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Conserved domains on  [gi|2574422656|ref|WP_308726846|]
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molybdopterin dinucleotide binding domain-containing protein [Frankia casuarinae]

Protein Classification

FdhF/YdeP family oxidoreductase( domain architecture ID 1006521)

FdhF/YdeP family oxidoreductase belongs to the molybdopterin-binding (MopB) superfamily of proteins

EC:  1.-.-.-
Gene Ontology:  GO:0030151|GO:0016491|GO:0046872

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Fdhalpha-like super family cl36953
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ...
7-337 2.31e-120

oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.


The actual alignment was detected with superfamily member TIGR01701:

Pssm-ID: 273765 [Multi-domain]  Cd Length: 743  Bit Score: 363.36  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:TIGR01701 416 QIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRSHVLAKEEALILPV 495
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGQPEVAESgtadrvgLAGDYRRIRA 166
Cdd:TIGR01701 496 LGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEI-------LVDTYDQIRD 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 167 HIARVVPGFTDYEAGLAELGGFPLPHPPRDSRTFPTPSGRAALTVNTCEVLRVPPGH---LLLQTVRSHDQYNTTIYGMD 243
Cdd:TIGR01701 569 AIAATNPGYDDINHRKRRPDGFQLPGAALCERKFPTPDGKANFIVIPLPEFRVPTGHefeLVLVTLRSHDQFNTTIYGED 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 244 DRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGMDRRAENFRVVAYPTARGCAAAYFPETNVLVPLDSTAARS 323
Cdd:TIGR01701 649 DRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLPLDHHDPQS 728
                         330
                  ....*....|....
gi 2574422656 324 NTPTSKSLIIRLEA 337
Cdd:TIGR01701 729 KTPEYKTIPVRLEA 742
 
Name Accession Description Interval E-value
Fdhalpha-like TIGR01701
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ...
7-337 2.31e-120

oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.


Pssm-ID: 273765 [Multi-domain]  Cd Length: 743  Bit Score: 363.36  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:TIGR01701 416 QIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRSHVLAKEEALILPV 495
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGQPEVAESgtadrvgLAGDYRRIRA 166
Cdd:TIGR01701 496 LGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEI-------LVDTYDQIRD 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 167 HIARVVPGFTDYEAGLAELGGFPLPHPPRDSRTFPTPSGRAALTVNTCEVLRVPPGH---LLLQTVRSHDQYNTTIYGMD 243
Cdd:TIGR01701 569 AIAATNPGYDDINHRKRRPDGFQLPGAALCERKFPTPDGKANFIVIPLPEFRVPTGHefeLVLVTLRSHDQFNTTIYGED 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 244 DRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGMDRRAENFRVVAYPTARGCAAAYFPETNVLVPLDSTAARS 323
Cdd:TIGR01701 649 DRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLPLDHHDPQS 728
                         330
                  ....*....|....
gi 2574422656 324 NTPTSKSLIIRLEA 337
Cdd:TIGR01701 729 KTPEYKTIPVRLEA 742
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
7-207 1.06e-75

The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239168 [Multi-domain]  Cd Length: 574  Bit Score: 242.98  E-value: 1.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:cd02767   379 EVFGFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPC 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGqpEVAESGtadrvGLAGDYRRIRA 166
Cdd:cd02767   459 LGRTEIDMQAGGAQAVTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGE--AKPEWE-----ILVEDYDRIRD 531
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2574422656 167 HIARVVP-GFTDYEAGLAELGGFPLPHPPRDsRTFPTPSGRA 207
Cdd:cd02767   532 EIAAVIYeGFADFNQRGDQPGGFHLPNGARE-RKFNTPSGKA 572
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
7-336 8.56e-73

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 239.56  E-value: 8.56e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:PRK09939  430 ERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPV 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGQPEVAESgtadrvgLAGDYRRIRA 166
Cdd:PRK09939  510 LGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEY-------LVEDYDRIRN 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 167 HIARVVPGFTDYEAGLAELGGFPLPHPPRDSRtFPTPSGRAALTvnTCEVLRVPP-----GHLLLQTVRSHDQYNTTIYG 241
Cdd:PRK09939  583 DIEAVLPEFADYNQRIRHPGGFHLINAAAERR-WMTPSGKANFI--TSKGLLEDPssafnSKLVMATVRSHDQYNTTIYG 659
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 242 MDDRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGM--DRRAENFRVVAYPTARGCAAAYFPETNVLVPLDST 319
Cdd:PRK09939  660 MDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKrsSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNH 739
                         330
                  ....*....|....*..
gi 2574422656 320 AARSNTPTSKSLIIRLE 336
Cdd:PRK09939  740 DPLSGIPGYKSIPVELE 756
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
23-337 3.65e-46

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 166.17  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  23 GTIRAMRDG---RVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVtgrAALILPALGRTEI-DVqaag 98
Cdd:COG0243   354 LTGEAILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERdDI---- 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  99 pqQVSVEDSmgMVHASRGGLAPAGpGLRSEVAIVCGVAAAtLAGQPEVAESGTADRVglagdyrrIRAHIARVVPGFTDY 178
Cdd:COG0243   427 --VTNSEDR--RVHLSRPAVEPPG-EARSDWEIFAELAKR-LGFEEAFPWGRTEEDY--------LRELLEATRGRGITF 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 179 EAgLAELGGFPLPHPP----RDSRTFPTPSGRAALTVNTCEVLRVP--------------PGHLLLQTVRSHDQYNTTIY 240
Cdd:COG0243   493 EE-LREKGPVQLPVPPepafRNDGPFPTPSGKAEFYSETLALPPLPryappyegaepldaEYPLRLITGRSRDQWHSTTY 571
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 241 GMDdrYRGVRRGRRVVFVHPDDLDDLGIADGthvDLVGVWTD-GmdrRAENFRVVAYPTARGCAAAYF-----------P 308
Cdd:COG0243   572 NNP--RLREIGPRPVVEINPEDAAALGIKDG---DLVRVESDrG---EVLARAKVTEGIRPGVVFAPHgwwyepaddkgG 643
                         330       340
                  ....*....|....*....|....*....
gi 2574422656 309 ETNVLVPlDSTAARSNTPTSKSLIIRLEA 337
Cdd:COG0243   644 NVNVLTP-DATDPLSGTPAFKSVPVRVEK 671
 
Name Accession Description Interval E-value
Fdhalpha-like TIGR01701
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ...
7-337 2.31e-120

oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.


Pssm-ID: 273765 [Multi-domain]  Cd Length: 743  Bit Score: 363.36  E-value: 2.31e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:TIGR01701 416 QIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRSHVLAKEEALILPV 495
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGQPEVAESgtadrvgLAGDYRRIRA 166
Cdd:TIGR01701 496 LGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEI-------LVDTYDQIRD 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 167 HIARVVPGFTDYEAGLAELGGFPLPHPPRDSRTFPTPSGRAALTVNTCEVLRVPPGH---LLLQTVRSHDQYNTTIYGMD 243
Cdd:TIGR01701 569 AIAATNPGYDDINHRKRRPDGFQLPGAALCERKFPTPDGKANFIVIPLPEFRVPTGHefeLVLVTLRSHDQFNTTIYGED 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 244 DRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGMDRRAENFRVVAYPTARGCAAAYFPETNVLVPLDSTAARS 323
Cdd:TIGR01701 649 DRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLPLDHHDPQS 728
                         330
                  ....*....|....
gi 2574422656 324 NTPTSKSLIIRLEA 337
Cdd:TIGR01701 729 KTPEYKTIPVRLEA 742
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
7-207 1.06e-75

The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239168 [Multi-domain]  Cd Length: 574  Bit Score: 242.98  E-value: 1.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:cd02767   379 EVFGFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPC 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGqpEVAESGtadrvGLAGDYRRIRA 166
Cdd:cd02767   459 LGRTEIDMQAGGAQAVTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGE--AKPEWE-----ILVEDYDRIRD 531
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2574422656 167 HIARVVP-GFTDYEAGLAELGGFPLPHPPRDsRTFPTPSGRA 207
Cdd:cd02767   532 EIAAVIYeGFADFNQRGDQPGGFHLPNGARE-RKFNTPSGKA 572
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
7-336 8.56e-73

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 239.56  E-value: 8.56e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656   7 AEFAFTPPRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVTGRAALILPA 86
Cdd:PRK09939  430 ERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPV 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  87 LGRTEIDVQAAGPQQVSVEDSMGMVHASRGGLAPAGPGLRSEVAIVCGVAAATLAGQPEVAESgtadrvgLAGDYRRIRA 166
Cdd:PRK09939  510 LGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEY-------LVEDYDRIRN 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 167 HIARVVPGFTDYEAGLAELGGFPLPHPPRDSRtFPTPSGRAALTvnTCEVLRVPP-----GHLLLQTVRSHDQYNTTIYG 241
Cdd:PRK09939  583 DIEAVLPEFADYNQRIRHPGGFHLINAAAERR-WMTPSGKANFI--TSKGLLEDPssafnSKLVMATVRSHDQYNTTIYG 659
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 242 MDDRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGM--DRRAENFRVVAYPTARGCAAAYFPETNVLVPLDST 319
Cdd:PRK09939  660 MDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKrsSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNH 739
                         330
                  ....*....|....*..
gi 2574422656 320 AARSNTPTSKSLIIRLE 336
Cdd:PRK09939  740 DPLSGIPGYKSIPVELE 756
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
23-337 3.65e-46

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 166.17  E-value: 3.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  23 GTIRAMRDG---RVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVQVSTTLNRSHVVtgrAALILPALGRTEI-DVqaag 98
Cdd:COG0243   354 LTGEAILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERdDI---- 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  99 pqQVSVEDSmgMVHASRGGLAPAGpGLRSEVAIVCGVAAAtLAGQPEVAESGTADRVglagdyrrIRAHIARVVPGFTDY 178
Cdd:COG0243   427 --VTNSEDR--RVHLSRPAVEPPG-EARSDWEIFAELAKR-LGFEEAFPWGRTEEDY--------LRELLEATRGRGITF 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 179 EAgLAELGGFPLPHPP----RDSRTFPTPSGRAALTVNTCEVLRVP--------------PGHLLLQTVRSHDQYNTTIY 240
Cdd:COG0243   493 EE-LREKGPVQLPVPPepafRNDGPFPTPSGKAEFYSETLALPPLPryappyegaepldaEYPLRLITGRSRDQWHSTTY 571
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 241 GMDdrYRGVRRGRRVVFVHPDDLDDLGIADGthvDLVGVWTD-GmdrRAENFRVVAYPTARGCAAAYF-----------P 308
Cdd:COG0243   572 NNP--RLREIGPRPVVEINPEDAAALGIKDG---DLVRVESDrG---EVLARAKVTEGIRPGVVFAPHgwwyepaddkgG 643
                         330       340
                  ....*....|....*....|....*....
gi 2574422656 309 ETNVLVPlDSTAARSNTPTSKSLIIRLEA 337
Cdd:COG0243   644 NVNVLTP-DATDPLSGTPAFKSVPVRVEK 671
MopB_CT_ydeP cd02787
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ...
224-335 2.11e-42

The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239188 [Multi-domain]  Cd Length: 112  Bit Score: 142.80  E-value: 2.11e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656 224 LLLQTVRSHDQYNTTIYGMDDRYRGVRRGRRVVFVHPDDLDDLGIADGTHVDLVGVWTDGMDRRAENFRVVAYPTARGCA 303
Cdd:cd02787     1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2574422656 304 AAYFPETNVLVPLDSTAARSNTPTSKSLIIRL 335
Cdd:cd02787    81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
14-209 3.36e-06

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239155 [Multi-domain]  Cd Length: 565  Bit Score: 48.76  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  14 PRRHGFDAVGTIRAMRDGRVRVFLGMGGNFVAASPDTAVTEAAMRSCRLTVqVSTTLNRShvVTGRAA-LILPALGRTEI 92
Cdd:cd02754   371 PPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV-VQDAFADT--ETAEYAdLVLPAASWGEK 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2574422656  93 DvqaaGpqqvSVEDSMGMVHASRGGLAPAGpGLRSEVAIVCGVAAAtlAGQPEV-AESGTADrvglagdyrrIRAHIARV 171
Cdd:cd02754   448 E----G----TMTNSERRVSLLRAAVEPPG-EARPDWWILADVARR--LGFGELfPYTSPEE----------VFEEYRRL 506
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2574422656 172 VPG----FTDYEAGLAELGGFPLPHPPRDSRT---------FPTPSGRAAL 209
Cdd:cd02754   507 SRGrgadLSGLSYERLRDGGVQWPCPDGPPEGtrrlfedgrFPTPDGRARF 557
 
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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