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Conserved domains on  [gi|757600339|ref|WP_042847974|]
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MULTISPECIES: tetrathionate reductase subunit TtrB [Providencia]

Protein Classification

PRK14993 family protein( domain architecture ID 11487554)

PRK14993 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-244 1.79e-174

tetrathionate reductase subunit TtrB;


:

Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 479.37  E-value: 1.79e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   1 MDLSKRKFLQQIGAVTAGASLIPIAEAGLNFSPTRREGNPEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  81 YQVAVKGEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 161 FCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKMLTEHEAEIKVLKPESGTLPQVFYLGLDDAFVQPLQGKGQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 757600339 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-244 1.79e-174

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 479.37  E-value: 1.79e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   1 MDLSKRKFLQQIGAVTAGASLIPIAEAGLNFSPTRREGNPEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  81 YQVAVKGEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 161 FCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKMLTEHEAEIKVLKPESGTLPQVFYLGLDDAFVQPLQGKGQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 757600339 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 46-222 2.77e-96

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 279.42  E-value: 2.77e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGFTNvlLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTF--LPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 126 VVDNERCVGCAYCVQACPYDARFIN------------HSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNS 193
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNpeephefgevpvRPKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                        170       180
                 ....*....|....*....|....*....
gi 757600339 194 TIRKMLTEHEAeiKVLKPESGTLPQVFYL 222
Cdd:cd10551  159 EVSKLLAERRA--YVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 40-226 1.69e-85

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 252.17  E-value: 1.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  40 PEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGFTNVllPRLCNHCDNPPCVPVCPVQATFQ 119
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATYK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 120 REDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKML 199
Cdd:COG0437   80 REDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRL 159

                        170       180
                 ....*....|....*....|....*..
gi 757600339 200 TEHEAeiKVLKPESGTLPQVFYLGLDD 226
Cdd:COG0437  160 AELPA--YRLLPELGTKPSVYYLPKRN 184
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 96-188 2.96e-35

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 121.20  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPAC 174
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|....
gi 757600339  175 VESCVGGARIIGDL 188
Cdd:pfam13247  86 VQTCPTGAMNFGDR 99
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 124-178 1.60e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  124 IVVVDNERCVGCAYCVQACPYDA-----RFINhsTQTADKCTFCAhrlevgllpACVESC 178
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGCD---------LCVEPC 155
 
Name Accession Description Interval E-value
PRK14993 PRK14993
tetrathionate reductase subunit TtrB;
1-244 1.79e-174

tetrathionate reductase subunit TtrB;


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 479.37  E-value: 1.79e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   1 MDLSKRKFLQQIGAVTAGASLIPIAEAGLNFSPTRREGNPEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQ 80
Cdd:PRK14993   1 MDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  81 YQVAVKGEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCT 160
Cdd:PRK14993  81 YQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 161 FCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKMLTEHEAEIKVLKPESGTLPQVFYLGLDDAFVQPLQGKGQPAL 240
Cdd:PRK14993 161 FCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPAL 240


                 ....
gi 757600339 241 WQEV 244
Cdd:PRK14993 241 WQEV 244
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 46-222 2.77e-96

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 279.42  E-value: 2.77e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGFTNvlLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd10551    1 MVIDLRKCIGCGACVVACKAENNVPPGVFRNRVLEYEVGEYPNVKRTF--LPVLCNHCENPPCVKVCPTGATYKREDGIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 126 VVDNERCVGCAYCVQACPYDARFIN------------HSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNS 193
Cdd:cd10551   79 LVDYDKCIGCRYCMAACPYGARYFNpeephefgevpvRPKGVVEKCTFCYHRLDEGLLPACVEACPTGARIFGDLDDPNS 158

                        170       180
                 ....*....|....*....|....*....
gi 757600339 194 TIRKMLTEHEAeiKVLKPESGTLPQVFYL 222
Cdd:cd10551  159 EVSKLLAERRA--YVLKPELGTKPKVYYI 185
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 40-226 1.69e-85

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 252.17  E-value: 1.69e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  40 PEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGFTNVllPRLCNHCDNPPCVPVCPVQATFQ 119
Cdd:COG0437    2 SMKRYGMVIDLTKCIGCRACVVACKEENNLPVGVTWRRVRRYEEGEFPNVEWLFV--PVLCNHCDDPPCVKVCPTGATYK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 120 REDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKML 199
Cdd:COG0437   80 REDGIVLVDYDKCIGCRYCVAACPYGAPRFNPETGVVEKCTFCADRLDEGLLPACVEACPTGALVFGDLDDPESEVSKRL 159

                        170       180
                 ....*....|....*....|....*..
gi 757600339 200 TEHEAeiKVLKPESGTLPQVFYLGLDD 226
Cdd:COG0437  160 AELPA--YRLLPELGTKPSVYYLPKRN 184
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 45-182 8.54e-55

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 172.36  E-value: 8.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  45 GMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGFTNVLLPrlCNHCDNPPCVPVCPVQATFQREDGI 124
Cdd:cd16371    1 GFYFDQERCIGCKACEIACKDKNDLPPGVNWRRVYEYEGGEFPEVFAYFLSMS--CNHCENPACVKVCPTGAITKREDGI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 757600339 125 VVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGA 182
Cdd:cd16371   79 VVVDQDKCIGCGYCVWACPYGAPQYNPETGKMDKCDMCVDRLDEGEKPACVAACPTRA 136
EBDH_beta cd10555
beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene ...
 40-221 2.16e-49

beta subunit of ethylbenzene-dehydrogenase (EBDH); This subfamily includes ethylbenzene dehydrogenase (EBDH, EC 1.17.99.2), a member of the DMSO reductase family. EBDH oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. It is a heterotrimer, with the alpha subunit containing the catalytic center with a molybdenum held by two molybdopterin-guanine dinucleotides, the beta subunit containing four iron-sulfur clusters (the electron transfer subunit) and the gamma subunit containing a methionine and a lysine as axial heme ligands. During catalysis, electrons produced by substrate oxidation are transferred to a heme in the gamma subunit and then presumably to a separate cytochrome involved in nitrate respiration.


Pssm-ID: 319877 [Multi-domain]  Cd Length: 316  Bit Score: 164.40  E-value: 2.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  40 PEKRYGMLIDLRRCIGCQSCTVSC----------------SVENQTPQG------------------------------- 72
Cdd:cd10555    1 SKRQLAMVMDLNKCIGCQTCTVACktlwtnrngreymywnNVETQPGKGypknwekkgggfkdkgelkpgiiptledygv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  73 ---------QFRTTVNQYQVAVKGE----------EG---FTNVL---LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVV 126
Cdd:cd10555   81 pweynheeeLFEGKGGRVRPSPKGDptwgpnwdedQGageYPNSYyfyLPRICNHCTNPACLAACPRKAIYKReEDGIVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 127 VDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIRKMLTEHeaei 206
Cdd:cd10555  161 VDQDRCRGYRYCVEACPYKKIYFNPVEQKSEKCIFCYPRIEKGVAPACARQCVGRIRFVGYLDDEESPVYKLVKKW---- 236

                        250
                 ....*....|....*...
gi 757600339 207 KV---LKPESGTLPQVFY 221
Cdd:cd10555  237 KValpLHPEYGTEPNVFY 254
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 46-186 1.54e-47

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 153.70  E-value: 1.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTPQGqfrttVNQYQVAVKGEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd04410    1 LVVDLDRCIGCGTCEVACKQEHGLRPG-----PDWSRIKVIEGGGLERAFLPVSCMHCEDPPCVKACPTGAIYKDEDGIV 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757600339 126 VVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIG 186
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIVFDPEPGKAVKCDLCGDRLDEGLEPACVKACPTGALTFG 136
TH_beta_N cd10552
N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This ...
 46-225 3.28e-47

N-terminal FeS domain of pyrogallol-phloroglucinol transhydroxylase (TH), beta subunit; This family includes the beta subunit of pyrogallol-phloroglucinol transhydroxylase (TH), a cytoplasmic molybdenum (Mo) enzyme from anaerobic microorganisms like Pelobacter acidigallici and Desulfitobacterium hafniense which catalyzes the conversion of pyrogallol to phloroglucinol, an important building block of plant polymers. TH belongs to the DMSO reductase (DMSOR) family; it is a heterodimer consisting of a large alpha catalytic subunit and a small beta FeS subunit. The beta subunit has two domains with the N-terminal domain containing three [4Fe-4S] centers and a seven-stranded, mainly antiparallel beta-barrel domain. In the anaerobic bacterium Pelobacter acidigallici, gallic acid, pyrogallol, phloroglucinol, or phloroglucinol carboxylic acid are fermented to three molecules of acetate (plus CO2), and TH is the key enzyme in the fermentation pathway, which converts pyrogallol to phloroglucinol in the absence of O2.


Pssm-ID: 319874 [Multi-domain]  Cd Length: 186  Bit Score: 154.79  E-value: 3.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVEN-----------QTPQGQFRTTVNQyqvAVKGEEGFTNV-LLPRLCNHCDNPPCVPVCP 113
Cdd:cd10552    1 LVIDVAKCNGCYNCFLACKDEHvgndwpgyaapQPRHGHFWMRILR---RERGQYPKVDVaYLPVPCNHCDNAPCIKAAK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 114 VQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVG-LLPACVESCVGGARIIGDLKDPN 192
Cdd:cd10552   78 DGAVYKRDDGIVIIDPEKAKGQKQLVDACPYGAIYWNEELQVPQKCTFCAHLLDDGwKEPRCVQACPTGALRFGKLEDEE 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 757600339 193 STIrkmlTEHEAEIKVLKPESGTLPQVFYLGLD 225
Cdd:cd10552  158 MAA----KAAEEGLEVLHPELGTKPRVYYKNLP 186
NarH_like cd16365
beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several ...
 42-222 7.86e-44

beta FeS subunits DMSOR NarH-like family; This subfamily contains beta FeS subunits of several DMSO reductase superfamily, including nitrate reductase A, ethylbenzene dehydrogenase and selenate reductase. DMSO Reductase (DMSOR) family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. . The beta subunits of DMSOR contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system. Nitrate reductase A contains three subunits (the catalytic subunit NarG, the catalytic subunit NarH with four [Fe-S] clusters, and integral membrane subunit NarI) and often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Ethylbenzene dehydrogenase oxidizes the hydrocarbon ethylbenzene to (S)-1-phenylethanol. Selenate reductase catalyzes reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor.


Pssm-ID: 319887 [Multi-domain]  Cd Length: 201  Bit Score: 146.57  E-value: 7.86e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  42 KRYGMLIDLRRCIGCQSCTVSC----------------SVENQTPQGQFRTtvnqYQVAVKGEEGFTNVL--LPRLCNHC 103
Cdd:cd16365    1 KQFAAVFNLNKCIGCQTCTVACknawtyrkgqeymwwnNVETKPGGGYPQD----WEVKTIDNGGNTRFFfyLQRLCNHC 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 104 DNPPCVPVCPVQATFQR-EDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGA 182
Cdd:cd16365   77 TNPACLAACPRGAIYKReEDGIVLIDQKRCRGYRKCVEQCPYKKIYFNGLSRVSEKCIACYPRIEGGDPTRCMSACVGRI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 757600339 183 RIIGDLKD-PNSTIRKMLTEHEAEIKvLKPESGTLPQVFYL 222
Cdd:cd16365  157 RLQGFLDDnPKSPVTKLIRHWKVALP-LHPEYGTEPNIYYV 196
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 45-222 2.02e-43

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 145.43  E-value: 2.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  45 GMLIDLRRCIGCQSCTVSCSVENQTPQGQF----------------RTTVNQYQVAvKGEEGFTNVllPRLCNHCDNPPC 108
Cdd:cd10561    1 GVLYDTTRCIGCRACEVACKEWNGLPAEDTafgpgwdnprdlsaktYTVIKRYEVE-TGGKGFVFV--KRQCMHCLDPAC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 109 VPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA-RFINHS-TQTADKCTFCAHRLEVGLLPACVESCVGGARIIG 186
Cdd:cd10561   78 VSACPVGALRKTPEGPVTYDEDKCIGCRYCMVACPFNIpKYEWDSaNPKIRKCTMCYDRLKEGKQPACVEACPTGALLFG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 757600339 187 DLKD------------PNSTIRKMLTEHEAeikvlkpeSGTlpQVFYL 222
Cdd:cd10561  158 KREEllaeakrriaanPGRYVDHVYGEKEA--------GGT--SVLYL 195
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 46-187 1.99e-38

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 131.27  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTPQGQFRT---------------TVNQYQVAVKGEEGFTNVLLPRLCNHCDNPPCVP 110
Cdd:cd10562    1 MLVDTSKCTACRGCQVACKQWNQLPAEKTPFtgsyqnppdltpntwTLIRFYEHEEDNGGIRWLFRKRQCMHCTDAACVK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339 111 VCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGD 187
Cdd:cd10562   81 VCPTGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRYDETTNKITKCTLCFDRIENGMQPACVKTCPTGALTFGD 157
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 46-182 1.58e-37

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 129.06  E-value: 1.58e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTP--QGQFRT-------------TVNQYQVAVKGEEGFTNVLLPRLCNHCDNPPCVP 110
Cdd:cd16366    1 FLVDTSRCTGCRACQVACKQWNGLPaeKTEFTGsyqnppdltahtwTLVRFYEVEKPGGDLSWLFRKDQCMHCTDAGCLA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600339 111 VCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGA 182
Cdd:cd16366   81 ACPTGAIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFDEETGRVAKCTLCYDRISNGLQPACVKTCPTGA 152
NarH_beta-like cd10557
beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes ...
 96-206 2.82e-37

beta subunit of nitrate reductase A (NarH) and similar proteins; This subfamily includes nitrate reductase A, a member of the DMSO reductase family. The respiratory nitrate reductase complex (NarGHI) from E. coli is a heterotrimer, with the catalytic subunit (NarG) with a molybdo-bis (molybdopterin guanine dinucleotide) cofactor and an [Fe-S] cluster, the electron transfer subunit (NarH) with four [Fe-S] clusters, and the integral membrane subunit (NarI) with two b-type hemes. Nitrate reductase A often forms a respiratory chain with the formate dehydrogenase via the lipid soluble quinol pool. Electron transfer from formate to nitrate is coupled to proton translocation across the cytoplasmic membrane generating proton motive force by a redox loop mechanism. Demethylmenaquinol (DMKH2) has been shown to be a good substrate for NarGHI in nitrate respiration in E. coli.


Pssm-ID: 319879 [Multi-domain]  Cd Length: 363  Bit Score: 134.03  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPAC 174
Cdd:cd10557  175 LPRICNHCLNPACVAACPSGAIYKReEDGIVLIDQDRCRGWRMCVSACPYKKVYYNWKTGKSEKCIFCYPRLEAGQPTVC 254

                         90       100       110
                 ....*....|....*....|....*....|...
gi 757600339 175 VESCVGGARIIGD-LKDPNSTIRKMLTEHEAEI 206
Cdd:cd10557  255 SETCVGRIRYLGVlLYDADRILEAAAVVPEKDL 287
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 43-182 5.73e-36

uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 124.40  E-value: 5.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  43 RYGMLIDLRRCIGCQSCTVSCSVENQTPQG-QFRTTVNQYQVAVKGEEGFTNVLLPrlCNHCDNPPCVPVCPVQATFQRE 121
Cdd:cd10553    2 KYYLYHDSKRCIGCLACEVHCKVKNNLPVGpRLCRIFAVGPKMVGGKPRLKFVYMS--CFHCENPWCVKACPTGAMQKRE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600339 122 -DGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGA 182
Cdd:cd10553   80 kDGIVYVDQELCIGCKACIEACPWGIPQWNPATGKVVKCDYCMDRIDQGLKPACVTGCTTHA 141
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and ...
 96-221 1.05e-35

Nitrate reductase beta subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 440755 [Multi-domain]  Cd Length: 485  Bit Score: 131.85  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  96 LPRLCNHCDNPPCVPVCPVQATFQR-EDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPAC 174
Cdd:COG1140  178 LPRICEHCLNPACVASCPSGAIYKReEDGIVLVDQDKCRGWRMCVSGCPYKKVYFNWKTGKAEKCIFCYPRIEAGQPTVC 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 175 VESCVGGARIIG-------------------DL--------KDPN-----------------------STIRKMLTEHea 204
Cdd:COG1140  258 SETCVGRIRYLGvllydadrveeaasvpdeqDLyeaqldvfLDPHdpeviaaarkdgipddwieaaqrSPVYKLAKEW-- 335

                        170       180
                 ....*....|....*....|
gi 757600339 205 eiKV---LKPESGTLPQVFY 221
Cdd:COG1140  336 --KValpLHPEYRTLPMVWY 353
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 47-196 2.10e-35

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 122.77  E-value: 2.10e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  47 LIDLRRCIGCQSCTVSCSVENQtpqGQFRTTVNQyqvavkGEEGFTnvlLPRLCNHCDNPPCVPVCPVQATFQREDGIVV 126
Cdd:cd16374    2 YVDPERCIGCRACEIACAREHS---GKPRISVEV------VEDLAS---VPVRCRHCEDAPCMEVCPTGAIYRDEDGAVL 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 127 VDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPNSTIR 196
Cdd:cd16374   70 VDPDKCIGCGMCAMACPFGVPRFDPSLKVAVKCDLCIDRRREGKLPACVEACPTGALKFGDIEELLKEKR 139
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 96-188 2.96e-35

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 404184 [Multi-domain]  Cd Length: 99  Bit Score: 121.20  E-value: 2.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPAC 174
Cdd:pfam13247   6 FPEQCRHCLNPPCKASCPVGAIYKDEeTGAVLLDEKTCRGWRECVSACPYNIPRYNDETGKAEKCDMCYDRVEAGLLPAC 85

                          90
                  ....*....|....
gi 757600339  175 VESCVGGARIIGDL 188
Cdd:pfam13247  86 VQTCPTGAMNFGDR 99
SER_beta cd10556
Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate ...
 36-222 8.54e-34

Beta subunit of selenate reductase; This subfamily includes beta FeS subunit of selenate reductase (SER), a member of the DMSO reductase family. SER catalyzes the reduction of selenate to selenite in bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The enzyme comprises three subunits SerABC, forming a heterotrimer, with the catalytic component (alpha-subunit), iron-sulfur protein (beta-subunit) and monomeric b-type heme-containing gamma subunit. Beta subunit contains coordinating one [3Fe-4S] cluster and three [4Fe-4S] clusters and functions as electron carrier.


Pssm-ID: 319878 [Multi-domain]  Cd Length: 287  Bit Score: 122.95  E-value: 8.54e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  36 REGNPEKRYGMLIDLRRCIGCQSCTVSC----------------SVENQ------------------------------- 68
Cdd:cd10556    4 EESRPDKQFAMVFDTNKCIACQTCTMACkstwtsgkgqeymwwnNVETKpyggyplgwdvrlldeeggqtwaeggvyegk 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  69 ---------------TPQGQFRTTVNQYQVAVKGEEGFTNVL-----------LPRLCNHCDNPPCVPVCPVQATFQR-E 121
Cdd:cd10556   84 tifeaaaageqvlgyRPEDEDWRYPNIGEDEVNGERTPDTGSslpphpiwffyLPRICNHCTYPACLAACPRKAIYKReE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 122 DGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKDPN--------S 193
Cdd:cd10556  164 DGIVLIDQERCRGYRECVEACPYKKPMYNPTTRVSEKCIGCYPRIEEGDQTQCVSACIGKIRLQGFINTPPdarwaddrD 243

                        250       260
                 ....*....|....*....|....*....
gi 757600339 194 TIRKMLTEHEAEIKVLKPESGTLPQVFYL 222
Cdd:cd10556  244 NPIDFLVHIKKVALPLYPQFGTEPNVYYI 272
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 47-210 9.66e-33

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 118.26  E-value: 9.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  47 LIDLRRCIGCQSCTVSCSVENQTPQGQfRTTVNQYQ---------------VAVKGEEGFTNVLLPRLCNHCDNPPCVPV 111
Cdd:cd10558    3 LIDVSKCIGCKACQVACKEWNDLRAEV-GHNVGTYQnpadlspetwtlmkfREVEDNGKLEWLIRKDGCMHCADPGCLKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 112 CPVQ-ATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGDLKD 190
Cdd:cd10558   82 CPSPgAIVQYANGIVDFQSDKCIGCGYCIKGCPFDIPRISKDDNKMYKCTLCSDRVSVGLEPACVKTCPTGALHFGTKED 161

                        170       180
                 ....*....|....*....|
gi 757600339 191 pnstirkMLTEHEAEIKVLK 210
Cdd:cd10558  162 -------MLALAEKRVAALK 174
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 45-190 1.40e-32

beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 118.26  E-value: 1.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  45 GMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQ---------------VAVKGEEGFTN-------VLLPRLCNH 102
Cdd:cd10560    1 GFFTDTSICIGCKACEVACKQWNQLPADGYDFSGMSYDntgdlsastwrhvkfIERPTEDGPANeggdlqwLFMSDVCKH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 103 CDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGA 182
Cdd:cd10560   81 CTDAGCLEACPTGAIFRTEFGTVYIQPDICNGCGYCVAACPFGVIDRNEETGRAHKCTLCYDRLKDGLEPACAKACPTGS 160


                 ....*...
gi 757600339 183 RIIGDLKD 190
Cdd:cd10560  161 IQFGPLEE 168
PRK10882 PRK10882
hydrogenase 2 operon protein HybA;
4-190 1.67e-28

hydrogenase 2 operon protein HybA;


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 110.14  E-value: 1.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   4 SKRKFLQQIGAVTAGASLIPIAeaglnfSPTRREGNPEKR--YGMLIDLRRCIGCQSCTVSCSVENQTP----------- 70
Cdd:PRK10882   2 NRRNFLKAASAGALLAGALPSV------SHAAAENRPPIPgaLGMLYDSTLCVGCQACVTKCQEINFPErnpqgeqtwdn 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  71 ----QGQFRTTVNQY-----QVAVKGEEGFTNVllPRLCNHCDNPPCVPVCPVQA-TFQREDGIVVVDNERCVGCAYCVQ 140
Cdd:PRK10882  76 pdklSPYTNNIIKVWksgtgVNKDQEENGYAYI--KKQCMHCVDPNCVSVCPVSAlTKDPKTGIVHYDKDVCTGCRYCMV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 757600339 141 ACPYDA-RF-INHSTQTADKCTFCAH----RLEVGLLPACVESCVGGARIIGDLKD 190
Cdd:PRK10882 154 ACPFNVpKYdYNNPFGAIHKCELCNQkgveRLDKGGLPGCVEVCPTGAVIFGTREE 209
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 46-182 1.75e-28

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 104.58  E-value: 1.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQtpqGQFRTTVNQYQVaVKGEEGFTNVllPRLCNHCDNPPCVPVCPVQA-TFQREDGI 124
Cdd:cd10550    1 LVVDPEKCTGCRTCELACSLKHE---GVFNPSLSRIRV-VRFEPEGLDV--PVVCRQCEDAPCVEACPVGAiSRDEETGA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 757600339 125 VVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCahrlevGLLPACVESCVGGA 182
Cdd:cd10550   75 VVVDEDKCIGCGMCVEACPFGAIRVDPETGKAIKCDLC------GGDPACVKVCPTGA 126
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 47-182 6.92e-27

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 100.79  E-value: 6.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  47 LIDLRRCIGCQSCTVSCSVE-----------NQTPQGQFRTTVnqyqvavkgeEGFTNVLLPRLCNHCDNPPCVPVCPVQ 115
Cdd:cd10563    3 FIDEEKCLGCKLCEVACAVAhskskdlikakLEKERPRPRIRV----------EESGGRSFPLQCRHCDEPPCVKACMSG 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757600339 116 A-TFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEvgllPACVESCVGGA 182
Cdd:cd10563   73 AmHKDPETGIVIHDEEKCVGCWMCVMVCPYGAIRPDKERKVALKCDLCPDRET----PACVEACPTGA 136
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
47-178 1.60e-26

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 99.73  E-value: 1.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  47 LIDLRRCIGCQSCTVSCSVENQTPQGQfrttVNQYQVAVKGEEGFTNvllPRLCNHCDNPPCVPVCPVQAtFQREDGIVV 126
Cdd:COG1142    6 IADPEKCIGCRTCEAACAVAHEGEEGE----PFLPRIRVVRKAGVSA---PVQCRHCEDAPCAEVCPVGA-ITRDDGAVV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757600339 127 VDNERCVGCAYCVQACPYDARFINHSTQ--TADKCTFCAHRLEvglLPACVESC 178
Cdd:COG1142   78 VDEEKCIGCGLCVLACPFGAITMVGEKSraVAVKCDLCGGREG---GPACVEAC 128
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 46-187 8.68e-26

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 99.00  E-value: 8.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSvENQTPQGQFRTTVNQYqvavkgEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd16369    4 FFIDPSRCIGCRACVAACR-ECGTHRGKSMIHVDYI------DRGESTQTAPTVCMHCEDPTCAEVCPADAIKVTEDGVV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757600339 126 V-VDNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARIIGD 187
Cdd:cd16369   77 QsALKPRCIGCSNCVNACPFGVPKYDEERNLMMKCDMCYDRTSVGKAPMCASVCPSGALFYGT 139
PRK09898 PRK09898
ferredoxin-like protein;
3-190 3.74e-24

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 95.67  E-value: 3.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339   3 LSKRKFLQQIGAVTAGaslIPIAEAGLNFSPTRRE-------GNPEKRYGMLIDLR-RCIGCQSCTVSCSVENQTPQGQF 74
Cdd:PRK09898  13 LTRLEFLRISGKGLAG---LTIAPALLSLLGCKQEdidsgtvGLINTPKGVLVTQRaRCTGCHRCEISCTNFNDGSVGTF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  75 RTTVNQYQVAVKGEEG-------FTNVLL-PRLCNHCDNPPCVPVCPVQA-TFQREDGIVVVDNERCVGCAYCVQACPYD 145
Cdd:PRK09898  90 FSRIKIHRNYFFGDNGvgsggglYGDLNYtADTCRQCKEPQCMNVCPIGAiTWQQKEGCITVDHKRCIGCSACTTACPWM 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 757600339 146 ARFINHSTQTADKCTFCAhrlevgllpACVESCVGGARIIGDLKD 190
Cdd:PRK09898 170 MATVNTESKKSSKCVLCG---------ECANACPTGALKIIEWKD 205
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 49-178 4.59e-24

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 93.86  E-value: 4.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  49 DLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVA----VKGEEgftnVLLPRLCNHCDNPPCVPVCPVQATFQrEDGI 124
Cdd:cd10554    5 DPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLPrlrvVKTGE----VTAPVQCRQCEDAPCANVCPVGAISQ-EDGV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600339 125 VVVDNERCVGCAYCVQACPYDA-----------RFINHSTQTADKCTFCAHRLEVgllPACVESC 178
Cdd:cd10554   80 VQVDEERCIGCKLCVLACPFGAiemapttvpgvDWERGPRAVAVKCDLCAGREGG---PACVEAC 141
DMSOR_beta_like cd16368
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 44-190 5.92e-21

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319890 [Multi-domain]  Cd Length: 200  Bit Score: 87.09  E-value: 5.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  44 YGMLIDLRRCIGCQ-----SCTVSCSVENQ--TPQGQF-----------------------RTT------VNQYQVAVKG 87
Cdd:cd16368    1 LATLIDLTKCDGCPgesipACVRACREKNQarFPEPVSkpiqpywprkriedwsdkrdvtdRLTpynwlyVQKLTVDTAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  88 EEgfTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYD--AR------FINHSTQTAD-- 157
Cdd:cd16368   81 GE--KEVFIPRRCMHCDNPPCAKLCPFGAARKTPEGAVYIDDDLCFGGAKCRDVCPWHipQRqagvgiYLHLAPEYAGgg 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 757600339 158 ---KCTFCAHRLEVGLLPACVESCVGGARIIGDLKD 190
Cdd:cd16368  159 vmyKCDLCKDLLAQGKPPACIEACPKGAQYFGPRKE 194
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 46-184 1.29e-20

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 84.67  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSvenQTPQGQFRTTVNQYQVAvkgeegftNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:cd16367   14 LVIDLDRCIRCDNCEKACA---DTHDGHSRLDRNGLRFG--------NLLVPTACRHCVDPVCMIGCPTGAIHRDDGGEV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 757600339 126 VVDnERCVGCAYCVQACPYDARFInhstQTADKCTFCAHRLEvgllPACVESCVGGARI 184
Cdd:cd16367   83 VIS-DACCGCGNCASACPYGAIQM----VRAVKCDLCAGYAG----PACVSACPTGAAI 132
W-FDH cd10559
tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit ...
 45-212 1.89e-20

tungsten-containing formate dehydrogenase, small subunit; This subfamily contains beta subunit of Tungsten-containing formate dehydrogenase (W-FDH), a member of the DMSO reductase family. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319881 [Multi-domain]  Cd Length: 200  Bit Score: 85.56  E-value: 1.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  45 GMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTT----------VNQYQVAV----KGEEGFTNVL-LPRLCNHCDNPPCV 109
Cdd:cd10559    1 SFLIDTTRCTACRGCQVACKQWNQLPAEQTKNTgshqnppdlsANTYKLVRfnevRNENGKPDWLfFPDQCRHCVTPPCK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 110 PVCPVQ--ATFQREDGIVVVDNERCVGCAYCV--QACPYDARFINHSTQTADKCTFCAHRLEVGLLPACVESCVGGARII 185
Cdd:cd10559   81 DAADMVpgAVIQDEATGAVVFTEKTAELDFDDvlSACPYNIPRKNEATGRIVKCDMCIDRVSNGLQPACVKACPTGAMNF 160

                        170       180
                 ....*....|....*....|....*..
gi 757600339 186 GDLkdpnstiRKMLTEHEAEIKVLKPE 212
Cdd:cd10559  161 GDR-------DEMLAMASKRLEELKKR 180
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 49-178 2.09e-20

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 89.81  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  49 DLRRCIGCQSCTVSCSVENQtpQGQFRTTVNQYQ---VAVKGEEGFTNVLlprlCNHCDNPPCVPVCPVQATFQREDGIV 125
Cdd:PRK12769   8 NSQQCLGCHACEIACVMAHN--DEQHVLSQHHFHpriTVIKHQQQRSAVT----CHHCEDAPCARSCPNGAISHVDDSIQ 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 126 VVdNERCVGCAYCVQACPYDARFI-------NHSTQTADKCTFCAHRlEVGllPACVESC 178
Cdd:PRK12769  82 VN-QQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENG--PACVENC 137
PRK10330 PRK10330
electron transport protein HydN;
46-178 9.91e-19

electron transport protein HydN;


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 80.70  E-value: 9.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  46 MLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEGfTNVLLPRLCNHCDNPPCVPVCPVQAtFQREDGIV 125
Cdd:PRK10330   5 IIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKG-VNVSTATVCRQCEDAPCANVCPNGA-ISRDKGFV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757600339 126 VVDNERCVGCAYCVQACPYDAR------FINHS---------TQTADKCTFCAHRlEVGllPACVESC 178
Cdd:PRK10330  83 HVMQERCIGCKTCVVACPYGAMevvvrpVIRNSgaglnvraeKAEANKCDLCNHR-EDG--PACMAAC 147
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 48-178 2.02e-17

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 75.77  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  48 IDLRRCIGCQSCTVSCSVENQtpqgqFRTTVNQYQVAVKGEEGFTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVV 127
Cdd:cd16370    6 KDMERCIGCYSCMLACSRRVH-----KSASLSKSAIRVRTRGGLEGGFTVVVCRACEDPPCAEACPTGALEPRKGGGVVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 757600339 128 DNERCVGCAYCVQACPYDARFINHSTQTADKCTFCAhrlevgllpACVESC 178
Cdd:cd16370   81 DKEKCIGCGNCVKACIVGAIFWDEETNKPIICIHCG---------YCARYC 122
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 49-178 2.35e-17

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 80.84  E-value: 2.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  49 DLRRCIGCQSCTVSCSV---ENQTPQGQ--FRTTVNQYqvavkgeeGFTNVLLPRLCNHCDNPPCVPVCPVQA-TFQRED 122
Cdd:PRK12809   8 EAAECIGCHACEIACAVahnQENWPLSHsdFRPRIHVV--------GKGQAANPVACHHCNNAPCVTACPVNAlTFQSDS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 757600339 123 giVVVDNERCVGCAYCVQACPYDArfINHSTQTADKCTFCAHRleVGLLPACVESC 178
Cdd:PRK12809  80 --VQLDEQKCIGCKRCAIACPFGV--VEMVDTIAQKCDLCNQR--SSGTQACIEVC 129
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 51-182 8.05e-13

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 63.51  E-value: 8.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  51 RRCIGCQSCTVSCSVenqtpqgQFRTTVNQYQVAVKGEEgFTNVLLPRLCNHCDNppCVPVCPVQATFQREDGIVVVDNE 130
Cdd:cd16372    8 EKCIGCLQCEEACSK-------TFFKEEDREKSCIRITE-TEGGYAINVCNQCGE--CIDVCPTGAITRDANGVVMINKK 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 757600339 131 RCVGCAYCVQACPYDARFINHSTQTADKCTFCAhrlevgllpACVESCVGGA 182
Cdd:cd16372   78 LCVGCLMCVGFCPEGAMFKHEDYPEPFKCIACG---------ICVKACPTGA 120
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 39-146 3.30e-10

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 56.25  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  39 NPEKRYGMLIDLRRCIGCQSCTVSCSVENQTPQGQFRTTVNQYQVAVKGEEgftnvllprLCNHCDNppCVPVCPVQATF 118
Cdd:cd10549   28 NGAIARGPEIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDEE---------KCIGCGL--CVKVCPVDAIT 96

                         90       100
                 ....*....|....*....|....*...
gi 757600339 119 QREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:cd10549   97 LEDELEIVIDKEKCIGCGICAEVCPVNA 124
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
97-150 6.49e-10

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.97  E-value: 6.49e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757600339  97 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNERCVGCAYCVQACPYDARFIN 150
Cdd:COG2768   10 EEKCIGCGA--CVKVCPVGA-ISIEDGKAVIDPEKCIGCGACIEVCPVGAIKIE 60
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 100-146 5.30e-09

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 51.98  E-value: 5.30e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 757600339 100 CNHCDNppCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG1144   32 CIGCGL--CWIVCPDGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKA 76
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 99-151 7.13e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 51.21  E-value: 7.13e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 757600339  99 LCNHCDNppCVPVCPVQAtFQREDGIVVVDNERCVGCAYCVQACPYDARFINH 151
Cdd:COG2221   16 KCIGCGL--CVAVCPTGA-ISLDDGKLVIDEEKCIGCGACIRVCPTGAIKGEK 65
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 97-146 5.25e-08

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 48.89  E-value: 5.25e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 757600339  97 PRLCNHCDNppCVPVCPVQAtFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG4231   21 EDKCTGCGA--CVKVCPADA-IEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 97-146 7.04e-08

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 48.19  E-value: 7.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 757600339  97 PRLCNHCDNppCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG1149   10 EEKCIGCGL--CVEVCPEGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGA 57
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
93-195 1.18e-07

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.95  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  93 NVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHSTQT--ADKCTFCAHrlevgl 170
Cdd:COG4624   54 CCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEidEEKCISCGQ------ 127

                         90       100       110
                 ....*....|....*....|....*....|...
gi 757600339 171 lpaCVESCVGGA--------RIIGDLKDPNSTI 195
Cdd:COG4624  128 ---CVAVCPFGAiteksdieKVKKALKDPEKVV 157
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 100-146 1.29e-07

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 47.43  E-value: 1.29e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 757600339 100 CNHCDNppCVPVCPVQA---TFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG1143    4 CIGCGL--CVRVCPVDAitiEDGEPGKVYVIDPDKCIGCGLCVEVCPTGA 51
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
97-199 2.48e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.96  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  97 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNERCVGCAYCVQACPYDA-RFINHSTQTADKCTfcaHRLEVG 169
Cdd:PRK13409  14 PKKCNY----ECIKYCPVVRTgeetieIDEDDGKPVISEELCIGCGICVKKCPFDAiSIVNLPEELEEEPV---HRYGVN 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 757600339 170 ---L--LPACVESCVGGarIIGdlkdPN----STIRKML 199
Cdd:PRK13409  87 gfkLygLPIPKEGKVTG--ILG----PNgigkTTAVKIL 119
NapF COG1145
Ferredoxin [Energy production and conversion];
100-146 3.20e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 49.72  E-value: 3.20e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 757600339 100 CNHCDNppCVPVCPVQA-TFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG1145  184 CIGCGL--CVKVCPTGAiRLKDGKPQIVVDPDKCIGCGACVKVCPVGA 229
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 97-146 5.40e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.78  E-value: 5.40e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 757600339  97 PRLCNHcdnpPCVPVCPVQAT------FQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:COG1245   14 PKKCNY----ECIKYCPVNRTgkeaieIDEDDGKPVISEELCIGCGICVKKCPFDA 65
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
108-178 1.14e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 48.13  E-value: 1.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600339 108 CVPVCPV---QATFQREDGIVV-VDNERCVGCAYCVQACPYDArFINHSTQTADKCTFCAhrlevgllpACVESC 178
Cdd:COG0348  184 CRYLCPYgafQGLLSDLSTLRVrYDRGDCIDCGLCVKVCPMGI-DIRKGEINQSECINCG---------RCIDAC 248
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 100-146 1.66e-06

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 44.05  E-value: 1.66e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 757600339  100 CNHCDNppCVPVCPVQATFQREDG------IVVVDNERCVGCAYCVQACPYDA 146
Cdd:pfam12838   1 CIGCGA--CVAACPVGAITLDEVGekkgtkTVVIDPERCVGCGACVAVCPTGA 51
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
87-153 2.59e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 47.93  E-value: 2.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339  87 GEEGFTNVLLPRLCNHCDNppCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDARFINHST 153
Cdd:COG1148  485 GVEPSVAEVDPEKCTGCGR--CVEVCPYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLKGFT 549
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 50-179 4.50e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 45.32  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  50 LRRCIGCQSCTVSCsvenqtpqgqfrttvnQYQVAVKG--EEGFTNVLLPRL------CNHCDNpPCVPVCPVQA----T 117
Cdd:cd16373   13 LALCIRCGLCVEAC----------------PTGVIQPAglEDGLEGGRTPYLdpregpCDLCCD-ACVEVCPTGAlrplD 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339 118 FQRED---GIVVVDNERCV------GCAYCVQACPYDARFINHSTQT------ADKCTFCAhrlevgllpACVESCV 179
Cdd:cd16373   76 LEEQKvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAIAIVLEDDVlrpvvdEDKCVGCG---------LCEYVCP 143
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
120-198 6.80e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 42.80  E-value: 6.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 120 REDGIVVVDNERCVGCAYCVQACPYDA-RFINHSTQT-ADKCTFCahrlevgllPACVESCVGGARIIGDlKDPNSTIRK 197
Cdd:COG2768    1 HSLGKPYVDEEKCIGCGACVKVCPVGAiSIEDGKAVIdPEKCIGC---------GACIEVCPVGAIKIEW-EEDEEFQEK 70


                 .
gi 757600339 198 M 198
Cdd:COG2768   71 M 71
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 108-143 7.39e-06

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 45.76  E-value: 7.39e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 757600339 108 CVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACP 143
Cdd:COG2878  145 CIKACPFDAIVGAAKGMHTVDEDKCTGCGLCVEACP 180
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
100-146 1.16e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 45.44  E-value: 1.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 757600339 100 CNHCDNppCVPVCPVqatfqredGIVV----VDNERCVGCAYCVQACPYDA 146
Cdd:COG0348  212 CIDCGL--CVKVCPM--------GIDIrkgeINQSECINCGRCIDACPKDA 252
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
108-145 2.04e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.54  E-value: 2.04e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 757600339 108 CVPVCPVQAtFQREDGIVVVDNERCVGCAYCVQACPYD 145
Cdd:PRK07118 147 CVAACPFDA-IHIENGLPVVDEDKCTGCGACVKACPRN 183
NapF COG1145
Ferredoxin [Energy production and conversion];
94-178 4.68e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.56  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  94 VLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA-RFINHSTQT---ADKCTFCahrlevg 169
Cdd:COG1145  146 ILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAiRLKDGKPQIvvdPDKCIGC------- 218


                 ....*....
gi 757600339 170 llPACVESC 178
Cdd:COG1145  219 --GACVKVC 225
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
108-146 5.01e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 41.47  E-value: 5.01e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 757600339 108 CVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:PRK09623  59 CWKFCPEPAIYIKEDGYVAIDYDYCKGCGICANECPTKA 97
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 94-143 5.48e-05

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 39.93  E-value: 5.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 757600339   94 VLLPRLCNHCDNppCVPVCPVQATFQR------EDGIVVVDNERCVGCAYCVQACP 143
Cdd:pfam13237   3 VIDPDKCIGCGR--CTAACPAGLTRVGaiverlEGEAVRIGVWKCIGCGACVEACP 56
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 99-143 7.02e-05

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 41.66  E-value: 7.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 757600339  99 LCNHCDNppCVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACP 143
Cdd:PRK09625  60 ICINCFN--CWVYCPDAAILSRDKKLKGVDYSHCKGCGVCVEVCP 102
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 94-146 9.65e-05

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 9.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339  94 VLLPRLCNHCDNppCVPVCPVQA-TFQREDGIV---VVDNERCVGCAYCVQACPYDA 146
Cdd:cd10549    2 KYDPEKCIGCGI--CVKACPTDAiELGPNGAIArgpEIDEDKCVFCGACVEVCPTGA 56
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 124-182 1.25e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 39.26  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757600339 124 IVVVDNERCVGCAYCVQACPYDA-RFINHSTQT-ADKCTFCAHrlevgllpaCVESCVGGA 182
Cdd:COG2221    9 PPKIDEEKCIGCGLCVAVCPTGAiSLDDGKLVIdEEKCIGCGA---------CIRVCPTGA 60
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 124-178 1.60e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 1.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  124 IVVVDNERCVGCAYCVQACPYDA-----RFINhsTQTADKCTFCAhrlevgllpACVESC 178
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACPVDAivgaaKAMH--TVIADECTGCD---------LCVEPC 155
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 99-143 1.91e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.17  E-value: 1.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 757600339  99 LCNHCDNppCVPVCPVQATFQ-REDGIVVVDNERCVGCAYCVQACP 143
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKlGPGRRYHFDYDKCTGCHICADVCP 554
PRK13795 PRK13795
hypothetical protein; Provisional
 99-150 2.51e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.90  E-value: 2.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757600339  99 LCNHCDnpPCVPVCPVQAtFQREDG--IVVVDNERCVGCAYCVQACPYdARFIN 150
Cdd:PRK13795 582 ECVGCG--VCVGACPTGA-IRIEEGkrKISVDEEKCIHCGKCTEVCPV-VKYKD 631
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 124-182 3.12e-04

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.17  E-value: 3.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757600339 124 IVVVDNERCVGCAYCVQACPYDA-RFINHSTQT--ADKCTFCAhrlevgllpACVESCVGGA 182
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCPEGAiKLDDGGAPVvdPDLCTGCG---------ACVGVCPTGA 57
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
108-157 3.36e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.86  E-value: 3.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757600339 108 CVPVCPVQA----TFQREDGIVVVDN-----ERCVGCAYCVQACPYDA-----RFINHSTQTAD 157
Cdd:PRK05888  66 CAAICPADAitieAAEREDGRRRTTRydinfGRCIFCGFCEEACPTDAivetpDFELATETREE 129
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 126-197 4.47e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 39.30  E-value: 4.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757600339 126 VVDNERCVGCAYCVQACPYDA-------RFINHSTQTADKCTFCAhrlevgllpACVESCVGGARIIGDLKDPNSTIRK 197
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAielgpngAIARGPEIDEDKCVFCG---------ACVEVCPTGAIELTPEGKEYVPKEK 71
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 125-146 4.85e-04

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 36.46  E-value: 4.85e-04
                          10        20
                  ....*....|....*....|..
gi 757600339  125 VVVDNERCVGCAYCVQACPYDA 146
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGA 22
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 123-182 6.94e-04

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 6.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757600339 123 GIVVVDNERCVGCAYCVQACPYDARFINHSTQTA-----DKCTFCAhrlevgllpACVESCVGGA 182
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCPVDVLELDEEGKKAlvinpEECIGCG---------ACELVCPVGA 56
PRK06991 PRK06991
electron transport complex subunit RsxB;
87-162 7.06e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 39.78  E-value: 7.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339  87 GEEGftnvlLPRLCNHCDNPPcVPVCPVQATfQREDGIVVVDNERCVGCAYCVQACPYDArfI-----NHSTQTADKCTF 161
Cdd:PRK06991  49 GAEG-----IARLAALLGKPV-IPLDPANGV-ERPRAVAVIDEQLCIGCTLCMQACPVDA--IvgapkQMHTVLADLCTG 119


                 .
gi 757600339 162 C 162
Cdd:PRK06991 120 C 120
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
129-178 7.76e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.09  E-value: 7.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339 129 NERCVGCAYCVQACPYDA----------------RF-INHStqtadKCTFCahrlevGLlpaCVESC 178
Cdd:PRK05888  57 EERCIACKLCAAICPADAitieaaeredgrrrttRYdINFG-----RCIFC------GF---CEEAC 109
Fer4_9 pfam13187
4Fe-4S dicluster domain;
100-146 1.10e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 35.99  E-value: 1.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 757600339  100 CNHCDNppCVPVCPVQATFQREDGIVVV---DNERCVGCAYCVQACPYDA 146
Cdd:pfam13187   2 CTGCGA--CVAACPAGAIVPDLVGQTIRgdiAGLACIGCGACVDACPRGA 49
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
108-143 1.54e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 38.76  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 757600339 108 CVPVCPVQAtFQREDGIVVVDNERCVGCAYCVQACP 143
Cdd:PRK07118 221 CVKACPAGA-ITMENNLAVIDQEKCTSCGKCVEKCP 255
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 108-146 2.23e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.55  E-value: 2.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 757600339 108 CVPVCPVQATFQREDGIVVVDNERCVGCAYCVQACPYDA 146
Cdd:PRK09624  59 CYIYCPEPAIYLDEEGYPVFDYDYCKGCGICANECPTKA 97
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 130-182 2.69e-03

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.49  E-value: 2.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 757600339 130 ERCVGCAYCVQACPYDARFINHSTQT------ADKCTFCAhrlevgllpACVESCVGGA 182
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDGEPGkvyvidPDKCIGCG---------LCVEVCPTGA 51
Fer COG1141
Ferredoxin [Energy production and conversion];
125-143 4.10e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 34.86  E-value: 4.10e-03
                         10
                 ....*....|....*....
gi 757600339 125 VVVDNERCVGCAYCVQACP 143
Cdd:COG1141    3 VTVDRDTCIGCGLCVALAP 21
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 125-178 4.83e-03

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.02  E-value: 4.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 757600339 125 VVVDNERCVGCAYCVQACPYDA-------RFINhstqtADKCTFCAhrlevgllpACVESC 178
Cdd:COG4231   17 YVIDEDKCTGCGACVKVCPADAieegdgkAVID-----PDLCIGCG---------SCVQVC 63
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 48-116 5.42e-03

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 36.47  E-value: 5.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339  48 IDLRRCIGCQSCTVSC---SVE-NQTPQGQFRTTVNQYQVAVKgeegftnvllprlCNHC----DNPPCVPVCPVQA 116
Cdd:cd10554   82 VDEERCIGCKLCVLACpfgAIEmAPTTVPGVDWERGPRAVAVK-------------CDLCagreGGPACVEACPTKA 145
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 128-178 5.92e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 36.90  E-value: 5.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 757600339 128 DNERCVGCAYCVQACPYDARFINHS---TQTADKCTFCAhrlevgllpACVESC 178
Cdd:COG2878  135 CEYGCIGCGDCIKACPFDAIVGAAKgmhTVDEDKCTGCG---------LCVEAC 179
PRK06991 PRK06991
electron transport complex subunit RsxB;
38-114 6.24e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 37.08  E-value: 6.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757600339  38 GNPEKRYGMLIDLRRCIGCQSCTVSCSVEnqtpqgqfrttvnqyqvAVKGEEGFTNVLLPRLCNHCDnpPCVPVCPV 114
Cdd:PRK06991  72 GVERPRAVAVIDEQLCIGCTLCMQACPVD-----------------AIVGAPKQMHTVLADLCTGCD--LCVPPCPV 129
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 108-146 6.42e-03

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 36.07  E-value: 6.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 757600339 108 CVPVCPVQA-TFQREDGIV---VVDNERCVGCAYCVQACPYDA 146
Cdd:cd10564   91 CQDACPTQAiRFRPRLGGIalpELDADACTGCGACVSVCPVGA 133
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 126-178 7.39e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 36.46  E-value: 7.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 757600339 126 VVDNERCVGCAYCVQACPYDArfINHSTQT-----ADKCTFCahrlevgllPACVESC 178
Cdd:PRK05113 110 FIDEDNCIGCTKCIQACPVDA--IVGATKAmhtviSDLCTGC---------DLCVAPC 156
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 124-146 7.70e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 32.97  E-value: 7.70e-03
                          10        20
                  ....*....|....*....|...
gi 757600339  124 IVVVDNERCVGCAYCVQACPYDA 146
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGA 23
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
 100-212 9.76e-03

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 36.53  E-value: 9.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757600339 100 CNHCDNPPCVPVCPVQA-TFQRED------GI-VVVDNERCVG-----CAYCVQACP-----------------YDARFI 149
Cdd:PRK09476  99 CEMCEDIPCVKACPSGAlDRELVDiddarmGLaVLVDQENCLNfqglrCDVCYRVCPlidkaitlelernertgKHAFFL 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757600339 150 nhSTQTADKCTFCahrlevGLlpaCVESCVggariigdlkdpnstirkmlTEhEAEIKVLKPE 212
Cdd:PRK09476 179 --PTVHSDACTGC------GK---CEKACV--------------------LE-KAAIKVLPRS 209
 
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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