NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1147707874|dbj|BAW98817|]
View 

periplasmic nitrate reductase, large subunit, partial [Sulfurimonas sp. M59]

Protein Classification

molybdopterin-binding domain-containing protein( domain architecture ID 172)

molybdopterin-binding domain-containing protein belongs to a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Molybdopterin-Binding super family cl09928
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 1-214 1.56e-153

Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.


The actual alignment was detected with superfamily member PRK13532:

Pssm-ID: 447860 [Multi-domain]  Cd Length: 830  Bit Score: 446.27  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:PRK13532   96 DRLTQPLLRMKD-GKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNID 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:PRK13532  175 PNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPD-VKVAVLSTFEHRSFEL 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNHPesIDWDFIKKNIIFAAGPVNIGYGFR 214
Cdd:PRK13532  254 ADNGIIFTPQTDLAILNYIANYIIQNNA--VNWDFVNKHTNFRKGATDIGYGLR 305
 
Name Accession Description Interval E-value
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
1-214 1.56e-153

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 446.27  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:PRK13532   96 DRLTQPLLRMKD-GKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNID 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:PRK13532  175 PNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPD-VKVAVLSTFEHRSFEL 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNHPesIDWDFIKKNIIFAAGPVNIGYGFR 214
Cdd:PRK13532  254 ADNGIIFTPQTDLAILNYIANYIIQNNA--VNWDFVNKHTNFRKGATDIGYGLR 305
NAPA TIGR01706
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a ...
 1-214 6.02e-126

periplasmic nitrate reductase, large subunit; This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase. The enzymes from Alicagenes eutrophus and Paracoccus pantotrophus have been characterized. In E. coli (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC). [Energy metabolism, Aerobic, Energy metabolism, Electron transport, Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 273766 [Multi-domain]  Cd Length: 830  Bit Score: 375.35  E-value: 6.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:TIGR01706  96 DRLTQPLLRMKD-GKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKGPTAIGMFGSGQWTIWEGYAALKLMKAGFRSNNID 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:TIGR01706 175 PNARHCMASAVVGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPK-VKVVVLSTFTHRSFDL 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNHpeSIDWDFIKKNIIFAAGPVNIGYGFR 214
Cdd:TIGR01706 254 ADIGIIFKPQTDLAILNYIANYIIQNN--AVNMDFVNKHTVFKTGATDIGYGLR 305
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 1-198 1.08e-90

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: 277.18  E-value: 1.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:cd02754    53 ERLTRPLLRRNG-------GELVPVSWDEALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNID 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:cd02754   126 TNSRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKANPG-AKIIVVDPRRTRTADI 204

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKK 198
Cdd:cd02754   205 ADLHLPIRPGTDLALLNGLLHVLIEE--GLIDRDFIDA 240
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
1-199 1.03e-59

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 198.53  E-value: 1.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASG----QYTIMEGYAAQKMMKAgFRS 76
Cdd:COG0243    77 DRLTYPMKRVGPRGS----GKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARA-LGT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  77 NAIDPNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPdrVKVVNIQTYTHR 156
Cdd:COG0243   152 NNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG--AKIVVIDPRRTE 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1147707874 157 TCDLGDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKKN 199
Cdd:COG0243   230 TAAIADEWLPIRPGTDAALLLALAHVLIEE--GLYDRDFLARH 270
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
2-184 1.83e-31

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 117.89  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLLRVNDkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAV-FASGQYTIME-GYAAQKMMKAGFRSNA- 78
Cdd:pfam00384   1 RLKYPMVRRGD-------GKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTDVEsLYALKKLLNRLGSKNGn 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  79 -IDPNARHCMASAvvgfyQTFGIDEPSG-----CYDDIELTDTIVTWGSNMAEMHPILWSRvTDRKLSDPDrVKVVNIQT 152
Cdd:pfam00384  74 tEDHNGDLCTAAA-----AAFGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNAR-IRKAALKGK-AKVIVIGP 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1147707874 153 YTHRTCDlgDFNIIFRPNTDLALWNYLAREIV 184
Cdd:pfam00384 147 RLDLTYA--DEHLGIKPGTDLALALAGAHVFI 176
 
Name Accession Description Interval E-value
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
1-214 1.56e-153

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 446.27  E-value: 1.56e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:PRK13532   96 DRLTQPLLRMKD-GKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNID 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:PRK13532  175 PNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPD-VKVAVLSTFEHRSFEL 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNHPesIDWDFIKKNIIFAAGPVNIGYGFR 214
Cdd:PRK13532  254 ADNGIIFTPQTDLAILNYIANYIIQNNA--VNWDFVNKHTNFRKGATDIGYGLR 305
NAPA TIGR01706
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a ...
 1-214 6.02e-126

periplasmic nitrate reductase, large subunit; This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase. The enzymes from Alicagenes eutrophus and Paracoccus pantotrophus have been characterized. In E. coli (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC). [Energy metabolism, Aerobic, Energy metabolism, Electron transport, Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 273766 [Multi-domain]  Cd Length: 830  Bit Score: 375.35  E-value: 6.02e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:TIGR01706  96 DRLTQPLLRMKD-GKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKGPTAIGMFGSGQWTIWEGYAALKLMKAGFRSNNID 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:TIGR01706 175 PNARHCMASAVVGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPK-VKVVVLSTFTHRSFDL 253

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNHpeSIDWDFIKKNIIFAAGPVNIGYGFR 214
Cdd:TIGR01706 254 ADIGIIFKPQTDLAILNYIANYIIQNN--AVNMDFVNKHTVFKTGATDIGYGLR 305
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
 1-198 1.08e-90

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: 277.18  E-value: 1.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:cd02754    53 ERLTRPLLRRNG-------GELVPVSWDEALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNID 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCDL 160
Cdd:cd02754   126 TNSRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKANPG-AKIIVVDPRRTRTADI 204

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKK 198
Cdd:cd02754   205 ADLHLPIRPGTDLALLNGLLHVLIEE--GLIDRDFIDA 240
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
1-199 1.03e-59

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


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 198.53  E-value: 1.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASG----QYTIMEGYAAQKMMKAgFRS 76
Cdd:COG0243    77 DRLTYPMKRVGPRGS----GKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARA-LGT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  77 NAIDPNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPdrVKVVNIQTYTHR 156
Cdd:COG0243   152 NNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG--AKIVVIDPRRTE 229

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1147707874 157 TCDLGDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKKN 199
Cdd:COG0243   230 TAAIADEWLPIRPGTDAALLLALAHVLIEE--GLYDRDFLARH 270
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
1-198 6.99e-57

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 191.25  E-value: 6.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRvndkgefdKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:COG3383    60 DRLTTPLIR--------RGGEFREVSWDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNID 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPdrvKVVNIQTYTHRTCDL 160
Cdd:COG3383   132 NNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGA---KLIVVDPRRTETARL 208

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKK 198
Cdd:COG3383   209 ADLHLQIKPGTDLALLNGLLHVIIEE--GLVDEDFIAE 244
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
 1-177 6.20e-45

Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.


Pssm-ID: 238218 [Multi-domain]  Cd Length: 374  Bit Score: 153.64  E-value: 6.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMkAGFRSNAID 80
Cdd:cd00368    53 DRLKYPLIRVG------GRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL-RALGSNNVD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGfYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDpdrVKVVNIQTYTHRTCDL 160
Cdd:cd00368   126 SHARLCHASAVAA-LKAFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRG---AKLIVIDPRRTETAAK 201

                         170
                  ....*....|....*..
gi 1147707874 161 GDFNIIFRPNTDLALWN 177
Cdd:cd00368   202 ADEWLPIRPGTDAALAL 218
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
 1-199 2.07e-39

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239154 [Multi-domain]  Cd Length: 512  Bit Score: 141.58  E-value: 2.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRvndkgefdKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:cd02753    53 DRLTKPLIR--------KNGKFVEASWDEALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVD 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDpdrVKVVNIQTYTHRTCDL 160
Cdd:cd02753   125 HCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNG---AKLIVADPRRTELARF 201

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1147707874 161 GDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKKN 199
Cdd:cd02753   202 ADLHLQLRPGTDVALLNAMAHVIIEE--GLYDEEFIEER 238
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
2-184 1.83e-31

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 117.89  E-value: 1.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLLRVNDkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAV-FASGQYTIME-GYAAQKMMKAGFRSNA- 78
Cdd:pfam00384   1 RLKYPMVRRGD-------GKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTDVEsLYALKKLLNRLGSKNGn 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  79 -IDPNARHCMASAvvgfyQTFGIDEPSG-----CYDDIELTDTIVTWGSNMAEMHPILWSRvTDRKLSDPDrVKVVNIQT 152
Cdd:pfam00384  74 tEDHNGDLCTAAA-----AAFGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNAR-IRKAALKGK-AKVIVIGP 146

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1147707874 153 YTHRTCDlgDFNIIFRPNTDLALWNYLAREIV 184
Cdd:pfam00384 147 RLDLTYA--DEHLGIKPGTDLALALAGAHVFI 176
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
 1-203 9.57e-21

The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239167 [Multi-domain]  Cd Length: 501  Bit Score: 89.62  E-value: 9.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFA-SGQYTIMEGYAAQKMMKAGFRSNAI 79
Cdd:cd02766    54 DRLLTPLKRVGRKG-----GQWERISWDEALDTIAAKLKEIKAEYGPESILPYSyAGTMGLLQRAARGRFFHALGASELR 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  80 DPnarHCMASAVVGFYQTFGiDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKlsdpDR-VKVVNIQTYTHRTC 158
Cdd:cd02766   129 GT---ICSGAGIEAQKYDFG-ASLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEAR----KRgAKVVVIDPYRTATA 200

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1147707874 159 DLGDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKKNIIFA 203
Cdd:cd02766   201 ARADLHIQIRPGTDGALALGVAKVLFRE--GLYDRDFLARHTEGF 243
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
 1-191 6.87e-17

Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239153 [Multi-domain]  Cd Length: 649  Bit Score: 78.98  E-value: 6.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGefdkkgKFAPISWKRAYDEME---KNIRKA-LKEK--------GPEGVAVFASGQYTIMEGYAAQK 68
Cdd:cd02752    53 KRLKYPMYRAPGSG------KWEEISWDEALDEIArkmKDIRDAsFVEKnaagvvvnRPDSIAFLGSAKLSNEECYLIRK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  69 MMKAgFRSNAIDPNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDRVKVV 148
Cdd:cd02752   127 FARA-LGTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVV 205

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1147707874 149 NIQtYThRTCDLGDFNIIFRPNTDLALWNYLAREIVYNHPESI 191
Cdd:cd02752   206 DPR-FT-RTAAKADLYVPIRSGTDIAFLGGMINYIIRYTPEEV 246
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 2-199 2.69e-15

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: 74.27  E-value: 2.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLLRvnDKGEfdkkGKFAPISWKRAYDEmeknIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKAgFRSNAIDP 81
Cdd:cd02767    64 RLTYPMRY--DAGS----DHYRPISWDEAFAE----IAARLRALDPDRAAFYTSGRASNEAAYLYQLFARA-YGTNNLPD 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  82 NARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKlsdpDR-VKVVNIQTY------- 153
Cdd:cd02767   133 CSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAK----KRgGKIIVINPLrepgler 208

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874 154 -----------THRTcDLGDFNIIFRPNTDLALWNYLAREIVYNHPES---IDWDFIKKN 199
Cdd:cd02767   209 fanpqnpesmlTGGT-KIADEYFQVRIGGDIALLNGMAKHLIERDDEPgnvLDHDFIAEH 267
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
 1-186 5.92e-15

The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239156 [Multi-domain]  Cd Length: 454  Bit Score: 73.10  E-value: 5.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGqyTIMEGYAAQKMmkAGFRSNAID 80
Cdd:cd02755    54 DRLKKPLIRVGERGE----GKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHG--GCYSPFFKHFA--AAFGSPNIF 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGcYDDIELTDTIVTWGSNMAE-MHPILWSRVTDRKLSDpdrVKVVNIQTYTHRTCD 159
Cdd:cd02755   126 SHESTCLASKNLAWKLVIDSFGGEV-NPDFENARYIILFGRNLAEaIIVVDARRLMKALENG---AKVVVVDPRFSELAS 201

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1147707874 160 LGDFNIIFRPNTD----LALWNYLAREIVYN 186
Cdd:cd02755   202 KADEWIPIKPGTDlafvLALIHVLISENLYD 232
MopB_Arsenate-R cd02757
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ...
 1-193 6.26e-14

This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239158 [Multi-domain]  Cd Length: 523  Bit Score: 70.16  E-value: 6.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFAsGQYTIMEGYAAQKMMKAgfrsNAID 80
Cdd:cd02757    55 DRILYPMKRTNPRKGRDVDPKFVPISWDEALDTIADKIRALRKENEPHKIMLHR-GRYGHNNSILYGRFTKM----IGSP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARH---CMASAVVGFYQT---FGIDEPsgcydDIELTDTIVTWGSN-MAEMHPI-LWSRVTDRKLsdpDRVKVVNIQT 152
Cdd:cd02757   130 NNISHssvCAESEKFGRYYTeggWDYNSY-----DYANAKYILFFGADpLESNRQNpHAQRIWGGKM---DQAKVVVVDP 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1147707874 153 YTHRTCDLGDFNIIFRPNTD----LALWNYLAREIVYNHPESIDW 193
Cdd:cd02757   202 RLSNTAAKADEWLPIKPGEDgalaLAIAHVILTEGLWDKDFVGDF 246
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
 1-198 1.14e-13

This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239171 [Multi-domain]  Cd Length: 617  Bit Score: 69.27  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAV-FASGQYtimeGYAAQKMMKAGFRSNAI 79
Cdd:cd02770    58 DRLKYPMKRVGKRGE----GKFVRISWDEALDTIASELKRIIEKYGNEAIYVnYGTGTY----GGVPAGRGAIARLLNLT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  80 DPNARH----CMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDRVKVVNIQ-TYT 154
Cdd:cd02770   130 GGYLNYygtySWAQITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAKKAGAKFIVIDpRYT 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1147707874 155 HRTCDLGDFNIIFRPNTDLALWNYLAREIVYNHPesIDWDFIKK 198
Cdd:cd02770   210 DTAVTLADEWIPIRPGTDAALVAAMAYVMITENL--HDQAFLDR 251
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
 1-199 1.52e-12

The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239166 [Multi-domain]  Cd Length: 567  Bit Score: 65.96  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVF-ASGQYTIMeGYAAQKMMKAGFRSN-- 77
Cdd:cd02765    54 DRLKYPMKRVGERGE----GKFERITWDEALDTIADKLTEAKREYGGKSILWMsSSGDGAIL-SYLRLALLGGGLQDAlt 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  78 -AIDPNARHCMaSAVVGFYQTFGIDEPsgcyDDIELTDTIVTWGSNMAEMHpilwsrVTD-RKLSDPDR--VKVVNIQTY 153
Cdd:cd02765   129 yGIDTGVGQGF-NRVTGGGFMPPTNEI----TDWVNAKTIIIWGSNILETQ------FQDaEFFLDAREngAKIVVIDPV 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1147707874 154 THRTCDLGDFNIIFRPNTD----LALWNYLAREIVYNHPesidwdFIKKN 199
Cdd:cd02765   198 YSTTAAKADQWVPIRPGTDpalaLGMINYILEHNWYDEA------FLKSN 241
MopB_Arsenite-Ox cd02756
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ...
 1-192 3.05e-12

Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239157 [Multi-domain]  Cd Length: 676  Bit Score: 65.20  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGvAVFAS------GQYTIMEGYAAQKMMKAGF 74
Cdd:cd02756   116 TRLTTPLVRRG--------GQLQPTTWDDAIDLVARVIKGILDKDGNDD-AVFASrfdhggGGGGFENNWGVGKFFFMAL 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  75 RSNAIDPNARHCMASAVVGFYQTfGIDEPSGCYDDIELTDTIVTWGSNMAE---------MHPILWSRVTDRK------- 138
Cdd:cd02756   187 QTPFVRIHNRPAYNSEVHATREM-GVGELNNSYEDARLADTIVLWGNNPYEtqtvyflnhWLPNLRGATVSEKqqwfppg 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147707874 139 -LSDPDRVKVVN---IQTYTHRTCDLGDFNII---FRPNTDLALWNYLAREIVYNHPESID 192
Cdd:cd02756   266 ePVPPGRIIVVDprrTETVHAAEAAAGKDRVLhlqVNPGTDTALANAIARYIYESLDEVLA 326
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
 1-122 1.86e-11

The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239160 [Multi-domain]  Cd Length: 477  Bit Score: 62.71  E-value: 1.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAvFASGqyTIMEGYAAQKMMKAGFRSNAID 80
Cdd:cd02759    53 DRLLYPLKRVGERGE----NKWERISWDEALDEIAEKLAEIKAEYGPESIA-TAVG--TGRGTMWQDSLFWIRFVRLFGS 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1147707874  81 PNARH----C-----MASAVVGFYQTfGIDEPsgcydDIELTDTIVTWGSN 122
Cdd:cd02759   126 PNLFLsgesCywprdMAHALTTGFGL-GYDEP-----DWENPECIVLWGKN 170
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
 1-198 2.49e-11

The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239152 [Multi-domain]  Cd Length: 609  Bit Score: 62.63  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVN------DKGEFDKKGKFAPISWKRAYDEMEKNIRKALKEKGPEgvAVFAsGQYTIMEGY---AAQKMMK 71
Cdd:cd02751    46 DRIKYPMKRVGwlgngpGSRELRGEGEFVRISWDEALDLVASELKRIREKYGNE--AIFG-GSYGWASAGrlhHAQSLLH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  72 -----AGFRSNAIDPnarHCMASAVVGFYQTFGIDEPSGCY---DDI-ELTDTIVTWGSNMAEMHPILWSRVTD------ 136
Cdd:cd02751   123 rflnlIGGYLGSYGT---YSTGAAQVILPHVVGSDEVYEQGtswDDIaEHSDLVVLFGANPLKTRQGGGGGPDHgsyyyl 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147707874 137 RKLSDpDRVKVVNI---QTYTHRTcdLGDFNIIFRPNTDLALWNYLAREIVYNhpESIDWDFIKK 198
Cdd:cd02751   200 KQAKD-AGVRFICIdprYTDTAAV--LAAEWIPIRPGTDVALMLAMAHTLITE--DLHDQAFLAR 259
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
 1-134 1.17e-10

MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239173 [Multi-domain]  Cd Length: 414  Bit Score: 60.45  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMkAGFRSNAID 80
Cdd:cd02772    53 DRLTKPMIKKD--------GQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLA-RGLGSDNID 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1147707874  81 PNARHCMASAVVgfyqTFGIDEPSGC-YDDIELTDTIVTWGSNMAEMHPILWSRV 134
Cdd:cd02772   124 HRLRQSDFRDDA----KASGAPWLGMpIAEISELDRVLVIGSNLRKEHPLLAQRL 174
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
 1-150 6.75e-10

MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.


Pssm-ID: 239169 [Multi-domain]  Cd Length: 386  Bit Score: 58.06  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdkkGKFAPISWKRAydemEKNIRKALKEKGPEGVAVFASGQYTIMEGYAAQKMMKaGFRSNAID 80
Cdd:cd02768    53 QRLTQPLIKKG--------GKLVPVSWEEA----LKTVAEGLKAVKGDKIGGIAGPRADLESLFLLKKLLN-KLGSNNID 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNARHcMASAVVGFYQTFGIDEPSgcYDDIELTDTIVTWGSNMAEMHPILWSRVtdRKLSDPDRVKVVNI 150
Cdd:cd02768   120 HRLRQ-SDLPADNRLRGNYLFNTS--IAEIEEADAVLLIGSNLRKEAPLLNARL--RKAVKKKGAKIAVI 184
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 1-175 2.11e-09

The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239163 [Multi-domain]  Cd Length: 539  Bit Score: 56.64  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAV---------FASGQYTimeGYAAQKMMK 71
Cdd:cd02762    53 DRLRTPMRRRG--------GSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVyggnpqahtHAGGAYS---PALLKALGT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  72 AGFRSNAIDPNARHCMASavvgfYQTFGiDEPSGCYDDIELTDTIVTWGSNMAEMHPILWSrVTDRK-----LSDPDRvK 146
Cdd:cd02762   122 SNYFSAATADQKPGHFWS-----GLMFG-HPGLHPVPDIDRTDYLLILGANPLQSNGSLRT-APDRVlrlkaAKDRGG-S 193

                         170       180
                  ....*....|....*....|....*....
gi 1147707874 147 VVNIQTYTHRTCDLGDFNIIFRPNTDLAL 175
Cdd:cd02762   194 LVVIDPRRTETAKLADEHLFVRPGTDAWL 222
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
 1-180 6.69e-09

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 55.42  E-value: 6.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAV-FASGQY--TIMEGYAAQKMMKAGFRS- 76
Cdd:PRK14990  118 DRLKYPMKRVGARGE----GKFERISWEEAYDIIATNMQRLIKEYGNESIYLnYGTGTLggTMTRSWPPGNTLVARLMNc 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  77 --NAIDPNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMH----PILWSRVTDRKLSDPdRVKVVNI 150
Cdd:PRK14990  194 cgGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRmsggGVTYYLEQARQKSNA-RMIIIDP 272

                         170       180       190
                  ....*....|....*....|....*....|
gi 1147707874 151 QtYTHRTCDLGDFNIIFRPNTDLALWNYLA 180
Cdd:PRK14990  273 R-YTDTGAGREDEWIPIRPGTDAALVNGLA 301
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
 1-156 4.27e-08

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 53.03  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRvndkgefDKKGKFAPISWKRAYDEMEKNIRKALkekgpEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:PRK07860  277 DRITTPLVR-------DEDGELEPASWSEALAVAARGLAAAR-----GRVGVLVGGRLTVEDAYAYAKFARVALGTNDID 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  81 PNAR-------HCMASAVVGfyQTFGIDepsgcYDDIELTDTIVTWGSNMAEMHPILWSRVtdRKLSDPDRVKVVNIQTY 153
Cdd:PRK07860  345 FRARphsaeeaDFLAARVAG--RGLGVT-----YADLEKAPAVLLVGFEPEEESPIVFLRL--RKAARKHGLKVYSIAPF 415


                  ...
gi 1147707874 154 THR 156
Cdd:PRK07860  416 ATR 418
MopB_NDH-1_NuoG2-N7 cd02771
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ...
 1-134 8.00e-08

MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239172 [Multi-domain]  Cd Length: 472  Bit Score: 52.01  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNdkgefdkkGKFAPISWkrayDEMEKNIRKALKEKGpEGVAVFASGQYTIMEGYAAQKMMKAGFRSNAID 80
Cdd:cd02771    53 DRLTQPLIRRG--------GTLVPVSW----NEALDVAAARLKEAK-DKVGGIGSPRASNESNYALQKLVGAVLGTNNVD 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1147707874  81 PNARHCMASAVvgfyQTFGIDEPSgcYDDIELTDTIVTWGSNMAEMHPILWSRV 134
Cdd:cd02771   120 HRARRLIAEIL----RNGPIYIPS--LRDIESADAVLVLGEDLTQTAPRIALAL 167
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
 2-198 2.77e-07

The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239164 [Multi-domain]  Cd Length: 679  Bit Score: 50.60  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIrKALKEKGPEGVAVFAS-GQYTIMEGYAAQKM------MKAGF 74
Cdd:cd02763    54 RLTKPLLRKGPRGS----GQFEEIEWEEAFSIATKRL-KAARATDPKKFAFFTGrDQMQALTGWFAGQFgtpnyaAHGGF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  75 RSnaidPNARHCMASAVVGFYQTFGidEPsgcydDIELTDTIVTWGsnMAEMHPilwSRVTDRKLSDPDRV--KVVNIQT 152
Cdd:cd02763   129 CS----VNMAAGGLYSIGGSFWEFG--GP-----DLEHTKYFMMIG--VAEDHH---SNPFKIGIQKLKRRggKFVAVNP 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1147707874 153 YTHRTCDLGDFNIIFRPNTDLALWNYLAREIVynHPESIDWDFIKK 198
Cdd:cd02763   193 VRTGYAAIADEWVPIKPGTDGAFILALAHELL--KAGLIDWEFLKR 236
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
 2-198 2.85e-07

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 50.44  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFA-SGQ-YTIMEGYAaqkmmkAGFRSNAI 79
Cdd:PRK15488   98 RIVKPLKRVGERGE----GKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSkSGSlSSHLFHLA------TAFGSPNT 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  80 DPNARHCMASAVVGFYQTFGIDEPSgcydDIELTDTIVTWGSNMAEMHPILWSRVTDRKLSDPDrVKVVNIQTYTHRTCD 159
Cdd:PRK15488  168 FTHASTCPAGYAIAAKVMFGGKLKR----DLANSKYIINFGHNLYEGINMSDTRGLMTAQMEKG-AKLVVFEPRFSVVAS 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1147707874 160 LGDFNIIFRPNTD----LALWNYLAREIVYnhpesiDWDFIKK 198
Cdd:PRK15488  243 KADEWHAIRPGTDlavvLALCHVLIEENLY------DKAFVER 279
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
 1-198 5.12e-07

Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239151 [Multi-domain]  Cd Length: 461  Bit Score: 49.62  E-value: 5.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   1 DRLTQPLLRVNDKGEfdkkGKFAPISWKRAYDEMEKNIRKALKEKGPEGVAVFASGQYTIMEGYAA-QKMMK--AGFRSN 77
Cdd:cd02750    65 DRVKYPLKRVGARGE----GKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAgSRFASliGGVSLS 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874  78 AIDPNARHCMASavvgfYQTFGI--DEPSgcYDDIELTDTIVTWGSNmaemhpILWSRVTDRKLSDPDR---VKVVNIQT 152
Cdd:cd02750   141 FYDWYGDLPPGS-----PQTWGEqtDVPE--SADWYNADYIIMWGSN------VPVTRTPDAHFLTEARyngAKVVVVSP 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1147707874 153 YTHRTCDLGDFNIIFRPNTDLALWNYLAREIVYNHpeSIDWDFIKK 198
Cdd:cd02750   208 DYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEK--LYDEDYLKE 251
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
2-128 4.74e-05

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 43.88  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147707874   2 RLTQPLlrvndkgEFDKKGK-FAPISWKRAYDEMEKNIRKAlkeKGPEGVAVFASGQyTIMEGYAAQKMMKAGFRSNAID 80
Cdd:PRK09939  108 RLTQPL-------KYDAVSDcYKPLSWQQAFDEIGARLQSY---SDPNQVEFYTSGR-TSNEAAFLYQLFAREYGSNNFP 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1147707874  81 PNARHCMASAVVGFYQTFGIDEPSGCYDDIELTDTIVTWGSNMAEMHP 128
Cdd:PRK09939  177 DCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHP 224
MopB_Phenylacetyl-CoA-OR cd02760
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ...
 1-46 1.61e-03

The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239161 [Multi-domain]  Cd Length: 760  Bit Score: 39.18  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1147707874   1 DRLTQPLLRVNDKGEFDKKGKFAPISWKRAYDEMEKNIRkALKEKG 46
Cdd:cd02760    57 NRVLQPMKRTNPKKGRNEDPGFVPISWDEALDLVAAKLR-RVREKG 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH