGERINACLTLAVMHEGDDVATIE 95
Cdd:TIGR02969    7 VNGRKVvEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVmisrynpstkSIRHHPVNACLTPICSLYGAAVTTVE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089   96 GLGEA-DHLNPMQQAFLDHDAFQCGYCTPGQICSAKAVLEevradlpSHVTKDLTapiEMTDAeicerMSGNLCRCGAYA 174
Cdd:TIGR02969   87 GIGSTrTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLR-------NHPEPTLD---QLTDA-----LGGNLCRCTGYR 151

                          170
                   ....*....|..
gi 2136496089  175 NILKAIKQVAEA 186
Cdd:TIGR02969  152 PIIDACKTFCKT 163
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
 23-187 1.44e-10

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 59.46  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLEL---DNRTTLLDALREHlkltgTKKGCDHGQ--CGACTVSVNGERINACLTLAVMHEGDDVATIEGL 97
Cdd:PRK09800    3 IHFTLNGAPQELTVnpgENVQKLLFNMGMH-----SVRNSDDGFgfAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  98 GEADHLNPMQQAFLDHDAFQCGYCTPgqicsAKAVleeVRADLPSHVtkdlTAPiemTDAEICERMSGNLCRCGAYANIL 177
Cdd:PRK09800   78 GKWNELSLVQQAMVDVGVVQSGYNDP-----AAAL---IITDLLDRI----AAP---TREEIDDALSGLFSRDAGWQQYY 142

                         170
                  ....*....|
gi 2136496089 178 KAIkQVAEAR 187
Cdd:PRK09800  143 QVI-ELAVAR 151
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 23-72 1.28e-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: 44.69  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2136496089  23 VSLVVNGAKHQLELDNRTTLLDALREHLKltGTKKGCDHGQCGACTVSVN 72
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAAREAGI--DIPYSCRAGACGTCKVEVV 48
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
32-116 2.75e-06

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 46.28  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2136496089  32 HQLELDNRTTLLDALR---EHLKLTGT-KKGCDHGQCGACTVSVNGERINACLTLA--VMHEGDDVATIEGLgeaDHLNP 105
Cdd:PRK12576   27 YKVKVDRFTQVTEALRrikEEQDPTLSyRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPM---DYFKV 103

                          90
                  ....*....|.
gi 2136496089 106 MQQAFLDHDAF 116
Cdd:PRK12576  104 VKDLIVDFDEF 114
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 32-97 5.12e-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: 40.68  E-value: 5.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2136496089  32 HQLELDNRTTLLDALrEHLK--LTGT---KKGCDHGQCGACTVSVNGERINACLTLaVMHEGDDVATIEGL 97
Cdd:pfam13085  21 YEVPYEEGMTVLDAL-NKIKeeQDPTlafRRSCREGICGSCAMNINGKPRLACKTL-IDDLLGQDITLEPL 89
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
25-72 3.24e-04

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 37.89  E-value: 3.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2136496089  25 LVVNGAKHQLEL-DNRTTLLDALREHLklTGTKKGCDHGQCGACTVSVN 72
Cdd:pfam00111   1 VTINGKGVTIEVpDGETTLLDAAEEAG--IDIPYSCRGGGCGTCAVKVL 47
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 32-95 1.39e-03

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 38.19  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2136496089  32 HQLELDNRTTLLDALrEHLKLTGT-----KKGCDHGQCGACTVSVNGERINACLTLavMHEGDDVATIE 95
Cdd:COG0479    23 YEVPVSPGMTVLDAL-DYIKEEQDptlafRRSCREGICGSCAMVINGRPRLACQTH--VRDLKDTITIE 88
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 59-97 3.73e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 37.29  E-value: 3.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2136496089  59 CDHGQCGACTVSVNGERINACltlavMHEGDDVATIEGL 97
Cdd:PRK06259   54 CRAGQCGSCAVTINGEPVLAC-----KTEVEDGMIIEPL 87
 
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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