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Conserved domains on  [gi|227484201|emb|CAY20684|]
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dissimilatory sulfite reductase alpha subunit, partial [bacterium enrichment culture clone Dan60S_dsr23E]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dsrA super family cl37041
sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes ...
 21-283 5.79e-133

sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the alpha subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


The actual alignment was detected with superfamily member TIGR02064:

Pssm-ID: 273948 [Multi-domain]  Cd Length: 402  Bit Score: 382.26  E-value: 5.79e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484201  260 VGATILVGAKAPILEGAQLGSVVI 283
Cdd:TIGR02064 294 RGVTILIGGKAPILDGAQMGWVVV 317
 
Name Accession Description Interval E-value
dsrA TIGR02064
sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes ...
 21-283 5.79e-133

sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the alpha subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273948 [Multi-domain]  Cd Length: 402  Bit Score: 382.26  E-value: 5.79e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484201  260 VGATILVGAKAPILEGAQLGSVVI 283
Cdd:TIGR02064 294 RGVTILIGGKAPILDGAQMGWVVV 317
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 106-195 2.69e-26

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 100.81  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  106 GSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCVAAIARaDCSIIGTWRDKIRId 185
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHAN-DIGFVGVWKDGGEI- 78

                          90
                  ....*....|
gi 227484201  186 qeAVRAYVGG 195
Cdd:pfam01077  79 --GFNILVGG 86
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 215-251 6.25e-09

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 51.59  E-value: 6.25e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227484201 215 KEVIDLCPTKCMEWDGKNLKIWDEDCTRCMHCINVMP 251
Cdd:COG2221   21 GLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCP 57
 
Name Accession Description Interval E-value
dsrA TIGR02064
sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes ...
 21-283 5.79e-133

sulfite reductase, dissimilatory-type alpha subunit; Dissimilatory sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide, as the terminal reaction in dissimilatory sulfate reduction. It remains unclear however, whether trithionate and thiosulfate serve as intermediate compounds to sulfide, or as end products of sulfite reduction. Sulfite reductase is a multisubunit enzyme composed of dimers of either alpha/beta or alpha/beta/gamma subunits, each containing a siroheme and iron sulfur cluster prosthetic center. Found in sulfate-reducing bacteria, these genes are commonly located in an unidirectional gene cluster. This model describes the alpha subunit of sulfite reductase. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 273948 [Multi-domain]  Cd Length: 402  Bit Score: 382.26  E-value: 5.79e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484201  260 VGATILVGAKAPILEGAQLGSVVI 283
Cdd:TIGR02064 294 RGVTILIGGKAPILDGAQMGWVVV 317
NIR_SIR pfam01077
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ...
 106-195 2.69e-26

Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.


Pssm-ID: 426031 [Multi-domain]  Cd Length: 153  Bit Score: 100.81  E-value: 2.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  106 GSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCVAAIARaDCSIIGTWRDKIRId 185
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHAN-DIGFVGVWKDGGEI- 78

                          90
                  ....*....|
gi 227484201  186 qeAVRAYVGG 195
Cdd:pfam01077  79 --GFNILVGG 86
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 215-251 6.25e-09

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 51.59  E-value: 6.25e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227484201 215 KEVIDLCPTKCMEWDGKNLKIWDEDCTRCMHCINVMP 251
Cdd:COG2221   21 GLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCP 57
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 49-166 8.88e-04

Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439925 [Multi-domain]  Cd Length: 519  Bit Score: 40.49  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  49 STEVLRKICDIWEEKGSG---LTN-----MHGstgdmILLgtttDQLEPIFYELtHELGMD-LGGSGSNMRTPSCCV--G 117
Cdd:COG0155   67 TPEQLRALADIAREYGRGylhLTTrqniqLHW-----ILL----EDLPEILREL-AEVGLTtIGACGDVVRNVTASPlaG 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 227484201 118 KARCEwsCIDTQDITYDITMRYQDElhrPMF---PYKFKFKTSGCPNNCVAA 166
Cdd:COG0155  137 VDPDE--LFDVRPYAEAISQHLLGH---PEYtylPRKFKIAFSGPPEDDADV 183
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 49-195 3.08e-03

Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439925 [Multi-domain]  Cd Length: 519  Bit Score: 38.95  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484201  49 STEVLRKICDIWEEKGSG---LTNMHGstgdMILLGTTTDQLEPIfYELTHELGMDLGGSGSnMRTPSCCVGKARCEWSC 125
Cdd:COG0155  318 TDEQLRALADLAERYGSGeirLTPNQN----LILADVPEEDLPAL-EAALRALGLATPPSGL-RRDSIACPGLPTCKLAI 391

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227484201 126 IDTQDITYDITMRYQDELHRPMFPYKFKFKTSGCPNNCvaaiAR---ADCSIIGTWRDKIRidqEAVRAYVGG 195
Cdd:COG0155  392 AESKRLAPALADRLEEDLDGLHDDEPIRIRISGCPNSC----GRhyiADIGLVGKAKKGVV---EAYQLYLGG 457
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
218-251 3.31e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 35.48  E-value: 3.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 227484201 218 IDLCPTKCMEWDGKNLKIWDEDCTRCMHCINVMP 251
Cdd:COG2768   20 VKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCP 53
NIR_SIR_ferr pfam03460
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ...
 36-94 6.26e-03

Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.


Pssm-ID: 377044 [Multi-domain]  Cd Length: 67  Bit Score: 34.43  E-value: 6.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227484201   36 HTMRVNQPASKFySTEVLRKICDIWEEKGSG---LTnmhgSTGDMILLGTTTDQLEPIFYEL 94
Cdd:pfam03460   8 YMVRVRVPGGRL-TAEQLRALADIAEKYGDGeirLT----TRQNLELHGVPEEDLPELLEEL 64
 
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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