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Conserved domains on  [gi|345651472|gb|AEO14748|]
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large subunit carbon monoxide dehydrogenase, partial [Paraburkholderia paradisi]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CO_dehy_Mo_lg super family cl31209
carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of ...
1-373 0e+00

carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of group of carbon-monoxide dehydrogenases that include molybdenum as part of the enzymatic cofactor. There are various forms of carbon-monoxide dehydrogenase; Salicibacter pomeroyi DSS-3, for example, has two forms. Note that, at least in some species, the active site Cys is modified with a selenium attached to (rather than replacing) the sulfur atom. This is termed selanylcysteine, and created post-translationally, in contrast to selenocysteine incorporation during translation as for many other selenoproteins. [Energy metabolism, Other]


The actual alignment was detected with superfamily member TIGR02416:

Pssm-ID: 131469 [Multi-domain]  Cd Length: 770  Bit Score: 652.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472    1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKWPAGMFHVCTGSYAIPNAFVSVDG 80
Cdd:TIGR02416 267 VKWVEDRMENLSTTSFARDYHMTGELAATKDGKILAMRCNVLADHGAFDACADPSKWPAGFFNICTGSYDIPVAHCAVDG 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   81 VYTNKFPGGVAYRCSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPYTTPLGLEYDSGDYDTALRKVLAAV 160
Cdd:TIGR02416 347 VYTNKAPGGVAYRCSFRVTEAVYAIERAVDTLAQRLEMDSADLRIKNFIQPEQFPYTAPLGWEYDSGDYPLAMKKAMDTV 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  161 DYDALRAEQARRRADPDAEWLMGIGVVNFTEIVGAGPSKMCDILGVGMFDSCEIRVHPDGSAIARMGTITQGQGHQTTYA 240
Cdd:TIGR02416 427 DYHQLRAEQAAKRKRGETRELMGIGISFFTEIVGAGPSKNCDILGVGMFDSCEIRIHPTGSAIARMGTKSQGQGHETTYA 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  241 QIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVLKG 320
Cdd:TIGR02416 507 QIIATELGIPAEDIMVEEGDTDTAPYGLGTYGSRSTPVAGAATALAARKIKAKAQMIAAHMLEVHEGDLEWDVDRFRVKG 586
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 345651472  321 SPDQFKTVKEVAWAAYNNVPEGLEMGLEAVDYYDPPNFTFPFGAYVCVLDVNR 373
Cdd:TIGR02416 587 DPSKFKTMADIAWAAYNSPPPGLEPGLEAVNYYDPPNMTYPFGAYFCVVDIDV 639
 
Name Accession Description Interval E-value
CO_dehy_Mo_lg TIGR02416
carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of ...
1-373 0e+00

carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of group of carbon-monoxide dehydrogenases that include molybdenum as part of the enzymatic cofactor. There are various forms of carbon-monoxide dehydrogenase; Salicibacter pomeroyi DSS-3, for example, has two forms. Note that, at least in some species, the active site Cys is modified with a selenium attached to (rather than replacing) the sulfur atom. This is termed selanylcysteine, and created post-translationally, in contrast to selenocysteine incorporation during translation as for many other selenoproteins. [Energy metabolism, Other]


Pssm-ID: 131469 [Multi-domain]  Cd Length: 770  Bit Score: 652.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472    1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKWPAGMFHVCTGSYAIPNAFVSVDG 80
Cdd:TIGR02416 267 VKWVEDRMENLSTTSFARDYHMTGELAATKDGKILAMRCNVLADHGAFDACADPSKWPAGFFNICTGSYDIPVAHCAVDG 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   81 VYTNKFPGGVAYRCSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPYTTPLGLEYDSGDYDTALRKVLAAV 160
Cdd:TIGR02416 347 VYTNKAPGGVAYRCSFRVTEAVYAIERAVDTLAQRLEMDSADLRIKNFIQPEQFPYTAPLGWEYDSGDYPLAMKKAMDTV 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  161 DYDALRAEQARRRADPDAEWLMGIGVVNFTEIVGAGPSKMCDILGVGMFDSCEIRVHPDGSAIARMGTITQGQGHQTTYA 240
Cdd:TIGR02416 427 DYHQLRAEQAAKRKRGETRELMGIGISFFTEIVGAGPSKNCDILGVGMFDSCEIRIHPTGSAIARMGTKSQGQGHETTYA 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  241 QIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVLKG 320
Cdd:TIGR02416 507 QIIATELGIPAEDIMVEEGDTDTAPYGLGTYGSRSTPVAGAATALAARKIKAKAQMIAAHMLEVHEGDLEWDVDRFRVKG 586
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 345651472  321 SPDQFKTVKEVAWAAYNNVPEGLEMGLEAVDYYDPPNFTFPFGAYVCVLDVNR 373
Cdd:TIGR02416 587 DPSKFKTMADIAWAAYNSPPPGLEPGLEAVNYYDPPNMTYPFGAYFCVVDIDV 639
CoxL COG1529
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
1-373 1.01e-119

Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441138 [Multi-domain]  Cd Length: 741  Bit Score: 363.01  E-value: 1.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKWPAGMfhVCTGSYAIPNAFVSVDG 80
Cdd:COG1529  268 VKLVLTREEDFLADTHRHATVQRVRLGADKDGKITALRHDVVADTGAYASFGEAVLPLGAT--MATGPYAIPNVRVEARA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  81 VYTNKFPGGvAYRcSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPyttPLGLEYDSGDYDTALRKVLAAV 160
Cdd:COG1529  346 VYTNTPPTG-AYR-GPGRPQAAFALESAMDELAEELGMDPVELRLRNLIRPGDFP---PTGQPYDSGRLAECLEKAAEAF 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 161 DYDALRAEQARRRADpdaeWLMGIGVVNFTEIVGAGPskmcdilgvgMFDSCEIRVHPDGSAIARMGTITQGQGHQTTYA 240
Cdd:COG1529  421 GWGERRARPAEARAG----KLRGIGVAAYIEGSGGGG----------DPESARVRLNPDGSVTVYTGATDIGQGHETVLA 486
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 241 QIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVlkg 320
Cdd:COG1529  487 QIAAEELGVPPEDVRVVLGDTDLTPYGGGTGGSRSTAVGGSAVRKAAEKLREKLLELAAHLLGADPEDLEFEDGRVR--- 563
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 345651472 321 SPDQFKTVKEVAWAAYnnvpeglEMGLEAVDYYDPP-NFTFPFGAYVCVLDVNR 373
Cdd:COG1529  564 VPGRSVSLAELAAAAY-------YGGLEATGTYDPPtYPTYSFGAHVAEVEVDP 610
glyceraldDH_alpha NF041018
glyceraldehyde dehydrogenase subunit alpha;
1-372 7.51e-77

glyceraldehyde dehydrogenase subunit alpha;


Pssm-ID: 468947 [Multi-domain]  Cd Length: 741  Bit Score: 251.16  E-value: 7.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAfARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKwPAGMFHVCTGSYAIPNAFVSVDG 80
Cdd:NF041018 268 VKWTATRSEEMLASE-ARHNVFKGEVAVKRDGTLLAIKGTLLVDLGAYLTYTEGLQ-PAIIPLMIPGPYKVRDLRIRSVA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  81 VYTNKFPGGvAYRCSFRvTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPYTTPLGLEYDSGDYDTALRKVLAAV 160
Cdd:NF041018 346 VYTNTPPIT-MYRGASR-PEATFIIERIMSTVADELGLDDVEVRERNLVRADEMPYTNPFGLKYDSGDYLGLLEEGLEKL 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 161 DYDALR--AEQARRRADpdaewLMGIGVVNFTEIVGAGPskmcdilgvgmFDSCEIRVHPDGSAIARMGTITQGQGHQTT 238
Cdd:NF041018 424 GYYELKkwAEEERKKGR-----KVGVGLAFYLEITTFGP-----------WEYAEVRVDEDGDVTVITGGTPHGQGTETA 487
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 239 YAQIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVL 318
Cdd:NF041018 488 IAQLVADELQIDIERVRVIWGDTDTVPAGIGTYGSRTITAAGSAALLASRQLLEKMKKVAARLLKADVEEVEYSNGEFIN 567
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 345651472 319 KGsPDQFKTVKEVAWAAYNnvpeGLEMGLEAVDYYdPPNFTFPFGAYVCVLDVN 372
Cdd:NF041018 568 KK-EGKKVSWNDVAKAAYR----GKEPGLSASVTY-EADVTFPYGVHVAVVEVD 615
MoCoBD_2 pfam20256
Molybdopterin cofactor-binding domain;
155-373 9.55e-68

Molybdopterin cofactor-binding domain;


Pssm-ID: 466407 [Multi-domain]  Cd Length: 282  Bit Score: 215.09  E-value: 9.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  155 KVLAAVDYDALRAEQARRRAdpdAEWLMGIGVVNFTEIVGAGPskmcdilGVGMFDSCEIRVHPDGSAIARMGTITQGQG 234
Cdd:pfam20256   1 KALELSDYDERRAEQAEFNR---GNRKRGIGIAPYVEGSGLGP-------GALNQAGALVRLNPDGSVTVYTGGTEMGQG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  235 HQTTYAQIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLD 314
Cdd:pfam20256  71 LETKLAQIAAEALGIPPEDVRVVEGDTDTVPNGGGTGASRSTDVGGNAVLLAAEKLRERLLKIAAHLLEASPEDLEFEDG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 345651472  315 RFVLKGSPdQFKTVKEVAWAAYnnvpeGLEMGLEAVDYY---------DPPNFTFPFGAYVCVLDVNR 373
Cdd:pfam20256 151 KVYVKGDP-RSVTFAELAAAAY-----GEGVGLSATGFYtppddetgqGPPFAYYPYGAHAAEVEVDP 212
PRK09970 PRK09970
xanthine dehydrogenase subunit XdhA; Provisional
1-342 3.19e-33

xanthine dehydrogenase subunit XdhA; Provisional


Pssm-ID: 236637 [Multi-domain]  Cd Length: 759  Bit Score: 130.97  E-value: 3.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVV------ADHGAFDACADPTKWPagmfhvctGSYAIPNA 74
Cdd:PRK09970 269 VKVSLSREECFLATRTRHAFTIDIKMGVNRDGTLKGYSLDVLsntgayASHGHSIASAGGNKVA--------YLYPRCAY 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  75 FVSVDGVYTNkFPGGVAYRcSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDqfpYTTPL-GLEYDSGDYDTAL 153
Cdd:PRK09970 341 KYSSKTVYTN-LPSAGAMR-GYGAPQVVFAVESMLDDAATALGIDPVEFRLRNAAREG---DANPLsGKRIYSAGLPECL 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 154 RKVLAAVDYDALRAEQARRRADPDAewlmGIGVVNFTEIVGAGPskmcdilgVGM-FDSCEIRVHPDGSAIARMGTITQG 232
Cdd:PRK09970 416 EKGRKIFEWDKRRAECKNQQGNLRR----GVGVACFSYTSGTWP--------VGLeIAGARLLMNQDGTVQVQSGATEIG 483
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 233 QGHQTTYAQIIASEAGIPASQIAV-EEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEF 311
Cdd:PRK09970 484 QGSDTVFSQMVAETVGIPVSDVRViSTQDTDVTPFDPGAYASRQSYVAGPAIRKAALELKEKILAHAAVMLHQSAMNLDI 563
                        330       340       350
                 ....*....|....*....|....*....|.
gi 345651472 312 DLDRFVLKGSPDQFKTVKEVAWAAYNNVPEG 342
Cdd:PRK09970 564 IDGHIVVKRPGEPLMSLEELAMDAYYHPERG 594
 
Name Accession Description Interval E-value
CO_dehy_Mo_lg TIGR02416
carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of ...
1-373 0e+00

carbon-monoxide dehydrogenase, large subunit; This model represents the large subunits of group of carbon-monoxide dehydrogenases that include molybdenum as part of the enzymatic cofactor. There are various forms of carbon-monoxide dehydrogenase; Salicibacter pomeroyi DSS-3, for example, has two forms. Note that, at least in some species, the active site Cys is modified with a selenium attached to (rather than replacing) the sulfur atom. This is termed selanylcysteine, and created post-translationally, in contrast to selenocysteine incorporation during translation as for many other selenoproteins. [Energy metabolism, Other]


Pssm-ID: 131469 [Multi-domain]  Cd Length: 770  Bit Score: 652.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472    1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKWPAGMFHVCTGSYAIPNAFVSVDG 80
Cdd:TIGR02416 267 VKWVEDRMENLSTTSFARDYHMTGELAATKDGKILAMRCNVLADHGAFDACADPSKWPAGFFNICTGSYDIPVAHCAVDG 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   81 VYTNKFPGGVAYRCSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPYTTPLGLEYDSGDYDTALRKVLAAV 160
Cdd:TIGR02416 347 VYTNKAPGGVAYRCSFRVTEAVYAIERAVDTLAQRLEMDSADLRIKNFIQPEQFPYTAPLGWEYDSGDYPLAMKKAMDTV 426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  161 DYDALRAEQARRRADPDAEWLMGIGVVNFTEIVGAGPSKMCDILGVGMFDSCEIRVHPDGSAIARMGTITQGQGHQTTYA 240
Cdd:TIGR02416 427 DYHQLRAEQAAKRKRGETRELMGIGISFFTEIVGAGPSKNCDILGVGMFDSCEIRIHPTGSAIARMGTKSQGQGHETTYA 506
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  241 QIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVLKG 320
Cdd:TIGR02416 507 QIIATELGIPAEDIMVEEGDTDTAPYGLGTYGSRSTPVAGAATALAARKIKAKAQMIAAHMLEVHEGDLEWDVDRFRVKG 586
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 345651472  321 SPDQFKTVKEVAWAAYNNVPEGLEMGLEAVDYYDPPNFTFPFGAYVCVLDVNR 373
Cdd:TIGR02416 587 DPSKFKTMADIAWAAYNSPPPGLEPGLEAVNYYDPPNMTYPFGAYFCVVDIDV 639
CoxL COG1529
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
1-373 1.01e-119

Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441138 [Multi-domain]  Cd Length: 741  Bit Score: 363.01  E-value: 1.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKWPAGMfhVCTGSYAIPNAFVSVDG 80
Cdd:COG1529  268 VKLVLTREEDFLADTHRHATVQRVRLGADKDGKITALRHDVVADTGAYASFGEAVLPLGAT--MATGPYAIPNVRVEARA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  81 VYTNKFPGGvAYRcSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPyttPLGLEYDSGDYDTALRKVLAAV 160
Cdd:COG1529  346 VYTNTPPTG-AYR-GPGRPQAAFALESAMDELAEELGMDPVELRLRNLIRPGDFP---PTGQPYDSGRLAECLEKAAEAF 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 161 DYDALRAEQARRRADpdaeWLMGIGVVNFTEIVGAGPskmcdilgvgMFDSCEIRVHPDGSAIARMGTITQGQGHQTTYA 240
Cdd:COG1529  421 GWGERRARPAEARAG----KLRGIGVAAYIEGSGGGG----------DPESARVRLNPDGSVTVYTGATDIGQGHETVLA 486
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 241 QIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVlkg 320
Cdd:COG1529  487 QIAAEELGVPPEDVRVVLGDTDLTPYGGGTGGSRSTAVGGSAVRKAAEKLREKLLELAAHLLGADPEDLEFEDGRVR--- 563
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 345651472 321 SPDQFKTVKEVAWAAYnnvpeglEMGLEAVDYYDPP-NFTFPFGAYVCVLDVNR 373
Cdd:COG1529  564 VPGRSVSLAELAAAAY-------YGGLEATGTYDPPtYPTYSFGAHVAEVEVDP 610
glyceraldDH_alpha NF041018
glyceraldehyde dehydrogenase subunit alpha;
1-372 7.51e-77

glyceraldehyde dehydrogenase subunit alpha;


Pssm-ID: 468947 [Multi-domain]  Cd Length: 741  Bit Score: 251.16  E-value: 7.51e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAfARDYHMTGELAADKDGRIKALRVNVVADHGAFDACADPTKwPAGMFHVCTGSYAIPNAFVSVDG 80
Cdd:NF041018 268 VKWTATRSEEMLASE-ARHNVFKGEVAVKRDGTLLAIKGTLLVDLGAYLTYTEGLQ-PAIIPLMIPGPYKVRDLRIRSVA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  81 VYTNKFPGGvAYRCSFRvTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDQFPYTTPLGLEYDSGDYDTALRKVLAAV 160
Cdd:NF041018 346 VYTNTPPIT-MYRGASR-PEATFIIERIMSTVADELGLDDVEVRERNLVRADEMPYTNPFGLKYDSGDYLGLLEEGLEKL 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 161 DYDALR--AEQARRRADpdaewLMGIGVVNFTEIVGAGPskmcdilgvgmFDSCEIRVHPDGSAIARMGTITQGQGHQTT 238
Cdd:NF041018 424 GYYELKkwAEEERKKGR-----KVGVGLAFYLEITTFGP-----------WEYAEVRVDEDGDVTVITGGTPHGQGTETA 487
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 239 YAQIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVL 318
Cdd:NF041018 488 IAQLVADELQIDIERVRVIWGDTDTVPAGIGTYGSRTITAAGSAALLASRQLLEKMKKVAARLLKADVEEVEYSNGEFIN 567
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 345651472 319 KGsPDQFKTVKEVAWAAYNnvpeGLEMGLEAVDYYdPPNFTFPFGAYVCVLDVN 372
Cdd:NF041018 568 KK-EGKKVSWNDVAKAAYR----GKEPGLSASVTY-EADVTFPYGVHVAVVEVD 615
MoCoBD_2 pfam20256
Molybdopterin cofactor-binding domain;
155-373 9.55e-68

Molybdopterin cofactor-binding domain;


Pssm-ID: 466407 [Multi-domain]  Cd Length: 282  Bit Score: 215.09  E-value: 9.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  155 KVLAAVDYDALRAEQARRRAdpdAEWLMGIGVVNFTEIVGAGPskmcdilGVGMFDSCEIRVHPDGSAIARMGTITQGQG 234
Cdd:pfam20256   1 KALELSDYDERRAEQAEFNR---GNRKRGIGIAPYVEGSGLGP-------GALNQAGALVRLNPDGSVTVYTGGTEMGQG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  235 HQTTYAQIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLD 314
Cdd:pfam20256  71 LETKLAQIAAEALGIPPEDVRVVEGDTDTVPNGGGTGASRSTDVGGNAVLLAAEKLRERLLKIAAHLLEASPEDLEFEDG 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 345651472  315 RFVLKGSPdQFKTVKEVAWAAYnnvpeGLEMGLEAVDYY---------DPPNFTFPFGAYVCVLDVNR 373
Cdd:pfam20256 151 KVYVKGDP-RSVTFAELAAAAY-----GEGVGLSATGFYtppddetgqGPPFAYYPYGAHAAEVEVDP 212
MoCoBD_1 pfam02738
Molybdopterin cofactor-binding domain;
1-128 1.37e-41

Molybdopterin cofactor-binding domain;


Pssm-ID: 460671 [Multi-domain]  Cd Length: 244  Bit Score: 146.06  E-value: 1.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472    1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAFdACADPTKWPAGMFHvCTGSYAIPNAFVSVDG 80
Cdd:pfam02738 121 VKWVLDREEDMLATGHRHPFLIKYKVGADKDGKILALDVDLYADGGAY-ADLSPAVPERALSH-LDGPYKIPNVRVDGRA 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 345651472   81 VYTNKFPGGvAYRCSFRVtEAVYLIERMVDVLAQKLGIDKAEIRLRNF 128
Cdd:pfam02738 199 VYTNTPPNG-AFRGFGRP-QGMFALERLMDELAEELGMDPLELRRRNL 244
PRK09970 PRK09970
xanthine dehydrogenase subunit XdhA; Provisional
1-342 3.19e-33

xanthine dehydrogenase subunit XdhA; Provisional


Pssm-ID: 236637 [Multi-domain]  Cd Length: 759  Bit Score: 130.97  E-value: 3.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVV------ADHGAFDACADPTKWPagmfhvctGSYAIPNA 74
Cdd:PRK09970 269 VKVSLSREECFLATRTRHAFTIDIKMGVNRDGTLKGYSLDVLsntgayASHGHSIASAGGNKVA--------YLYPRCAY 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  75 FVSVDGVYTNkFPGGVAYRcSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRKDqfpYTTPL-GLEYDSGDYDTAL 153
Cdd:PRK09970 341 KYSSKTVYTN-LPSAGAMR-GYGAPQVVFAVESMLDDAATALGIDPVEFRLRNAAREG---DANPLsGKRIYSAGLPECL 415
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 154 RKVLAAVDYDALRAEQARRRADPDAewlmGIGVVNFTEIVGAGPskmcdilgVGM-FDSCEIRVHPDGSAIARMGTITQG 232
Cdd:PRK09970 416 EKGRKIFEWDKRRAECKNQQGNLRR----GVGVACFSYTSGTWP--------VGLeIAGARLLMNQDGTVQVQSGATEIG 483
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 233 QGHQTTYAQIIASEAGIPASQIAV-EEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEF 311
Cdd:PRK09970 484 QGSDTVFSQMVAETVGIPVSDVRViSTQDTDVTPFDPGAYASRQSYVAGPAIRKAALELKEKILAHAAVMLHQSAMNLDI 563
                        330       340       350
                 ....*....|....*....|....*....|.
gi 345651472 312 DLDRFVLKGSPDQFKTVKEVAWAAYNNVPEG 342
Cdd:PRK09970 564 IDGHIVVKRPGEPLMSLEELAMDAYYHPERG 594
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
25-372 7.37e-17

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 82.19  E-value: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  25 ELAADKDGRIKALRVNVVADHGAF--DACADPTKWPAGMFHVctgsYAIPNAFVSVDGVYTNKFPGGvAYRcSFRVTEAV 102
Cdd:PRK09800 492 KLGAKKDGRLTAVKMDFRANTGPYgnHSLTVPCNGPALSLPL----YPCDNVDFQVTTYYSNICPNG-AYQ-GYGAPKGN 565
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 103 YLIERMVDVLAQKLGIDKAEIRLRNFIRKDQ------------FPYTTPlglEYDSGDYDTALRKVLAAVDYDALRAeqa 170
Cdd:PRK09800 566 FAITMALAELAEQLQIDQLEIIERNRVHEGQelkilgaigegkAPTSVP---SAASCALEEILRQGREMIQWSSPKP--- 639
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 171 rrrADPDaeWLMGIGVVnfteIVGAGpSKMCDIlgvgmfD--SCEIRVHPDGSAIARMGTITQGQGHQTTYAQIIASEAG 248
Cdd:PRK09800 640 ---QNGD--WHIGRGVA----IIMQK-SGIPDI------DqaNCMIKLESDGTFIVHSGGADIGTGLDTVVTKLAAEVLH 703
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472 249 IPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLLEASPDDVEFDLDRFVlKGSPDqfktv 328
Cdd:PRK09800 704 CPPQDVHVISGDTDHALFDKGAYASSGTCFSGNAARLAAENLREKILFHGAQMLGEPVADVQLATPGVV-RGKKG----- 777
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 345651472 329 kEVAWAAYNNVPE-GLEMG-LEAVDYYDPPNFTFPFGAYVCVLDVN 372
Cdd:PRK09800 778 -EVSFGDIAHKGEtGTGFGsLVGTGSYITPDFAFPYGANFAEVAVN 822
PLN02906 PLN02906
xanthine dehydrogenase
30-336 1.21e-12

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 69.34  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   30 KDGRIKALRVNVVADHG-AFDaCADPTKWPAgMFHVcTGSYAIPNafVSVDGV--YTNkFPGGVAYRcSFRVTEAVYLIE 106
Cdd:PLN02906  848 NEGKILALDLEIYNNGGnSLD-LSGAVLERA-MFHS-DNVYEIPN--VRIVGNvcFTN-FPSNTAFR-GFGGPQGMLITE 920
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  107 RMVDVLAQKLGIDKAEIRLRNFiRKDQfpYTTPLGLEYDSGDYDTALRKVLAAVDYDALRAEQARRRADpdAEWLM-GIG 185
Cdd:PLN02906  921 NWIQRIAVELNKSPEEIREMNF-QGEG--SVTHYGQVLQHCTLPQLWDELKVSCDFLKRREEVDEFNAK--NRWKKrGVA 995
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472  186 VV------NFTeivgagpSKMCDILGVgmfdscEIRVHPDGSAIARMGTITQGQGHQTTYAQIIASEAGIPASQIAVEEG 259
Cdd:PLN02906  996 MVptkfgiSFT-------TKFMNQAGA------LVHVYTDGTVLVTHGGVEMGQGLHTKVAQVAASAFNIPLSSVFISET 1062
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345651472  260 DTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKIAAHLleaspddvefdldrfvlkgspdQFKTVKEVAWAAY 336
Cdd:PLN02906 1063 STDKVPNASPTAASASSDMYGAAVLDACEQIKARMEPVASKL----------------------NFSSFAELVTACY 1117
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
1-297 1.14e-10

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: 63.49  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472     1 VKWIESRSENLSSTAFARDYHMTGELAADKDGRIKALRVNVVADHGAfdaCADPTKW--PAGMFHVcTGSYAIPNAFVSV 78
Cdd:TIGR02969  824 VRCTLERGEDMLITGGRHPYLGKYKAGFMNDGRIVALDVEHYSNGGS---SLDESLWviEMGLLKM-DNAYKFPNLRCRG 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472    79 DGVYTNkFPGGVAYRcSFRVTEAVYLIERMVDVLAQKLGIDKAEIRLRNFIRK-DQFPYTTplglEYDSGDYDTALRKVL 157
Cdd:TIGR02969  900 WACRTN-LPSNTAFR-GFGFPQAGLITEACITEVAAKCGLSPEKVRTINMYKEiDQTPYKQ----EINAKNLFQCWRECM 973
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345651472   158 AAVDYDALRAeqARRRADPDAEWLM-GIGVVNFTEIVGAGPSKMCDILGVgmfdsceIRVHPDGSAIARMGTITQGQGHQ 236
Cdd:TIGR02969  974 AKSSYSERKV--AVEKFNAENYWKKrGLAVIPLKFPVGLGSVAMGQAAAL-------VHIYLDGSVLVTHGGIEMGQGVH 1044
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345651472   237 TTYAQIIASEAGIPASQIAVEEGDTSTAPYGLGTYGSRSTPVAGAAVARASRKIREKARKI 297
Cdd:TIGR02969 1045 TKMIQVVSRELKMPMSNVHLRGTSTETVPNTNASGGSVVADLNGLAVKDACQTLLKRLEPI 1105
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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