|
Name |
Accession |
Description |
Interval |
E-value |
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
12-177 |
3.51e-87 |
|
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: 253.09 E-value: 3.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 12 ITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADGDD 91
Cdd:COG2080 4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 92 LHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQA 171
Cdd:COG2080 84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN-----------------PNP-TEEEIREALSGNLCRCTGYVRIVRA 145
|
....*.
gi 1863504267 172 VAHAAG 177
Cdd:COG2080 146 VKRAAA 151
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
2-177 |
8.87e-84 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 246.61 E-value: 8.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 2 APEPSPTSSAITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVT 81
Cdd:PRK11433 42 AATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 82 TVEGLADGDDLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHAAGWPSAVTPDVdpdATPAPLTPEEIRERLSGNLCR 161
Cdd:PRK11433 122 TIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDL---TAAPELTADEIRERMSGNICR 198
|
170
....*....|....*.
gi 1863504267 162 CGAYVSIVQAVAHAAG 177
Cdd:PRK11433 199 CGAYSNILEAIEDVAG 214
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
11-176 |
7.22e-53 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 166.51 E-value: 7.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 11 AITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADGD 90
Cdd:NF041020 10 KIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 91 DLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQ 170
Cdd:NF041020 90 KLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKEN-----------------PNP-TEEEIRDGIHGNLCRCTGYQNIVK 151
|
....*.
gi 1863504267 171 AVAHAA 176
Cdd:NF041020 152 AVKEAS 157
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
13-176 |
1.03e-42 |
|
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: 140.37 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 13 TLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADgDDL 92
Cdd:TIGR03198 5 RFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 93 HPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQAV 172
Cdd:TIGR03198 84 DPCQTAFLEEGGFQCGYCTPGMVVALKALFRET-----------------PQP-SDEDMEEGLSGNLCRCTGYGGIIRSA 145
|
....
gi 1863504267 173 AHAA 176
Cdd:TIGR03198 146 CRIR 149
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
82-172 |
5.76e-35 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 117.92 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 82 TVEGLADGDDlHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPLTPEEIRERLSGNLCR 161
Cdd:pfam01799 1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERN-----------------PPPPTEAEIREALSGNLCR 62
|
90
....*....|.
gi 1863504267 162 CGAYVSIVQAV 172
Cdd:pfam01799 63 CTGYRRIVDAV 73
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
12-79 |
1.55e-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: 44.31 E-value: 1.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863504267 12 ITLHINGEKHHLSVDHRTTLLDALRErLDLTgTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDRE 79
Cdd:cd00207 1 VTINVPGSGVEVEVPEGETLLDAARE-AGID-IPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAE 66
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
12-177 |
3.51e-87 |
|
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: 253.09 E-value: 3.51e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 12 ITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADGDD 91
Cdd:COG2080 4 ITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 92 LHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQA 171
Cdd:COG2080 84 LHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN-----------------PNP-TEEEIREALSGNLCRCTGYVRIVRA 145
|
....*.
gi 1863504267 172 VAHAAG 177
Cdd:COG2080 146 VKRAAA 151
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
2-177 |
8.87e-84 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 246.61 E-value: 8.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 2 APEPSPTSSAITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVT 81
Cdd:PRK11433 42 AATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 82 TVEGLADGDDLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHAAGWPSAVTPDVdpdATPAPLTPEEIRERLSGNLCR 161
Cdd:PRK11433 122 TIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDL---TAAPELTADEIRERMSGNICR 198
|
170
....*....|....*.
gi 1863504267 162 CGAYVSIVQAVAHAAG 177
Cdd:PRK11433 199 CGAYSNILEAIEDVAG 214
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
11-176 |
7.22e-53 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 166.51 E-value: 7.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 11 AITLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADGD 90
Cdd:NF041020 10 KIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 91 DLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQ 170
Cdd:NF041020 90 KLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKEN-----------------PNP-TEEEIRDGIHGNLCRCTGYQNIVK 151
|
....*.
gi 1863504267 171 AVAHAA 176
Cdd:NF041020 152 AVKEAS 157
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
12-191 |
2.30e-48 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 163.38 E-value: 2.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 12 ITLHINGEKHHLS-VDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRR--------VVSCLTLAVTAQDREVTT 82
Cdd:COG4630 1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVGELDdgglryraVNACILFLPQLDGKALVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 83 VEGLADGDD-LHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEhaagwpsavtpdvdpdatPAPLTPEEIRERLSGNLCR 161
Cdd:COG4630 81 VEGLAGPDGaLHPVQQAMVDHHGSQCGFCTPGFVMSLFALYER------------------GPAPDRADIEDALSGNLCR 142
|
170 180 190
....*....|....*....|....*....|
gi 1863504267 162 CGAYVSIVQAvAHAAGTHGRNPALTTEEGA 191
Cdd:COG4630 143 CTGYRPIIDA-ARAMAEAPAPDPFAADRAA 171
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
13-176 |
1.03e-42 |
|
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: 140.37 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 13 TLHINGEKHHLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADgDDL 92
Cdd:TIGR03198 5 RFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAE-NEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 93 HPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLCRCGAYVSIVQAV 172
Cdd:TIGR03198 84 DPCQTAFLEEGGFQCGYCTPGMVVALKALFRET-----------------PQP-SDEDMEEGLSGNLCRCTGYGGIIRSA 145
|
....
gi 1863504267 173 AHAA 176
Cdd:TIGR03198 146 CRIR 149
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
3-172 |
4.37e-39 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 131.19 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 3 PEPSPTSsAITLHINGEKHHLSVDHRTTLLDALRERlDLTGTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVTT 82
Cdd:PRK09908 1 MNHSETI-TIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 83 VEGLADGDDLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEhaagwpsavtpdvdpdATPAPLTPEEIRERLSGNLCRC 162
Cdd:PRK09908 79 LEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAK----------------PREKPLTITEIRRGLAGNLCRC 142
|
170
....*....|
gi 1863504267 163 GAYVSIVQAV 172
Cdd:PRK09908 143 TGYQMIVNTV 152
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
12-189 |
9.52e-38 |
|
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: 135.09 E-value: 9.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 12 ITLHINGEKHHLS-VDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDR---------RRVVSCLTLAVTAQDREVT 81
Cdd:TIGR02963 1 IRFFLNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVGElvdggklryRSVNACIQFLPSLDGKAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 82 TVEGLADGD-DLHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSGNLC 160
Cdd:TIGR02963 81 TVEDLRQPDgRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNS-----------------PAP-SRADIEDALQGNLC 142
|
170 180
....*....|....*....|....*....
gi 1863504267 161 RCGAYVSIVQAvAHAAGTHGRNPALTTEE 189
Cdd:TIGR02963 143 RCTGYRPILDA-AEAAFDYPCSDPLDADR 170
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
82-172 |
5.76e-35 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 117.92 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 82 TVEGLADGDDlHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPLTPEEIRERLSGNLCR 161
Cdd:pfam01799 1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERN-----------------PPPPTEAEIREALSGNLCR 62
|
90
....*....|.
gi 1863504267 162 CGAYVSIVQAV 172
Cdd:pfam01799 63 CTGYRRIVDAV 73
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
8-171 |
2.66e-32 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 122.13 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 8 TSSAITLHINGEKHHL-SVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVL----------VDRRRVVSCLTLAVTAQ 76
Cdd:PLN00192 2 SNMSLVFAVNGERFELsSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLlskydpvldqVEDFTVSSCLTLLCSVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 77 DREVTTVEGLADGDD-LHPVQQAFLDLDGYQCGYCTPGqICSAI--ALIEEHAAGWPsavtpdvDPDATPAPLTPEEIRE 153
Cdd:PLN00192 82 GCSITTSEGLGNSKDgFHPIHKRFAGFHASQCGFCTPG-MCISLfsALVNADKTDRP-------EPPSGFSKLTVVEAEK 153
|
170
....*....|....*...
gi 1863504267 154 RLSGNLCRCGAYVSIVQA 171
Cdd:PLN00192 154 AVSGNLCRCTGYRPIVDA 171
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
30-171 |
2.19e-30 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 116.72 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 30 TLLDALRErLDLTGTKKGCDQGQCGACTVLV---DR-------RRVVSCLTLAVTAQDREVTTVEGLADGDD-LHPVQQA 98
Cdd:PLN02906 3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMVshyDRktgkcvhYAVNACLAPLYSVEGMHVITVEGIGNRRDgLHPVQEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863504267 99 FLDLDGYQCGYCTPGQICSAIALIEehaagwpsavtpdvdpdATPAPLTPEEIRERLSGNLCRCGAYVSIVQA 171
Cdd:PLN02906 82 LASMHGSQCGFCTPGFIMSMYALLR-----------------SSKTPPTEEQIEECLAGNLCRCTGYRPILDA 137
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
10-171 |
6.24e-30 |
|
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: 115.49 E-value: 6.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 10 SAITLHINGEKH-HLSVDHRTTLLDALRERLDLTGTKKGCDQGQCGACTVLVDRRR----------VVSCLTLAVTAQDR 78
Cdd:TIGR02969 1 PELLFYVNGRKVvEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNpstksirhhpVNACLTPICSLYGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 79 EVTTVEGLADGDD-LHPVQQAFLDLDGYQCGYCTPGQICSAIALIEEHaagwpsavtpdvdpdatPAPlTPEEIRERLSG 157
Cdd:TIGR02969 81 AVTTVEGIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNH-----------------PEP-TLDQLTDALGG 142
|
170
....*....|....
gi 1863504267 158 NLCRCGAYVSIVQA 171
Cdd:TIGR02969 143 NLCRCTGYRPIIDA 156
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
51-188 |
2.32e-08 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 52.91 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 51 GQCGACTVLVDRRRVVSCLTLAVTAQDREVTTVEGLADGDDLHPVQQAFLDLDGYQCGYCTPgqicsAIALIeehaagwp 130
Cdd:PRK09800 42 GFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKWNELSLVQQAMVDVGVVQSGYNDP-----AAALI-------- 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1863504267 131 saVTPDVDPDATPaplTPEEIRERLSGNLCRCGAYVSIVQAVAHAAgTHGRNPALTTE 188
Cdd:PRK09800 109 --ITDLLDRIAAP---TREEIDDALSGLFSRDAGWQQYYQVIELAV-ARKNNPQATID 160
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
12-79 |
1.55e-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: 44.31 E-value: 1.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863504267 12 ITLHINGEKHHLSVDHRTTLLDALRErLDLTgTKKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDRE 79
Cdd:cd00207 1 VTINVPGSGVEVEVPEGETLLDAARE-AGID-IPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAE 66
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| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
19-173 |
2.67e-06 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 46.28 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 19 EKHHLSVDHRTTLLDALR---ERLDLTGT-KKGCDQGQCGACTVLVDRRRVVSCLTLA--VTAQDREVTTVEGLadgDDL 92
Cdd:PRK12576 25 QEYKVKVDRFTQVTEALRrikEEQDPTLSyRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPM---DYF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863504267 93 HPVQQAFLDLDGYQcgyctpgqicsaialiEEHAAGWPSAVTPD--VDPDATPaPLTPEEIRERLSGNLC-RCGAYVSIV 169
Cdd:PRK12576 102 KVVKDLIVDFDEFY----------------ERMFKVKPRLYRAKevLEGKAEH-RLKPEDQKELWKFAQCiWCGLCVSAC 164
|
....
gi 1863504267 170 QAVA 173
Cdd:PRK12576 165 PVVA 168
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
14-61 |
1.92e-05 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 41.36 E-value: 1.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1863504267 14 LHINGEKHHLSV-DHRTTLLDALRErlDLTGTKKGCDQGQCGACTVLVD 61
Cdd:pfam00111 1 VTINGKGVTIEVpDGETTLLDAAEE--AGIDIPYSCRGGGCGTCAVKVL 47
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
19-81 |
2.38e-04 |
|
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: 38.76 E-value: 2.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863504267 19 EKHHLSVDHRTTLLDAL---RERLDLTGT-KKGCDQGQCGACTVLVDRRRVVSCLTLAVTAQDREVT 81
Cdd:pfam13085 19 QEYEVPYEEGMTVLDALnkiKEEQDPTLAfRRSCREGICGSCAMNINGKPRLACKTLIDDLLGQDIT 85
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