|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
6-490 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 766.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVENIVPTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGELVNDNLQLRSVNACIQFLPTLDG 85
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLRE-----DRGLTGTKEGCAEGDCGACTVVVGELDDGGLRYRAVNACILFLPQLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 86 KALFTVEDLHSllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQsLSKDKISDYLSGNLCRCTGYRPIL 165
Cdd:COG4630 76 KALVTVEGLAG----PDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPA-PDRADIEDALSGNLCRCTGYRPII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 166 DAAQKAYDYP---RVVLERQKVIDVLKEIRTLPALYLNDQKQQFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQG 242
Cdd:COG4630 151 DAARAMAEAPapdPFAADRAAVAAALRALADGETVELGAGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 243 RDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIKISDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMP 322
Cdd:COG4630 231 RDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 323 ALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVEAIVIPLREGQTRFKFasYKIAKRFEQDISAVCAAISCEL 402
Cdd:COG4630 311 ALIALGAELVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRA--YKVSKRFDDDISAVCAAFALTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 403 DNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKRFYLEKI 482
Cdd:COG4630 389 DDGTVTE-ARIAFGGMAATPKRARAAEAALLGQPWTEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQ 467
|
....*...
gi 940328420 483 LSQTLTRV 490
Cdd:COG4630 468 GEAPATRV 475
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
6-480 |
0e+00 |
|
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: 722.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVENIVPTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGELVNDN-LQLRSVNACIQFLPTLD 84
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLRE-----DAGLTGTKEGCAEGDCGACTVVVGELVDGGkLRYRSVNACIQFLPSLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 85 GKALFTVEDLHSllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSlSKDKISDYLSGNLCRCTGYRPI 164
Cdd:TIGR02963 76 GKAVVTVEDLRQ----PDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAP-SRADIEDALQGNLCRCTGYRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 165 LDAAQKAYDYP---RVVLERQKVIDVLKEIRTLPALYLNDQKQQFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQ 241
Cdd:TIGR02963 151 LDAAEAAFDYPcsdPLDADRAPIIERLRALRAGETVELNFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 242 GRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIKISDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSM 321
Cdd:TIGR02963 231 MRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 322 PALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVEAIVIPLREGQTRfkFASYKIAKRFEQDISAVCAAISCE 401
Cdd:TIGR02963 311 PALIALGARLTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGER--FRAYKISKRFDDDISAVCAAFNLE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940328420 402 LDNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKRFYLE 480
Cdd:TIGR02963 389 LDGGVVAE-IRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGDFTPLSDMRASAEYRLLTAKNLLRRFFLE 466
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
24-479 |
3.03e-81 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 275.04 E-value: 3.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 24 MTVLQFLREytqtgkTRQTGTKEGCAEGDCGACTVVIG--ELVNDNLQLRSVNACIQFLPTLDGKALFTVEDLHSllpVQ 101
Cdd:PLN02906 2 QTLLEYLRD------LGLTGTKLGCGEGGCGACTVMVShyDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGN---RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 102 DGtLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSLSKDKISDYLSGNLCRCTGYRPILDAAQ---KAYD---YP 175
Cdd:PLN02906 73 DG-LHPVQEALASMHGSQCGFCTPGFIMSMYALLRSSKTPPTEEQIEECLAGNLCRCTGYRPILDAFRvfaKTDDalyTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 176 RVVLERQK--------------------VIDVLKEIRTLPALYLN------DQKQQFFAPK------------------- 210
Cdd:PLN02906 152 VSSLSLQDgepicpstgkpcscgskttsAAGTCKSDRFQPISYSEidgswyTEKELIFPPElllrkltplkllgnggltw 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 211 ----TLQDFATLRLQLPQARIVAGSTDVGLWVTkqgrdLGDMLY-----IGQVEELKKIVVTDLALTIGANVSLS----- 276
Cdd:PLN02906 232 yrptSLQHLLELKAEYPDAKLVVGNTEVGIEMR-----FKNAQYpvlisPTHVPELNAIKVKDDGLEIGAAVRLSelqnl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 277 -DALIKISDFYPD-----FQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRL-ILRVGKQTREIALEDFYL 349
Cdd:PLN02906 307 fRKVVKERPAHETsackaFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFvIISCDGDIRSVPASDFFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 350 DYQKTALQLGEFVEAIVIPLregqTR-FKFA-SYKIAKRFEQDISAVCAAISCEL---DNDDVTHNVRIAFGGMAAIPKR 424
Cdd:PLN02906 387 GYRKVDLKPDEILLSVFLPW----TRpFEYVkEFKQAHRRDDDIAIVNAGMRVKLeekDGEWIVSDASIAYGGVAPLSVS 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 940328420 425 AKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRAS-SAYRLHVAKNCLKRFYL 479
Cdd:PLN02906 463 ARKTEEFLIGKPWNKETLQDALKVLQKDILIKEDAPGGmVEFRKSLALSFFFKFFL 518
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
205-369 |
6.85e-61 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 197.00 E-value: 6.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 205 QFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQGRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIK-IS 283
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPlLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 284 DFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVE 363
Cdd:pfam00941 84 EAYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELIT 163
|
....*.
gi 940328420 364 AIVIPL 369
Cdd:pfam00941 164 AVIIPL 169
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
380-480 |
7.42e-32 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 117.72 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 380 SYKIAKRFEQDISAVCAAISCELDNDDVThNVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQ-AQQALSQDYQPLDD 458
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDGGRVT-EARIALGGVAPTPKRAAEAEAALVGKPLTDEALARaAAAALAQDFTPLSD 79
|
90 100
....*....|....*....|..
gi 940328420 459 GRASSAYRLHVAKNCLKRFYLE 480
Cdd:smart01092 80 MRASAEYRRQLAANLLRRALLE 101
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
6-77 |
1.94e-03 |
|
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: 37.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVEnIVPTMTVLQFLREytqTGKTrqtgTKEGCAEGDCGACTV-VIGELVNDNLQL---------RSVNA 75
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAARE---AGID----IPYSCRAGACGTCKVeVVEGEVDQSDPSlldeeeaegGYVLA 72
|
..
gi 940328420 76 CI 77
Cdd:cd00207 73 CQ 74
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
6-490 |
0e+00 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 766.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVENIVPTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGELVNDNLQLRSVNACIQFLPTLDG 85
Cdd:COG4630 1 IRFLLNGELVELSDVPPTTTLLDWLRE-----DRGLTGTKEGCAEGDCGACTVVVGELDDGGLRYRAVNACILFLPQLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 86 KALFTVEDLHSllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQsLSKDKISDYLSGNLCRCTGYRPIL 165
Cdd:COG4630 76 KALVTVEGLAG----PDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPA-PDRADIEDALSGNLCRCTGYRPII 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 166 DAAQKAYDYP---RVVLERQKVIDVLKEIRTLPALYLNDQKQQFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQG 242
Cdd:COG4630 151 DAARAMAEAPapdPFAADRAAVAAALRALADGETVELGAGGSRFLAPATLDELAALLAAHPDARLVAGATDVGLWVTKQL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 243 RDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIKISDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMP 322
Cdd:COG4630 231 RDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAAHFPELAELLRRFASRQIRNAGTLGGNIANGSPIGDSPP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 323 ALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVEAIVIPLREGQTRFKFasYKIAKRFEQDISAVCAAISCEL 402
Cdd:COG4630 311 ALIALGAELVLRSGDGRRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRA--YKVSKRFDDDISAVCAAFALTL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 403 DNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKRFYLEKI 482
Cdd:COG4630 389 DDGTVTE-ARIAFGGMAATPKRARAAEAALLGQPWTEATVAAAAAALAQDFTPLSDMRASAEYRLAVAANLLRRFFLETQ 467
|
....*...
gi 940328420 483 LSQTLTRV 490
Cdd:COG4630 468 GEAPATRV 475
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
6-480 |
0e+00 |
|
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: 722.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVENIVPTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGELVNDN-LQLRSVNACIQFLPTLD 84
Cdd:TIGR02963 1 IRFFLNGETVTLSDVDPTRTLLDYLRE-----DAGLTGTKEGCAEGDCGACTVVVGELVDGGkLRYRSVNACIQFLPSLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 85 GKALFTVEDLHSllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSlSKDKISDYLSGNLCRCTGYRPI 164
Cdd:TIGR02963 76 GKAVVTVEDLRQ----PDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAP-SRADIEDALQGNLCRCTGYRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 165 LDAAQKAYDYP---RVVLERQKVIDVLKEIRTLPALYLNDQKQQFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQ 241
Cdd:TIGR02963 151 LDAAEAAFDYPcsdPLDADRAPIIERLRALRAGETVELNFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVGLWVTKQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 242 GRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIKISDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSM 321
Cdd:TIGR02963 231 MRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPELGELLRRFASLQIRNAGTLGGNIANGSPIGDSP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 322 PALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVEAIVIPLREGQTRfkFASYKIAKRFEQDISAVCAAISCE 401
Cdd:TIGR02963 311 PALIALGARLTLRKGEGRRTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGER--FRAYKISKRFDDDISAVCAAFNLE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940328420 402 LDNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKRFYLE 480
Cdd:TIGR02963 389 LDGGVVAE-IRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMAALAGDFTPLSDMRASAEYRLLTAKNLLRRFFLE 466
|
|
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
24-479 |
3.03e-81 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 275.04 E-value: 3.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 24 MTVLQFLREytqtgkTRQTGTKEGCAEGDCGACTVVIG--ELVNDNLQLRSVNACIQFLPTLDGKALFTVEDLHSllpVQ 101
Cdd:PLN02906 2 QTLLEYLRD------LGLTGTKLGCGEGGCGACTVMVShyDRKTGKCVHYAVNACLAPLYSVEGMHVITVEGIGN---RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 102 DGtLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSLSKDKISDYLSGNLCRCTGYRPILDAAQ---KAYD---YP 175
Cdd:PLN02906 73 DG-LHPVQEALASMHGSQCGFCTPGFIMSMYALLRSSKTPPTEEQIEECLAGNLCRCTGYRPILDAFRvfaKTDDalyTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 176 RVVLERQK--------------------VIDVLKEIRTLPALYLN------DQKQQFFAPK------------------- 210
Cdd:PLN02906 152 VSSLSLQDgepicpstgkpcscgskttsAAGTCKSDRFQPISYSEidgswyTEKELIFPPElllrkltplkllgnggltw 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 211 ----TLQDFATLRLQLPQARIVAGSTDVGLWVTkqgrdLGDMLY-----IGQVEELKKIVVTDLALTIGANVSLS----- 276
Cdd:PLN02906 232 yrptSLQHLLELKAEYPDAKLVVGNTEVGIEMR-----FKNAQYpvlisPTHVPELNAIKVKDDGLEIGAAVRLSelqnl 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 277 -DALIKISDFYPD-----FQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRL-ILRVGKQTREIALEDFYL 349
Cdd:PLN02906 307 fRKVVKERPAHETsackaFIEQLKWFAGTQIRNVASIGGNICTASPISDLNPLWMAAGATFvIISCDGDIRSVPASDFFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 350 DYQKTALQLGEFVEAIVIPLregqTR-FKFA-SYKIAKRFEQDISAVCAAISCEL---DNDDVTHNVRIAFGGMAAIPKR 424
Cdd:PLN02906 387 GYRKVDLKPDEILLSVFLPW----TRpFEYVkEFKQAHRRDDDIAIVNAGMRVKLeekDGEWIVSDASIAYGGVAPLSVS 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 940328420 425 AKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRAS-SAYRLHVAKNCLKRFYL 479
Cdd:PLN02906 463 ARKTEEFLIGKPWNKETLQDALKVLQKDILIKEDAPGGmVEFRKSLALSFFFKFFL 518
|
|
| CutB |
COG1319 |
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ... |
205-476 |
2.37e-65 |
|
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440930 [Multi-domain] Cd Length: 285 Bit Score: 212.68 E-value: 2.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 205 QFFAPKTLQD-FATLRLQLPQARIVAGSTDVGLWVtKQGRDLGDML-YIGQVEELKKIVVTDLALTIGANVSLSD----A 278
Cdd:COG1319 5 EYHRPTSLEEaLALLAEHGPDARVLAGGTDLLPLM-KLRLARPEHLvDINRIPELRGIEEEGGGLRIGALVTHAElaasP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 279 LIKisDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRLILRVGKQTREIALEDFYLDYQKTALQL 358
Cdd:COG1319 84 LVR--ERYPLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELAGPDGERTIPAADFFLGPGETALEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 359 GEFVEAIVIPLREGQTRFKFasYKIAKRFEQDISAVCAAISCELDNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQIT 438
Cdd:COG1319 162 GELITAVRLPAPPAGAGSAY--LKVGRRASDAIALVSVAVALRLDGGTIRD-ARIALGGVAPTPWRAREAEAALAGKPLS 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 940328420 439 AELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKR 476
Cdd:COG1319 239 EEAIEAAAEAAAAAADPIDDVRASAEYRRHLARVLVRR 276
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
205-369 |
6.85e-61 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 197.00 E-value: 6.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 205 QFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQGRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLSDALIK-IS 283
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPlLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 284 DFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRLILRVGKQTREIALEDFYLDYQKTALQLGEFVE 363
Cdd:pfam00941 84 EAYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEGERTVPLEDFFLGYGKTALEPGELIT 163
|
....*.
gi 940328420 364 AIVIPL 369
Cdd:pfam00941 164 AVIIPL 169
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
5-491 |
1.36e-50 |
|
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: 186.37 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 5 PITFFFRGGQQQVENIV-PTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGEL--VNDNLQLRSVNACIQFLP 81
Cdd:TIGR02969 1 PELLFYVNGRKVVEKNVdPETMLLPYLRK-----KLRLTGTKYGCGGGGCGACTVMISRYnpSTKSIRHHPVNACLTPIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 82 TLDGKALFTVEDLHSllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSlSKDKISDYLSGNLCRCTGY 161
Cdd:TIGR02969 76 SLYGAAVTTVEGIGS----TRTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEP-TLDQLTDALGGNLCRCTGY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 162 RPILDAAQ---KAYD----------------------------YPRVVLERQKV-IDVLKEIRTLPALYLNDQKQ----- 204
Cdd:TIGR02969 151 RPIIDACKtfcKTSGccqskengvccldqginglpefeegdetSPELFSEEEFLpLDPTQELIFPPELMRMAEKQpqrtr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 205 -------QFFAPKTLQDFATLRLQLPQARIVAGSTDVGLWVTKQGRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLS- 276
Cdd:TIGR02969 231 vfysermMWISPVTLKELLEAKFKYPQAPVVMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHTGDGLTLGAGLSLAq 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 277 --DALIKISDFYPD-----FQELQRRFASMP---IKNAGTLGGNIANGSPIGDSMPALITLGTRLILRVGKQTREIALED 346
Cdd:TIGR02969 311 vkDILADVVQKLPEettqtYRALLKHLGTLAgsqIRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLSE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 347 FYLDYQKTA-LQLGEFVEAIVIPLREgqtRFKFAS-YKIAKRFEQDISAVCAAISCEL-DNDDVTHNVRIAFGGMAAIPK 423
Cdd:TIGR02969 391 QFLSKCPDAdLKPQEILVSVNIPYSR---KWEFVSaFRQAQRQQNALAIVNSGMRVFFgEGDGIIRELSISYGGVGPTTI 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940328420 424 RAKYAEAILEGQQITAELIVQAQQALSQDYQPLDDGRASSA-YRLHVAKNCLKRFYLEkiLSQTLTRVN 491
Cdd:TIGR02969 468 CAKNSCQKLIGRPWNEEMLDTACRLILDEVSLAGSAPGGKVeFKRTLIISFLFKFYLE--VSQILKRMD 534
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
13-171 |
9.78e-48 |
|
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: 162.18 E-value: 9.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 13 GQQQVENIVPTMTVLQFLREYTQtgktrQTGTKEGCAEGDCGACTVvigeLVNDnlqlRSVNACIQFLPTLDGKALFTVE 92
Cdd:COG2080 10 GKPVEVDVDPDTPLLDVLRDDLG-----LTGTKFGCGHGQCGACTV----LVDG----KAVRSCLTLAVQADGKEITTIE 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940328420 93 DLHsllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYEnEQQSLSKDKISDYLSGNLCRCTGYRPILDAAQKA 171
Cdd:COG2080 77 GLA-----EDGELHPLQQAFIEHGALQCGYCTPGMIMAAVALLD-ENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRA 149
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
3-477 |
6.76e-47 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 175.29 E-value: 6.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 3 ERPITFFFRGGQQQVENIVPTMTVLQFLREytqtgKTRQTGTKEGCAEGDCGACTVVIGEL--VNDNLQLRSVNACIQFL 80
Cdd:PLN00192 3 NMSLVFAVNGERFELSSVDPSTTLLEFLRT-----QTPFKSVKLGCGEGGCGACVVLLSKYdpVLDQVEDFTVSSCLTLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 81 PTLDGKALFTVEDLHSllpVQDGtLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSLSKDKISDY---------- 150
Cdd:PLN00192 78 CSVNGCSITTSEGLGN---SKDG-FHPIHKRFAGFHASQCGFCTPGMCISLFSALVNADKTDRPEPPSGFskltvveaek 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 151 -LSGNLCRCTGYRPILDAAQ-----------------KAYDYPRVVLERQKVIDVLKEIRTLP---------ALYLNDQK 203
Cdd:PLN00192 154 aVSGNLCRCTGYRPIVDACKsfaadvdiedlglnsfwKKGESEEAKLSKLPPYNHSDHICTFPeflkkeiksSLLLDSSR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 204 QQFFAPKTLQDFATLrLQLPQA-----RIVAGSTDVGlwVTKQGRDLGDMLYIGQVEELKKIVVTDLALTIGANVSLS-- 276
Cdd:PLN00192 234 YRWYTPVSVEELQSL-LESNNFdgvsvKLVVGNTGTG--YYKDEELYDKYIDIRHIPELSMIRRDEKGIEIGAVVTISka 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 277 -DALIKISDFYPDFQEL---QRRFASMPIKNAGTLGGNI--ANGSPI-GDSMPALITLGTRLILRVGKQTREIALEDFY- 348
Cdd:PLN00192 311 iEALREESKSEYVFKKIadhMEKIASRFVRNTGSIGGNLvmAQRKQFpSDIATILLAAGSTVNIQNASKREKLTLEEFLe 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 349 ---LDYQKTALqlgefveAIVIP----LREGQTRFKFASYKIAKR-FEQDISAVCAA----ISCELDNDDVT-HNVRIAF 415
Cdd:PLN00192 391 rppLDSKSLLL-------SVEIPswtsSSGSDTKLLFETYRAAPRpLGNALPYLNAAflaeVSQDASSGGIVvNDCRLAF 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940328420 416 ---GGMAAIpkRAKYAEAILEGQQITAELIVQAQQALSQDYQPlDDGRASSAYRLHVAKNCLKRF 477
Cdd:PLN00192 464 gayGTKHAI--RARKVEEFLTGKVLSDSVLYEAVRLLKGIVVP-EDGTSHPEYRSSLAVGFLFDF 525
|
|
| PRK09971 |
PRK09971 |
xanthine dehydrogenase subunit XdhB; Provisional |
204-476 |
2.20e-38 |
|
xanthine dehydrogenase subunit XdhB; Provisional
Pssm-ID: 182175 [Multi-domain] Cd Length: 291 Bit Score: 141.72 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 204 QQFFAPKTLQDFATLRLQLPQARIVAGSTDVgLWVTKQGRDLG-DMLYIGQVEELKKI-VVTDLALTIGANVSLS----D 277
Cdd:PRK09971 5 AEYHEAATLEEAIELLADNPQAKLIAGGTDV-LIQLHHHNDRYrHLVSIHNIAELRGItLAEDGSIRIGAATTFTqiieD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 278 ALIKisDFYPDFQELQRRFASMPIKNAGTLGGNIANGSPIGDSMPALITLGTRLILRVGKQTREIALEDFYLDYQKTALQ 357
Cdd:PRK09971 84 PIIQ--KHLPALAEAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSPNGVRFVPINGFYTGPGKVSLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 358 LGEFVEAIVIPlREGQTRFKFASYKIAKRFEQDISAVCAAISCELDNDDVThNVRIAFGGMAAIPKRAKYAEAILEGQQI 437
Cdd:PRK09971 162 HDEILVAFIIP-PEPYEHAGGAYIKYAMRDAMDIATIGCAVLCRLDNGNFE-DLRLAFGVAAPTPIRCQHAEQTAKGAPL 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 940328420 438 TAELIVQAQQALSQDYQPLDDGRASSAYRLHVAKNCLKR 476
Cdd:PRK09971 240 NLETLEAIGELVLQDVAPRSSWRASKEFRLHLIQELTKR 278
|
|
| CO_deh_flav_C |
pfam03450 |
CO dehydrogenase flavoprotein C-terminal domain; |
379-480 |
7.27e-35 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 460921 [Multi-domain] Cd Length: 102 Bit Score: 125.75 E-value: 7.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 379 ASYKIAKRFEQDISAVCAAISCELDNDDVTHnVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQAQQALSQDYQPLDD 458
Cdd:pfam03450 1 AAYKQAKRRDDDIAIVNAAFRVRLDGGTVED-ARIAFGGVAPTPIRATEAEAALIGKPWDEETLEAAAALLLEDLSPLSD 79
|
90 100
....*....|....*....|..
gi 940328420 459 GRASSAYRLHVAKNCLKRFYLE 480
Cdd:pfam03450 80 PRGSAEYRRHLARSLLFRFLLE 101
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
90-168 |
4.11e-32 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 117.53 E-value: 4.11e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 940328420 90 TVEDLhsllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSLSKDKISDYLSGNLCRCTGYRPILDAA 168
Cdd:pfam01799 1 TIEGL------AESGGEPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
380-480 |
7.42e-32 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 117.72 E-value: 7.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 380 SYKIAKRFEQDISAVCAAISCELDNDDVThNVRIAFGGMAAIPKRAKYAEAILEGQQITAELIVQ-AQQALSQDYQPLDD 458
Cdd:smart01092 1 AYKKSRRRDGDIALVSAAVALTLDGGRVT-EARIALGGVAPTPKRAAEAEAALVGKPLTDEALARaAAAALAQDFTPLSD 79
|
90 100
....*....|....*....|..
gi 940328420 459 GRASSAYRLHVAKNCLKRFYLE 480
Cdd:smart01092 80 MRASAEYRRQLAANLLRRALLE 101
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
20-170 |
1.45e-28 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 110.78 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 20 IVPTMTVLQFLREYTQTGktrqtgTKEGCAEGDCGACTVVIGELVNDnlqlrsvnACIQFLPTLDGKALFTVEDLHsllp 99
Cdd:PRK09908 22 AAPGTPLSELLREQGLLS------VKQGCCVGECGACTVLVDGTAID--------SCLYLAAWAEGKEIRTLEGEA---- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 940328420 100 vQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYEN-EQQSLSKDKISDYLSGNLCRCTGYRPILDAAQK 170
Cdd:PRK09908 84 -KGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKpREKPLTITEIRRGLAGNLCRCTGYQMIVNTVLD 154
|
|
| 4hydroxCoAred |
TIGR03193 |
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ... |
18-171 |
5.98e-27 |
|
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.
Pssm-ID: 132237 [Multi-domain] Cd Length: 148 Bit Score: 106.11 E-value: 5.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 18 ENIVP-TMTVLQFLREYTQTgktrqTGTKEGCAEGDCGACTVVIGElvndnlqlRSVNACIQFLPTLDGKALFTVEDLHS 96
Cdd:TIGR03193 12 EDAVAdNMLLVDYLRDTVGL-----TGTKQGCDGGECGACTVLVDG--------RPRLACSTLAHRVAGRKVETVEGLAT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 940328420 97 llpvqDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSlSKDKISDYLSGNLCRCTGYRPILDAAQKA 171
Cdd:TIGR03193 79 -----NGRLSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSP-SRDEIRAALAGNLCRCTGYVKIIESVEAA 147
|
|
| PRK11433 |
PRK11433 |
aldehyde oxidoreductase 2Fe-2S subunit; Provisional |
5-167 |
2.41e-24 |
|
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
Pssm-ID: 236910 [Multi-domain] Cd Length: 217 Bit Score: 101.00 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 5 PITFFFRGGQQQVENIVPTmTVLQFLREYTQTgktrqTGTKEGCAEGDCGACTVvigeLVNDnlqlRSVNACIQFLPTLD 84
Cdd:PRK11433 51 PVTLKVNGKTEQLEVDTRT-TLLDALREHLHL-----TGTKKGCDHGQCGACTV----LVNG----RRLNACLTLAVMHQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 85 GKALFTVEDLHsllpvQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYE--------------NEQQSLSKDKISDY 150
Cdd:PRK11433 117 GAEITTIEGLG-----SPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKeikdgipshvtvdlTAAPELTADEIRER 191
|
170
....*....|....*..
gi 940328420 151 LSGNLCRCTGYRPILDA 167
Cdd:PRK11433 192 MSGNICRCGAYSNILEA 208
|
|
| PRK09800 |
PRK09800 |
putative hypoxanthine oxidase; Provisional |
73-171 |
2.00e-05 |
|
putative hypoxanthine oxidase; Provisional
Pssm-ID: 182084 [Multi-domain] Cd Length: 956 Bit Score: 47.52 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 73 VNACIQFLPTLDGKALFTVEDLhsllpVQDGTLHPVQQAMVDIHGSQCGFCTPGFIMSLWSMYENEQQSlSKDKISDYLS 152
Cdd:PRK09800 56 VNASLLIAAQLEKADIRTAESL-----GKWNELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAP-TREEIDDALS 129
|
90
....*....|....*....
gi 940328420 153 GNLCRCTGYRPILDAAQKA 171
Cdd:PRK09800 130 GLFSRDAGWQQYYQVIELA 148
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
6-77 |
1.94e-03 |
|
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: 37.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 6 ITFFFRGGQQQVEnIVPTMTVLQFLREytqTGKTrqtgTKEGCAEGDCGACTV-VIGELVNDNLQL---------RSVNA 75
Cdd:cd00207 1 VTINVPGSGVEVE-VPEGETLLDAARE---AGID----IPYSCRAGACGTCKVeVVEGEVDQSDPSlldeeeaegGYVLA 72
|
..
gi 940328420 76 CI 77
Cdd:cd00207 73 CQ 74
|
|
| Fer2_3 |
pfam13085 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
22-101 |
8.74e-03 |
|
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: 36.06 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 940328420 22 PTMTVLQFLreytQTGKTRQTGT---KEGCAEGDCGACTVVIgelvNDnlqlRSVNACIQFLPTLDGKALfTVEDLhSLL 98
Cdd:pfam13085 27 EGMTVLDAL----NKIKEEQDPTlafRRSCREGICGSCAMNI----NG----KPRLACKTLIDDLLGQDI-TLEPL-PGF 92
|
...
gi 940328420 99 PVQ 101
Cdd:pfam13085 93 PVI 95
|
|
|