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Conserved domains on  [gi|1134525100|gb|APX24909|]
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xanthine dehydrogenase YagT iron-sulfur-binding subunit [Salipiger 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
 1-194 3.04e-93

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: 270.88  E-value: 3.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   1 MSPPIDFRIRRRTLLQGGAAVAAFGAASNGNSAQAqsqSQDAAPAGSETTTVSLTVNGEQRELTVDNRVTLLDALREHMQ 80
Cdd:PRK11433    4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAA---SVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  81 LTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGTPQTMDPMQTAFVENDGFQCGYCTPGQIQSARK 160
Cdd:PRK11433   81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134525100 161 VIEEI-----------------------RERMSGNICRCGAYANILAAITQVAEDQA 194
Cdd:PRK11433  161 VLKEIkdgipshvtvdltaapeltadeiRERMSGNICRCGAYSNILEAIEDVAGEIA 217
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-194 3.04e-93

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 270.88  E-value: 3.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   1 MSPPIDFRIRRRTLLQGGAAVAAFGAASNGNSAQAqsqSQDAAPAGSETTTVSLTVNGEQRELTVDNRVTLLDALREHMQ 80
Cdd:PRK11433    4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAA---SVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  81 LTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGTPQTMDPMQTAFVENDGFQCGYCTPGQIQSARK 160
Cdd:PRK11433   81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134525100 161 VIEEI-----------------------RERMSGNICRCGAYANILAAITQVAEDQA 194
Cdd:PRK11433  161 VLKEIkdgipshvtvdltaapeltadeiRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 49-191 2.59e-78

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: 230.75  E-value: 2.59e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  49 TTTVSLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGT 128
Cdd:COG2080     1 MMMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134525100 129 PQTMDPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:COG2080    81 DGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLdenpnpteEEIREALSGNLCRCTGYVRIVRAVKRAAA 151
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
48-191 3.41e-46

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 149.56  E-value: 3.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  48 ETTTVSLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIG 127
Cdd:NF041020    7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134525100 128 TPQTMDPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:NF041020   87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLkenpnpteEEIRDGIHGNLCRCTGYQNIVKAVKEASQ 158
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 53-191 1.77e-39

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: 131.90  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  53 SLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGTpQTM 132
Cdd:TIGR03198   5 RFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NEL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134525100 133 DPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:TIGR03198  84 DPCQTAFLEEGGFQCGYCTPGMVVALKALFretpqpsdEDMEEGLSGNLCRCTGYGGIIRSACRIRR 150
Fer2_2 pfam01799
[2Fe-2S] binding domain;
122-186 1.76e-27

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 98.66  E-value: 1.76e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134525100 122 TIEGIGTPQTmDPMQTAFVENDGFQCGYCTPGQIQSARKVIE---------EIRERMSGNICRCGAYANILAAI 186
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLErnppppteaEIREALSGNLCRCTGYRRIVDAV 73
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 52-101 5.12e-07

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: 45.85  E-value: 5.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134525100  52 VSLTVNGEQRELTVDNRVTLLDALREhmQLTGTKKGCDHGQCGACTCTVN 101
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAARE--AGIDIPYSCRAGACGTCKVEVV 48
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-194 3.04e-93

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 270.88  E-value: 3.04e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   1 MSPPIDFRIRRRTLLQGGAAVAAFGAASNGNSAQAqsqSQDAAPAGSETTTVSLTVNGEQRELTVDNRVTLLDALREHMQ 80
Cdd:PRK11433    4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAA---SVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  81 LTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGTPQTMDPMQTAFVENDGFQCGYCTPGQIQSARK 160
Cdd:PRK11433   81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1134525100 161 VIEEI-----------------------RERMSGNICRCGAYANILAAITQVAEDQA 194
Cdd:PRK11433  161 VLKEIkdgipshvtvdltaapeltadeiRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 49-191 2.59e-78

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: 230.75  E-value: 2.59e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  49 TTTVSLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGT 128
Cdd:COG2080     1 MMMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1134525100 129 PQTMDPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:COG2080    81 DGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLdenpnpteEEIREALSGNLCRCTGYVRIVRAVKRAAA 151
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
48-191 3.41e-46

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 149.56  E-value: 3.41e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  48 ETTTVSLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIG 127
Cdd:NF041020    7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1134525100 128 TPQTMDPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:NF041020   87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLkenpnpteEEIRDGIHGNLCRCTGYQNIVKAVKEASQ 158
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 53-191 1.77e-39

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: 131.90  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  53 SLTVNGEQRELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETIEGIGTpQTM 132
Cdd:TIGR03198   5 RFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NEL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1134525100 133 DPMQTAFVENDGFQCGYCTPGQIQSARKVI--------EEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:TIGR03198  84 DPCQTAFLEEGGFQCGYCTPGMVVALKALFretpqpsdEDMEEGLSGNLCRCTGYGGIIRSACRIRR 150
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
 52-194 1.20e-36

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


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 132.57  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  52 VSLTVNGEQRELT-VDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVnGER---------INSCLSLAVMHDGDEVE 121
Cdd:COG4630     1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVV-GELddgglryraVNACILFLPQLDGKALV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100 122 TIEGIGTPQ-TMDPMQTAFVENDGFQCGYCTPGQI--------QSARKVIEEIRERMSGNICRCGAYANILAAITQVAED 192
Cdd:COG4630    80 TVEGLAGPDgALHPVQQAMVDHHGSQCGFCTPGFVmslfalyeRGPAPDRADIEDALSGNLCRCTGYRPIIDAARAMAEA 159


                  ..
gi 1134525100 193 QA 194
Cdd:COG4630   160 PA 161
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
44-186 1.98e-33

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 116.94  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  44 PAGSETTTVSLTVNGEQRELTVDNRVTLLDALREHmQLTGTKKGCDHGQCGACTCTVNGERINSCLSLAVMHDGDEVETI 123
Cdd:PRK09908    1 MNHSETITIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1134525100 124 EGIGTPQTMDPMQTAFVENDGFQCGYCTPGQIQSARKV----------IEEIRERMSGNICRCGAYANILAAI 186
Cdd:PRK09908   80 EGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMlakprekpltITEIRRGLAGNLCRCTGYQMIVNTV 152
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
 56-191 8.48e-33

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: 122.00  E-value: 8.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  56 VNGEQRELT-VDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTV----NGERI-----NSCLSLAVMHDGDEVETIEG 125
Cdd:TIGR02963   5 LNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKLryrsvNACIQFLPSLDGKAVVTVED 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1134525100 126 IGTPQ-TMDPMQTAFVENDGFQCGYCTPG--------QIQSARKVIEEIRERMSGNICRCGAYANILAAITQVAE 191
Cdd:TIGR02963  85 LRQPDgRLHPVQQAMVECHGSQCGFCTPGfvmslyalYKNSPAPSRADIEDALQGNLCRCTGYRPILDAAEAAFD 159
Fer2_2 pfam01799
[2Fe-2S] binding domain;
122-186 1.76e-27

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 98.66  E-value: 1.76e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1134525100 122 TIEGIGTPQTmDPMQTAFVENDGFQCGYCTPGQIQSARKVIE---------EIRERMSGNICRCGAYANILAAI 186
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLErnppppteaEIREALSGNLCRCTGYRRIVDAV 73
PLN02906 PLN02906
xanthine dehydrogenase
 70-185 2.35e-24

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 99.39  E-value: 2.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   70 TLLDALREhMQLTGTKKGCDHGQCGACTC----------TVNGERINSCLSLAVMHDGDEVETIEGIGTPQT-MDPMQTA 138
Cdd:PLN02906     3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVmvshydrktgKCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDgLHPVQEA 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1134525100  139 FVENDGFQCGYCTPGQIQSARKVI---------EEIRERMSGNICRCGAYANILAA 185
Cdd:PLN02906    82 LASMHGSQCGFCTPGFIMSMYALLrssktppteEQIEECLAGNLCRCTGYRPILDA 137
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 56-185 1.02e-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: 97.77  E-value: 1.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   56 VNGEQR-ELTVDNRVTLLDALREHMQLTGTKKGCDHGQCGACTCTVN-----GERI-----NSCLSLAVMHDGDEVETIE 124
Cdd:TIGR02969    7 VNGRKVvEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISrynpsTKSIrhhpvNACLTPICSLYGAAVTTVE 86

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  125 GIGTPQT-MDPMQTAFVENDGFQCGYCTPGQIQS--------ARKVIEEIRERMSGNICRCGAYANILAA 185
Cdd:TIGR02969   87 GIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSmyallrnhPEPTLDQLTDALGGNLCRCTGYRPIIDA 156
PLN00192 PLN00192
aldehyde oxidase
 47-192 7.42e-20

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 86.69  E-value: 7.42e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100   47 SETTTVSLTVNGEQREL-TVDNRVTLLDALREHMQLTGTKKGCDHGQCGAC----------TCTVNGERINSCLSLAVMH 115
Cdd:PLN00192     1 SSNMSLVFAVNGERFELsSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACvvllskydpvLDQVEDFTVSSCLTLLCSV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1134525100  116 DGDEVETIEGIG-TPQTMDPMQTAFVendGF---QCGYCTPG--------------------QIQSARKVIEEIRERMSG 171
Cdd:PLN00192    81 NGCSITTSEGLGnSKDGFHPIHKRFA---GFhasQCGFCTPGmcislfsalvnadktdrpepPSGFSKLTVVEAEKAVSG 157

                          170       180
                   ....*....|....*....|.
gi 1134525100  172 NICRCGAYANILAAITQVAED 192
Cdd:PLN00192   158 NLCRCTGYRPIVDACKSFAAD 178
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 52-101 5.12e-07

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: 45.85  E-value: 5.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1134525100  52 VSLTVNGEQRELTVDNRVTLLDALREhmQLTGTKKGCDHGQCGACTCTVN 101
Cdd:cd00207     1 VTINVPGSGVEVEVPEGETLLDAARE--AGIDIPYSCRAGACGTCKVEVV 48
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
54-121 1.02e-05

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 42.13  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1134525100  54 LTVNGEQRELTV-DNRVTLLDALREhmQLTGTKKGCDHGQCGACTCTVNGERINSCLSLavmHDGDEVE 121
Cdd:pfam00111   1 VTINGKGVTIEVpDGETTLLDAAEE--AGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSF---LEDDELA 64
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 49-100 4.66e-05

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 42.93  E-value: 4.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1134525100  49 TTTVSLTVNGEQRELTVDNRVTLLDAL-REHMQLTGtkkGCD-HGQCGACTCTV 100
Cdd:COG2871    32 SGEVKITINGDGKEIEVEEGQTLLDALlRQGIFLPS---ACGgGGTCGQCKVKV 82
Fdx COG0633
Ferredoxin [Energy production and conversion];
54-100 6.17e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 34.44  E-value: 6.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1134525100  54 LTVNGEQRELTVDNRVTLLDALREH-MQLTGtkkGCDHGQCGACTCTV 100
Cdd:COG0633     4 VTFIPEGHTVEVPAGESLLEAALRAgIDLPY---SCRSGACGTCHVRV 48
 
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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