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Conserved domains on  [gi|227484197|emb|CAY20680|]
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dissimilatory sulfite reductase alpha subunit, partial [bacterium enrichment culture clone Dan60S_dsr21E]

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 1.11e-132

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: 381.49  E-value: 1.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484197  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 1.11e-132

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: 381.49  E-value: 1.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484197  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 1.23e-24

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: 96.57  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  106 GSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCVAAIARaDCSIIGTWRDKIRId 185
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHAN-DIGFVGVWKDGGEI- 78

                          90
                  ....*....|
gi 227484197  186 qeAVRAYVGG 195
Cdd:pfam01077  79 --GFNILVGG 86
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 215-251 6.07e-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: 6.07e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227484197 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 1.11e-132

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: 381.49  E-value: 1.11e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197   21 RYCDRPDLFPNVAHFHTMRVNQPASKFYSTEVLRKICDIWEEKGSGLTNMHGSTGDMILLGTTTDQLEPIFYELThELGM 100
Cdd:TIGR02064  67 RYSDQGEKFPGVAEFHTVRVAQPSGKFYSTDYLRQLCDVWEKYGSGLTNFHGQTGDIVFLGTQTPQLQEIFEELT-NLGT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  101 DLGGSGSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCVAAIARADCSIIGTWRD 180
Cdd:TIGR02064 146 DLGGSGSNLRTPESCVGPARCEFACYDTLKACYELTMEYQDELHRPAFPYKFKFKFSGCPNDCVAAIARSDFAVIGTWKD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  181 KIRIDQEAVRAYVGGelvpnggahgteKRALDIQKEVIDLCPTKCMEWDGKN-LKIWDEDCTRCMHCINVMPRALRPGQD 259
Cdd:TIGR02064 226 DIKVDQEAVKAYIAG------------WGKFDIENEVVNRCPTKAISWDGSKeLSIDNRECVRCMHCINKMPKALHPGDE 293

                         250       260
                  ....*....|....*....|....
gi 227484197  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 1.23e-24

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: 96.57  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  106 GSNMRTPSCCVGKARCEWSCIDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCVAAIARaDCSIIGTWRDKIRId 185
Cdd:pfam01077   1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDYGFPYLPRKFKIAVSGCPNNCVAAHAN-DIGFVGVWKDGGEI- 78

                          90
                  ....*....|
gi 227484197  186 qeAVRAYVGG 195
Cdd:pfam01077  79 --GFNILVGG 86
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 215-251 6.07e-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: 6.07e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227484197 215 KEVIDLCPTKCMEWDGKNLKIWDEDCTRCMHCINVMP 251
Cdd:COG2221   21 GLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCP 57
sulfite_red_C TIGR02912
sulfite reductase, subunit C; Members of this protein family include the C subunit, one of ...
 87-176 1.50e-05

sulfite reductase, subunit C; Members of this protein family include the C subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 131958 [Multi-domain]  Cd Length: 314  Bit Score: 45.63  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197   87 LEPIFYELTHEL-GMDLGGSGSNMRTPSCCVGKARCEWSCIDTQdityditmRYQDELHRPMFPYEFKFKT--SGCPNDC 163
Cdd:TIGR02912  77 LQPIIEGLEINQeDVQKGYSASGTRNITACIGNRVCPFANYDTT--------KFAKRIEKAVFPNDYHVKIalTGCPNDC 148

                          90
                  ....*....|...
gi 227484197  164 VAAiARADCSIIG 176
Cdd:TIGR02912 149 AKA-RMHDFGIIG 160
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 49-195 1.13e-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: 40.10  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  49 STEVLRKICDIWEEKGSG---LTNMHGstgdMILLGTTTDQLEPIfYELTHELGMDLGGSGSnMRTPSCCVGKARCEWSC 125
Cdd:COG0155  318 TDEQLRALADLAERYGSGeirLTPNQN----LILADVPEEDLPAL-EAALRALGLATPPSGL-RRDSIACPGLPTCKLAI 391

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227484197 126 IDTQDITYDITMRYQDELHRPMFPYEFKFKTSGCPNDCvaaiAR---ADCSIIGTWRDKIRidqEAVRAYVGG 195
Cdd:COG0155  392 AESKRLAPALADRLEEDLDGLHDDEPIRIRISGCPNSC----GRhyiADIGLVGKAKKGVV---EAYQLYLGG 457
Peptidase_C70 pfam12385
Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in ...
 149-211 1.44e-03

Papain-like cysteine protease AvrRpt2; This is a family of cysteine proteases, found in actinobacteria, protobacteria and firmicutes. Papain-like cysteine proteases play a crucial role in plant-pathogen/pest interactions. On entering the host they act on non-self substrates, thereby manipulating the host to evade proteolysis. AvrRpt2 from Pseudomonas syringae pv. tomato DC3000 triggers resistance to P. syringae-2-dependent defence responses, including hypersensitive cell death, by cleaving the Arabidopsis RIN4 protein which is monitored by the cognate resistance protein RPS2.


Pssm-ID: 403550 [Multi-domain]  Cd Length: 143  Bit Score: 38.21  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227484197  149 PYEFKFKTSGCpndcvaaiARADCSIIGTWRDKIRIDQEAVRAYVGGELVPNGGAHGTEKRAL 211
Cdd:pfam12385   8 PYNVQQAAMGC--------WAASASMIAGYRGQKPIDPSEIAALVPGWSQYDTGLNGPEDIAL 62
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
218-251 3.41e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 35.48  E-value: 3.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 227484197 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 227484197   36 HTMRVNQPASKFySTEVLRKICDIWEEKGSG---LTnmhgSTGDMILLGTTTDQLEPIFYEL 94
Cdd:pfam03460   8 YMVRVRVPGGRL-TAEQLRALADIAEKYGDGeirLT----TRQNLELHGVPEEDLPELLEEL 64
CysI COG0155
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ...
 49-166 9.09e-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: 37.40  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227484197  49 STEVLRKICDIWEEKGSG---LTN-----MHGstgdmILLgtttDQLEPIFYELtHELGMD-LGGSGSNMRTPSCCV--G 117
Cdd:COG0155   67 TPEQLRALADIAREYGRGylhLTTrqniqLHW-----ILL----EDLPEILREL-AEVGLTtIGACGDVVRNVTASPlaG 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 227484197 118 KARCEwsCIDTQDITYDITMRYQDElhrPMFpYEF--KFKT--SGCPNDCVAA 166
Cdd:COG0155  137 VDPDE--LFDVRPYAEAISQHLLGH---PEY-TYLprKFKIafSGPPEDDADV 183
 
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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