|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
18-404 |
0e+00 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 662.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 18 ILRSV-DAPTEEKIEESLEGNLCRCTGYRPIVDAFRVFAKTDDMLYTDAYLNSNAKGEFVCPSTGKPCSCRSETVCKEDN 96
Cdd:PLN02906 104 LLRSSkTPPTEEQIEECLAGNLCRCTGYRPILDAFRVFAKTDDALYTGVSSLSLQDGEPICPSTGKPCSCGSKTTSAAGT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 97 ieqkkACGDSYEHISYSEIDGRTYTDKELIFPPELLLRKLTYLNLSGFGGLKWYRSVRLQHVLDIKSRYPDTKLVVGNTE 176
Cdd:PLN02906 184 -----CKSDRFQPISYSEIDGSWYTEKELIFPPELLLRKLTPLKLLGNGGLTWYRPTSLQHLLELKAEYPDAKLVVGNTE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 177 IGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEQASHYTSSCQAFIEQIKWFAGTQIK 256
Cdd:PLN02906 259 VGIEMRFKNAQYPVLISPTHVPELNAIKVKDDGLEIGAAVRLSELQNLFRKVVKERPAHETSACKAFIEQLKWFAGTQIR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 257 NVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNIRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQ 336
Cdd:PLN02906 339 NVASIGGNICTASPISDLNPLWMAAGATFVIISCDGDIRSVPASDFFLGYRKVDLKPDEILLSVFLPWTRPFEYVKEFKQ 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160690108 337 AHRRDDDIAIVNAGMRVCLEEKNEKWVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGALEV 404
Cdd:PLN02906 419 AHRRDDDIAIVNAGMRVKLEEKDGEWIVSDASIAYGGVAPLSVSARKTEEFLIGKPWNKETLQDALKV 486
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
19-403 |
2.96e-76 |
|
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: 244.11 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 19 LRSVDAPTEEKIEESLEGNLCRCTGYRPIVDAfrvfaktddmlytdaylnsnakGEFVCpstGKPCSCRSeTVCKEDNIE 98
Cdd:TIGR02963 122 YKNSPAPSRADIEDALQGNLCRCTGYRPILDA----------------------AEAAF---DYPCSDPL-DADRAPIIE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 99 QKKACGDsYEHISYseidgrtytdkelifppelllrkltylnlsGFGGLKWYRSVRLQHVLDIKSRYPDTKLVVGNTEIG 178
Cdd:TIGR02963 176 RLRALRA-GETVEL------------------------------NFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 179 IEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEqashytsscqaFIEQIKWFAGTQIKNV 258
Cdd:TIGR02963 225 LWVTKQMRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPE-----------LGELLRRFASLQIRNA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 259 ASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNiRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQAH 338
Cdd:TIGR02963 294 GTLGGNIANGSPIGDSPPALIALGARLTLRKGEGR-RTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGERFRAYKISK 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160690108 339 RRDDDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGALE 403
Cdd:TIGR02963 373 RFDDDISAVCAAFNLELDGG----VVAEIRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMA 433
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
23-396 |
4.16e-66 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 217.70 E-value: 4.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 23 DAPTEEKIEESLEGNLCRCTGYRPIVDA-FRVFAktddmlytdaylnsnakgefvCPSTGKPCSCRSETVckedniEQKK 101
Cdd:COG4630 125 PAPDRADIEDALSGNLCRCTGYRPIIDAaRAMAE---------------------APAPDPFAADRAAVA------AALR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 102 ACGDSyEHISYSEIDGRtytdkelifppelllrkltylnlsgfgglkWYRSVRLQHVLDIKSRYPDTKLVVGNTEIGIEM 181
Cdd:COG4630 178 ALADG-ETVELGAGGSR------------------------------FLAPATLDELAALLAAHPDARLVAGATDVGLWV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 182 RLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRatkeqasHYTsscqAFIEQIKWFAGTQIKNVASV 261
Cdd:COG4630 227 TKQLRDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAA-------HFP----ELAELLRRFASRQIRNAGTL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 262 GGNICTASPISDLNPIWMAAGAKFRIIDCKGnIRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQAHRRD 341
Cdd:COG4630 296 GGNIANGSPIGDSPPALIALGAELVLRSGDG-RRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFD 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160690108 342 DDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHE 396
Cdd:COG4630 375 DDISAVCAAFALTLDDG----TVTEARIAFGGMAATPKRARAAEAALLGQPWTEA 425
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
148-324 |
4.93e-58 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 186.98 E-value: 4.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 148 KWYRSVRLQHVLDIKSRYPDTKLVVGNTEIGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRR 227
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 228 AtkeqashytsSCQAFIEQIKWFAGTQIKNVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGnIRTTAAENFFLGYR 307
Cdd:pfam00941 84 E----------AYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEG-ERTVPLEDFFLGYG 152
|
170
....*....|....*..
gi 160690108 308 KVDLASNEILLSIFLPW 324
Cdd:pfam00941 153 KTALEPGELITAVIIPL 169
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
334-401 |
2.03e-12 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 63.02 E-value: 2.03e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160690108 334 FKQAHRRDDDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGA 401
Cdd:smart01092 2 YKKSRRRDGDIALVSAAVALTLDGG----RVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALARA 65
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02906 |
PLN02906 |
xanthine dehydrogenase |
18-404 |
0e+00 |
|
xanthine dehydrogenase
Pssm-ID: 215491 [Multi-domain] Cd Length: 1319 Bit Score: 662.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 18 ILRSV-DAPTEEKIEESLEGNLCRCTGYRPIVDAFRVFAKTDDMLYTDAYLNSNAKGEFVCPSTGKPCSCRSETVCKEDN 96
Cdd:PLN02906 104 LLRSSkTPPTEEQIEECLAGNLCRCTGYRPILDAFRVFAKTDDALYTGVSSLSLQDGEPICPSTGKPCSCGSKTTSAAGT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 97 ieqkkACGDSYEHISYSEIDGRTYTDKELIFPPELLLRKLTYLNLSGFGGLKWYRSVRLQHVLDIKSRYPDTKLVVGNTE 176
Cdd:PLN02906 184 -----CKSDRFQPISYSEIDGSWYTEKELIFPPELLLRKLTPLKLLGNGGLTWYRPTSLQHLLELKAEYPDAKLVVGNTE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 177 IGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEQASHYTSSCQAFIEQIKWFAGTQIK 256
Cdd:PLN02906 259 VGIEMRFKNAQYPVLISPTHVPELNAIKVKDDGLEIGAAVRLSELQNLFRKVVKERPAHETSACKAFIEQLKWFAGTQIR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 257 NVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNIRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQ 336
Cdd:PLN02906 339 NVASIGGNICTASPISDLNPLWMAAGATFVIISCDGDIRSVPASDFFLGYRKVDLKPDEILLSVFLPWTRPFEYVKEFKQ 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160690108 337 AHRRDDDIAIVNAGMRVCLEEKNEKWVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGALEV 404
Cdd:PLN02906 419 AHRRDDDIAIVNAGMRVKLEEKDGEWIVSDASIAYGGVAPLSVSARKTEEFLIGKPWNKETLQDALKV 486
|
|
| xanthine_xdhA |
TIGR02963 |
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ... |
19-403 |
2.96e-76 |
|
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: 244.11 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 19 LRSVDAPTEEKIEESLEGNLCRCTGYRPIVDAfrvfaktddmlytdaylnsnakGEFVCpstGKPCSCRSeTVCKEDNIE 98
Cdd:TIGR02963 122 YKNSPAPSRADIEDALQGNLCRCTGYRPILDA----------------------AEAAF---DYPCSDPL-DADRAPIIE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 99 QKKACGDsYEHISYseidgrtytdkelifppelllrkltylnlsGFGGLKWYRSVRLQHVLDIKSRYPDTKLVVGNTEIG 178
Cdd:TIGR02963 176 RLRALRA-GETVEL------------------------------NFGGERFIAPTTLDDLAALKAAHPDARIVAGSTDVG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 179 IEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEqashytsscqaFIEQIKWFAGTQIKNV 258
Cdd:TIGR02963 225 LWVTKQMRDLPDVIYVGQVAELKRIEETDDGIEIGAAVTLTDAYAALAKRYPE-----------LGELLRRFASLQIRNA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 259 ASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNiRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQAH 338
Cdd:TIGR02963 294 GTLGGNIANGSPIGDSPPALIALGARLTLRKGEGR-RTLPLEDFFIDYGKTDRQPGEFVEALHVPRPTPGERFRAYKISK 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160690108 339 RRDDDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGALE 403
Cdd:TIGR02963 373 RFDDDISAVCAAFNLELDGG----VVAEIRIAFGGMAATPKRAAATEAALLGKPWNEATVEAAMA 433
|
|
| XdhA |
COG4630 |
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ... |
23-396 |
4.16e-66 |
|
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];
Pssm-ID: 443668 [Multi-domain] Cd Length: 476 Bit Score: 217.70 E-value: 4.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 23 DAPTEEKIEESLEGNLCRCTGYRPIVDA-FRVFAktddmlytdaylnsnakgefvCPSTGKPCSCRSETVckedniEQKK 101
Cdd:COG4630 125 PAPDRADIEDALSGNLCRCTGYRPIIDAaRAMAE---------------------APAPDPFAADRAAVA------AALR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 102 ACGDSyEHISYSEIDGRtytdkelifppelllrkltylnlsgfgglkWYRSVRLQHVLDIKSRYPDTKLVVGNTEIGIEM 181
Cdd:COG4630 178 ALADG-ETVELGAGGSR------------------------------FLAPATLDELAALLAAHPDARLVAGATDVGLWV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 182 RLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRatkeqasHYTsscqAFIEQIKWFAGTQIKNVASV 261
Cdd:COG4630 227 TKQLRDLPPVIFLGRVAELRRIEETDDGLEIGAAVTLSDAEAALAA-------HFP----ELAELLRRFASRQIRNAGTL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 262 GGNICTASPISDLNPIWMAAGAKFRIIDCKGnIRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEFKQAHRRD 341
Cdd:COG4630 296 GGNIANGSPIGDSPPALIALGAELVLRSGDG-RRTLPLEDFFLGYRKTDLQPGEFVEAIRIPLPAAGQRLRAYKVSKRFD 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 160690108 342 DDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHE 396
Cdd:COG4630 375 DDISAVCAAFALTLDDG----TVTEARIAFGGMAATPKRARAAEAALLGQPWTEA 425
|
|
| mam_aldehyde_ox |
TIGR02969 |
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ... |
18-397 |
3.75e-65 |
|
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: 225.66 E-value: 3.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 18 ILRSVDAPTEEKIEESLEGNLCRCTGYRPIVDAFRVFAKTDDMLytdaylnSNAKGEFVCPSTGKPCSCRSEtvckedni 97
Cdd:TIGR02969 124 LLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCC-------QSKENGVCCLDQGINGLPEFE-------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 98 EQKKACGDSYEHISYSEIDgrtyTDKELIFPPELLL---RKLTYLNLSGFGGLKWYRSVRLQHVLDIKSRYPDTKLVVGN 174
Cdd:TIGR02969 189 EGDETSPELFSEEEFLPLD----PTQELIFPPELMRmaeKQPQRTRVFYSERMMWISPVTLKELLEAKFKYPQAPVVMGN 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 175 TEIGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEQASHYTSSCQAFIEQIKWFAGTQ 254
Cdd:TIGR02969 265 TSVGPEVKFKGVFHPVIISPDRIEELSVVNHTGDGLTLGAGLSLAQVKDILADVVQKLPEETTQTYRALLKHLGTLAGSQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 255 IKNVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNIRTTAAENFFLGYRKVDLASNEILLSIFLPWTRPFEFVKEF 334
Cdd:TIGR02969 345 IRNMASLGGHIISRHLDSDLNPLLAVGNCTLNLLSKEGKRQIPLSEQFLSKCPDADLKPQEILVSVNIPYSRKWEFVSAF 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160690108 335 KQAHRRDDDIAIVNAGMRVCLEEKNEkwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHEL 397
Cdd:TIGR02969 425 RQAQRQQNALAIVNSGMRVFFGEGDG--IIRELSISYGGVGPTTICAKNSCQKLIGRPWNEEM 485
|
|
| FAD_binding_5 |
pfam00941 |
FAD binding domain in molybdopterin dehydrogenase; |
148-324 |
4.93e-58 |
|
FAD binding domain in molybdopterin dehydrogenase;
Pssm-ID: 460007 [Multi-domain] Cd Length: 170 Bit Score: 186.98 E-value: 4.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 148 KWYRSVRLQHVLDIKSRYPDTKLVVGNTEIGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRR 227
Cdd:pfam00941 4 GYYRPASLAEALELLAAGPDAKLVAGGTSLGPLMKLRLARPDHLIDINGIPELRGIEETDGGLEIGAAVTLSEIAEPLLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 228 AtkeqashytsSCQAFIEQIKWFAGTQIKNVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGnIRTTAAENFFLGYR 307
Cdd:pfam00941 84 E----------AYPALSEALRKIASPQIRNVGTIGGNIANASPISDLPPALLALDAKVELRSGEG-ERTVPLEDFFLGYG 152
|
170
....*....|....*..
gi 160690108 308 KVDLASNEILLSIFLPW 324
Cdd:pfam00941 153 KTALEPGELITAVIIPL 169
|
|
| CutB |
COG1319 |
Aldehyde, CO, or xanthine dehydrogenase, FAD-binding subunit [Energy production and conversion] ... |
155-397 |
1.09e-39 |
|
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: 142.95 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 155 LQHVLDIKSRY-PDTKLVVGNTEIGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLT--VFRRAtke 231
Cdd:COG1319 12 LEEALALLAEHgPDARVLAGGTDLLPLMKLRLARPEHLVDINRIPELRGIEEEGGGLRIGALVTHAELAAspLVRER--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 232 qashytssCQAFIEQIKWFAGTQIKNVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGNiRTTAAENFFLGYRKVDL 311
Cdd:COG1319 89 --------YPLLAEAARAIASPQIRNRGTIGGNLANADPAADLPPALLALDATVELAGPDGE-RTIPAADFFLGPGETAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 312 ASNEILLSIFLP---WTRPFEFVkefKQAHRRDDDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFL 388
Cdd:COG1319 160 EPGELITAVRLPappAGAGSAYL---KVGRRASDAIALVSVAVALRLDGG----TIRDARIALGGVAPTPWRAREAEAAL 232
|
....*....
gi 160690108 389 IAKTWNHEL 397
Cdd:COG1319 233 AGKPLSEEA 241
|
|
| PLN00192 |
PLN00192 |
aldehyde oxidase |
31-401 |
6.13e-26 |
|
aldehyde oxidase
Pssm-ID: 215096 [Multi-domain] Cd Length: 1344 Bit Score: 110.58 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 31 EESLEGNLCRCTGYRPIVDAFRVFAKTDDMlyTDAYLNSNAKgefvcpstgkpcscrsetvcKEDNIEQKKACGDSYEHi 110
Cdd:PLN00192 152 EKAVSGNLCRCTGYRPIVDACKSFAADVDI--EDLGLNSFWK--------------------KGESEEAKLSKLPPYNH- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 111 syseidgrtytDKELIFPPELLLRKLTYLNLSGFGGLKWYRSV---RLQHVLD-IKSRYPDTKLVVGNTEIGIEMRLKgi 186
Cdd:PLN00192 209 -----------SDHICTFPEFLKKEIKSSLLLDSSRYRWYTPVsveELQSLLEsNNFDGVSVKLVVGNTGTGYYKDEE-- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 187 QYQVLTCVAYVPELNKVSVKDDGLEIGAAVRLSELLTVFRRATKEQ------ASHytsscqafIEQIkwfAGTQIKNVAS 260
Cdd:PLN00192 276 LYDKYIDIRHIPELSMIRRDEKGIEIGAVVTISKAIEALREESKSEyvfkkiADH--------MEKI---ASRFVRNTGS 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 261 VGGNICTAS----PiSDLNPIWMAAGAKFRIIDCKGNIRTTAAEnfFLGYRKVDlaSNEILLSIFLP-WTRPFE-----F 330
Cdd:PLN00192 345 IGGNLVMAQrkqfP-SDIATILLAAGSTVNIQNASKREKLTLEE--FLERPPLD--SKSLLLSVEIPsWTSSSGsdtklL 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160690108 331 VKEFKQAHR-RDDDIAIVNAGM--RVCLEEKNEKWVVSEASIAYGGV-APLSVSAVKTKNFLIAKTWNHELSLGA 401
Cdd:PLN00192 420 FETYRAAPRpLGNALPYLNAAFlaEVSQDASSGGIVVNDCRLAFGAYgTKHAIRARKVEEFLTGKVLSDSVLYEA 494
|
|
| PRK09971 |
PRK09971 |
xanthine dehydrogenase subunit XdhB; Provisional |
150-397 |
3.01e-24 |
|
xanthine dehydrogenase subunit XdhB; Provisional
Pssm-ID: 182175 [Multi-domain] Cd Length: 291 Bit Score: 101.27 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 150 YRSVRLQHVLDIKSRYPDTKLVVGNTEIGIEMRLKGIQYQVLTCVAYVPELNKVSVKDDG-LEIGAAVRLSELLT--VFR 226
Cdd:PRK09971 8 HEAATLEEAIELLADNPQAKLIAGGTDVLIQLHHHNDRYRHLVSIHNIAELRGITLAEDGsIRIGAATTFTQIIEdpIIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 227 RATKEQAshytsscqafiEQIKWFAGTQIKNVASVGGNICTASPISDLNPIWMAAGAKFRIIDCKGnIRTTAAENFFLGY 306
Cdd:PRK09971 88 KHLPALA-----------EAAVSIGGPQIRNVATIGGNICNGATSADSAPPLFALDAKLEIHSPNG-VRFVPINGFYTGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160690108 307 RKVDLASNEILLSIFLPwTRPFEFVKE--FKQAHRRDDDIAIVnaGMRVCLEEKNEKwvVSEASIAYGGVAPLSVSAVKT 384
Cdd:PRK09971 156 GKVSLEHDEILVAFIIP-PEPYEHAGGayIKYAMRDAMDIATI--GCAVLCRLDNGN--FEDLRLAFGVAAPTPIRCQHA 230
|
250
....*....|...
gi 160690108 385 KNFLIAKTWNHEL 397
Cdd:PRK09971 231 EQTAKGAPLNLET 243
|
|
| CO_deh_flav_C |
pfam03450 |
CO dehydrogenase flavoprotein C-terminal domain; |
334-397 |
2.89e-17 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 460921 [Multi-domain] Cd Length: 102 Bit Score: 76.83 E-value: 2.89e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160690108 334 FKQAHRRDDDIAIVNAGMRVCLEEknekWVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHEL 397
Cdd:pfam03450 3 YKQAKRRDDDIAIVNAAFRVRLDG----GTVEDARIAFGGVAPTPIRATEAEAALIGKPWDEET 62
|
|
| CO_deh_flav_C |
smart01092 |
CO dehydrogenase flavoprotein C-terminal domain; |
334-401 |
2.03e-12 |
|
CO dehydrogenase flavoprotein C-terminal domain;
Pssm-ID: 215021 [Multi-domain] Cd Length: 102 Bit Score: 63.02 E-value: 2.03e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160690108 334 FKQAHRRDDDIAIVNAGMRVCLEEKnekwVVSEASIAYGGVAPLSVSAVKTKNFLIAKTWNHELSLGA 401
Cdd:smart01092 2 YKKSRRRDGDIALVSAAVALTLDGG----RVTEARIALGGVAPTPKRAAEAEAALVGKPLTDEALARA 65
|
|
| Fer2_2 |
pfam01799 |
[2Fe-2S] binding domain; |
16-51 |
2.79e-12 |
|
[2Fe-2S] binding domain;
Pssm-ID: 460336 [Multi-domain] Cd Length: 73 Bit Score: 61.68 E-value: 2.79e-12
10 20 30
....*....|....*....|....*....|....*.
gi 160690108 16 AIILRSVDAPTEEKIEESLEGNLCRCTGYRPIVDAF 51
Cdd:pfam01799 38 ALLERNPPPPTEAEIREALSGNLCRCTGYRRIVDAV 73
|
|
| CutS |
COG2080 |
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ... |
18-56 |
1.52e-09 |
|
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: 56.25 E-value: 1.52e-09
10 20 30
....*....|....*....|....*....|....*....
gi 160690108 18 ILRSVDAPTEEKIEESLEGNLCRCTGYRPIVDAFRVFAK 56
Cdd:COG2080 113 LLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAA 151
|
|
| PRK09908 |
PRK09908 |
xanthine dehydrogenase iron sulfur-binding subunit XdhC; |
26-58 |
3.82e-04 |
|
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
Pssm-ID: 182139 [Multi-domain] Cd Length: 159 Bit Score: 40.67 E-value: 3.82e-04
10 20 30
....*....|....*....|....*....|...
gi 160690108 26 TEEKIEESLEGNLCRCTGYRPIVDAFRVFAKTD 58
Cdd:PRK09908 127 TITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK 159
|
|
|