|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
1-165 |
2.58e-91 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 267.02 E-value: 2.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 1 MSTLTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIG 80
Cdd:PRK11433 49 ISPVTLKVNGKTEQLE-VDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 81 LPESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQNWPSHVTTDLQNPDGLLVQEIAERMSGNICRCSAYPNIIK 160
Cdd:PRK11433 128 SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILE 207
|
....*
gi 1002778021 161 AISQV 165
Cdd:PRK11433 208 AIEDV 212
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
1-167 |
2.10e-83 |
|
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: 244.62 E-value: 2.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 1 MSTLTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIG 80
Cdd:COG2080 1 MMMITLTVNGKPVEVD-VDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 81 LPESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKqnwpshvttdlqNPDgllVQEIAERMSGNICRCSAYPNIIK 160
Cdd:COG2080 80 EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENP------------NPT---EEEIREALSGNLCRCTGYVRIVR 144
|
....*..
gi 1002778021 161 AISQVLE 167
Cdd:COG2080 145 AVKRAAA 151
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
4-162 |
1.03e-48 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 156.88 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 4 LTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIGLPE 83
Cdd:NF041020 11 IRVKVNGVWYEAE-VEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDG 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002778021 84 SLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQnwPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPNIIKAI 162
Cdd:NF041020 90 KLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPN--PTE-------------EEIRDGIHGNLCRCTGYQNIVKAV 153
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
4-165 |
1.76e-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: 133.05 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 4 LTLTINKQDYQLDNlDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIGlPE 83
Cdd:TIGR03198 4 FRFTVNGQAWEVAA-VPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIA-EN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 84 SLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQnwPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPNIIKAIS 163
Cdd:TIGR03198 82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQ--PSD-------------EDMEEGLSGNLCRCTGYGGIIRSAC 146
|
..
gi 1002778021 164 QV 165
Cdd:TIGR03198 147 RI 148
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
75-162 |
8.12e-32 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 110.60 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 75 TIEGIGLPESLsELQQAFKDHDAFQCGYCTPGQICSATALIEEvkqnwpshvttdlqNPDGLLVQEIAERMSGNICRCSA 154
Cdd:pfam01799 1 TIEGLAESGGE-PVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65
|
....*...
gi 1002778021 155 YPNIIKAI 162
Cdd:pfam01799 66 YRRIVDAV 73
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
4-59 |
1.90e-05 |
|
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: 41.61 E-value: 1.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002778021 4 LTLTINKQDYQLDnLDPRTTLLDVCRQHlQITGPKkGCDHGQCGACTILINGERVN 59
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAAREA-GIDIPY-SCRAGACGTCKVEVVEGEVD 53
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
1-165 |
2.58e-91 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 267.02 E-value: 2.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 1 MSTLTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIG 80
Cdd:PRK11433 49 ISPVTLKVNGKTEQLE-VDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 81 LPESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQNWPSHVTTDLQNPDGLLVQEIAERMSGNICRCSAYPNIIK 160
Cdd:PRK11433 128 SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILE 207
|
....*
gi 1002778021 161 AISQV 165
Cdd:PRK11433 208 AIEDV 212
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
1-167 |
2.10e-83 |
|
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: 244.62 E-value: 2.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 1 MSTLTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIG 80
Cdd:COG2080 1 MMMITLTVNGKPVEVD-VDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 81 LPESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKqnwpshvttdlqNPDgllVQEIAERMSGNICRCSAYPNIIK 160
Cdd:COG2080 80 EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENP------------NPT---EEEIREALSGNLCRCTGYVRIVR 144
|
....*..
gi 1002778021 161 AISQVLE 167
Cdd:COG2080 145 AVKRAAA 151
|
|
| glyceraldDH_gamma |
NF041020 |
glyceraldehyde dehydrogenase subunit gamma; |
4-162 |
1.03e-48 |
|
glyceraldehyde dehydrogenase subunit gamma;
Pssm-ID: 468949 [Multi-domain] Cd Length: 162 Bit Score: 156.88 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 4 LTLTINKQDYQLDnLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIGLPE 83
Cdd:NF041020 11 IRVKVNGVWYEAE-VEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDG 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002778021 84 SLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQnwPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPNIIKAI 162
Cdd:NF041020 90 KLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPN--PTE-------------EEIRDGIHGNLCRCTGYQNIVKAV 153
|
|
| pucE |
TIGR03198 |
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ... |
4-165 |
1.76e-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: 133.05 E-value: 1.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 4 LTLTINKQDYQLDNlDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIGlPE 83
Cdd:TIGR03198 4 FRFTVNGQAWEVAA-VPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIA-EN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 84 SLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQnwPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPNIIKAIS 163
Cdd:TIGR03198 82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQ--PSD-------------EDMEEGLSGNLCRCTGYGGIIRSAC 146
|
..
gi 1002778021 164 QV 165
Cdd:TIGR03198 147 RI 148
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
4-173 |
2.29e-38 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 137.96 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 4 LTLTINKQDYQLDNLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILInGER---------VNSCLTLAVMHDGDEIT 74
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVV-GELddgglryraVNACILFLPQLDGKALV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 75 TIEGIGLPE-SLSELQQAFKDHDAFQCGYCTPGQICSATALieevkqnWpshvttdlQNPDGLLVQEIAERMSGNICRCS 153
Cdd:COG4630 80 TVEGLAGPDgALHPVQQAMVDHHGSQCGFCTPGFVMSLFAL-------Y--------ERGPAPDRADIEDALSGNLCRCT 144
|
170 180
....*....|....*....|
gi 1002778021 154 AYPNIIKAISQVLENQIADK 173
Cdd:COG4630 145 GYRPIIDAARAMAEAPAPDP 164
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
3-162 |
6.11e-36 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 124.26 E-value: 6.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 3 TLTLTINKQDYQLdNLDPRTTLLDVCRQHlQITGPKKGCDHGQCGACTILINGERVNSCLTLAVMHDGDEITTIEGIGLP 82
Cdd:PRK09908 8 TIECTINGMPFQL-HAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 83 ESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQNWPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPNIIKAI 162
Cdd:PRK09908 86 GKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKPLTI-------------TEIRRGLAGNLCRCTGYQMIVNTV 152
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
9-173 |
2.43e-32 |
|
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: 121.61 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 9 NKQDYQLDNLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILI----NGER-----VNSCLTLAVMHDGDEITTIEGI 79
Cdd:TIGR02963 6 NGETVTLSDVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKlryrsVNACIQFLPSLDGKAVVTVEDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 80 GLPES-LSELQQAFKDHDAFQCGYCTPGQICSATALieevkqnWPSHvttdlQNPDgllVQEIAERMSGNICRCSAYPNI 158
Cdd:TIGR02963 86 RQPDGrLHPVQQAMVECHGSQCGFCTPGFVMSLYAL-------YKNS-----PAPS---RADIEDALQGNLCRCTGYRPI 150
|
170
....*....|....*
gi 1002778021 159 IKAISQVLENQIADK 173
Cdd:TIGR02963 151 LDAAEAAFDYPCSDP 165
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
75-162 |
8.12e-32 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 110.60 E-value: 8.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 75 TIEGIGLPESLsELQQAFKDHDAFQCGYCTPGQICSATALIEEvkqnwpshvttdlqNPDGLLVQEIAERMSGNICRCSA 154
Cdd:pfam01799 1 TIEGLAESGGE-PVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65
|
....*...
gi 1002778021 155 YPNIIKAI 162
Cdd:pfam01799 66 YRRIVDAV 73
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
2-161 |
3.94e-27 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 108.26 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 2 STLTLTINKQDYQLDNLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGE----------RVNSCLTLAVMHDGD 71
Cdd:PLN00192 4 MSLVFAVNGERFELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLSKYdpvldqvedfTVSSCLTLLCSVNGC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 72 EITTIEGIG-LPESLSELQQAFKDHDAFQCGYCTPGQICS-ATALIEEVKQNWPShvttdlqNPDG---LLVQEiAER-M 145
Cdd:PLN00192 84 SITTSEGLGnSKDGFHPIHKRFAGFHASQCGFCTPGMCISlFSALVNADKTDRPE-------PPSGfskLTVVE-AEKaV 155
|
170
....*....|....*.
gi 1002778021 146 SGNICRCSAYPNIIKA 161
Cdd:PLN00192 156 SGNLCRCTGYRPIVDA 171
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
2-161 |
5.70e-25 |
|
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: 102.40 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 2 STLTLTINKQDYQLDNLDPRTTLLDVCRQHLQITGPKKGCDHGQCGACTILINGER----------VNSCLTLAVMHDGD 71
Cdd:TIGR02969 1 PELLFYVNGRKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYNpstksirhhpVNACLTPICSLYGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 72 EITTIEGIGLPES-LSELQQAFKDHDAFQCGYCTPGQICSATALIEevkqnwpshvttdlQNPDGLLVQeIAERMSGNIC 150
Cdd:TIGR02969 81 AVTTVEGIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSMYALLR--------------NHPEPTLDQ-LTDALGGNLC 145
|
170
....*....|.
gi 1002778021 151 RCSAYPNIIKA 161
Cdd:TIGR02969 146 RCTGYRPIIDA 156
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
23-161 |
1.52e-21 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 92.45 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 23 TLLDVCRQhLQITGPKKGCDHGQCGACTIL----------INGERVNSCLTLAVMHDGDEITTIEGIGLPES-LSELQQA 91
Cdd:PLN02906 3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMvshydrktgkCVHYAVNACLAPLYSVEGMHVITVEGIGNRRDgLHPVQEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 92 FKDHDAFQCGYCTPGQICSATALIEEVKQNwPShvttdlqnpdgllVQEIAERMSGNICRCSAYPNIIKA 161
Cdd:PLN02906 82 LASMHGSQCGFCTPGFIMSMYALLRSSKTP-PT-------------EEQIEECLAGNLCRCTGYRPILDA 137
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
3-162 |
1.54e-06 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 48.29 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 3 TLTLTINKQDYQL-----DNLDprtTLLDVCRQHlQITGPKKGcdHGQCGACTILINGERVNSCLTLAVMHDGDEITTIE 77
Cdd:PRK09800 2 IIHFTLNGAPQELtvnpgENVQ---KLLFNMGMH-SVRNSDDG--FGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 78 GIGLPESLSELQQAFKDHDAFQCGYCTPGQICSATALIEEVKQnwPSHvttdlqnpdgllvQEIAERMSGNICRCSAYPN 157
Cdd:PRK09800 76 SLGKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAA--PTR-------------EEIDDALSGLFSRDAGWQQ 140
|
....*
gi 1002778021 158 IIKAI 162
Cdd:PRK09800 141 YYQVI 145
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
4-59 |
1.90e-05 |
|
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: 41.61 E-value: 1.90e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002778021 4 LTLTINKQDYQLDnLDPRTTLLDVCRQHlQITGPKkGCDHGQCGACTILINGERVN 59
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAAREA-GIDIPY-SCRAGACGTCKVEVVEGEVD 53
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
11-77 |
3.50e-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: 41.45 E-value: 3.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002778021 11 QDYQLDNlDPRTTLLDvCRQHL--QITGP---KKGCDHGQCGACTILINGERVNSCLTLaVMHDGDEITTIE 77
Cdd:pfam13085 19 QEYEVPY-EEGMTVLD-ALNKIkeEQDPTlafRRSCREGICGSCAMNINGKPRLACKTL-IDDLLGQDITLE 87
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
6-63 |
1.90e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 38.66 E-value: 1.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002778021 6 LTINKQDYQLDNLDPRTTLLDVCRQHLqiTGPKKGCDHGQCGACTILINGERVNSCLT 63
Cdd:pfam00111 1 VTINGKGVTIEVPDGETTLLDAAEEAG--IDIPYSCRGGGCGTCAVKVLEGEDQSDQS 56
|
|
| SdhB/FrdB |
COG0479 |
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ... |
11-77 |
8.61e-04 |
|
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: 38.96 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002778021 11 QDYQLDnLDPRTTLLDVCRQ-HLQITGP---KKGCDHGQCGACTILINGERVNSCLTLavMHD-GDEItTIE 77
Cdd:COG0479 21 QTYEVP-VSPGMTVLDALDYiKEEQDPTlafRRSCREGICGSCAMVINGRPRLACQTH--VRDlKDTI-TIE 88
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
1-82 |
1.38e-03 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 39.22 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 1 MSTLTLTINKQDYQLD---------NLDPRTTLLDVCRQHLQITGP----KKGCDHGQCGACTILINGERVNSCLTLAvm 67
Cdd:PRK06259 1 MKMITITVKRFDPEKDephfesyevPVKEGMTVLDALEYINKTYDAniafRSSCRAGQCGSCAVTINGEPVLACKTEV-- 78
|
90
....*....|....*
gi 1002778021 68 HDGDeitTIEGIGLP 82
Cdd:PRK06259 79 EDGM---IIEPLDFP 90
|
|
| sdhB |
PRK05950 |
succinate dehydrogenase iron-sulfur subunit; Reviewed |
11-82 |
3.23e-03 |
|
succinate dehydrogenase iron-sulfur subunit; Reviewed
Pssm-ID: 235652 [Multi-domain] Cd Length: 232 Bit Score: 37.47 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002778021 11 QDYQLDNLDPRTTLLDVCrqhLQITGPKKG-------CDHGQCGACTILINGERVNSCLTLavMHD--GDEItTIEGI-G 80
Cdd:PRK05950 18 QTYEVDVDECGPMVLDAL---IKIKNEIDPtltfrrsCREGVCGSDAMNINGKNGLACITP--ISDlkKGKI-VIRPLpG 91
|
..
gi 1002778021 81 LP 82
Cdd:PRK05950 92 LP 93
|
|
| PRK12576 |
PRK12576 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
11-77 |
5.31e-03 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 237143 [Multi-domain] Cd Length: 279 Bit Score: 37.04 E-value: 5.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002778021 11 QDYQLDnLDPRTTLLDVCRQHLQITGP----KKGCDHGQCGACTILINGERVNSCLTLA--VMHDGDEITTIE 77
Cdd:PRK12576 25 QEYKVK-VDRFTQVTEALRRIKEEQDPtlsyRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIE 96
|
|
|