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Conserved domains on  [gi|16129188|ref|NP_415743.1|]
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nitrate reductase 1, beta (Fe-S) subunit [Escherichia coli str. K-12 substr. MG1655]

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List of domain hits

Name Accession Description Interval E-value
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
359-438 5.63e-44

Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between subunits and shielding of the Fe-S clusters


:

Pssm-ID: 258848  Cd Length: 79  Bit Score: 150.68  E-value: 5.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   359 LSPIQSAADAGELGsNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEA 438
Cdd:pfam14711   1 LSPVQSAAEAGGSD-AGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALERLLAMRSYMRAKNVGGEPDEAILEAVGLTEE 79
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion]
1-512 0e+00

Nitrate reductase beta subunit [Energy production and conversion]


:

Pssm-ID: 224063 [Multi-domain]  Cd Length: 513  Bit Score: 1102.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGN 80
Cdd:COG1140   1 MKIRAQVGMVLNLDKCIGCHTCSVTCKNVWTNREGMEYAWFNNVETKPGVGYPKQWEDQEKWKGGWVRDKNGKLRPRMGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  81 RAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGsKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKN 160
Cdd:COG1140  81 RIEKLAKIFANPKLPGIDDYYEPFTYDYENLHSAPEG-KHQPTARPRSLITGERMDKIEWGPNWEDDLAGEFEKRAKDPN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 161 FDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK 240
Cdd:COG1140 160 FEKIQKEIYGQFENTFMMYLPRLCEHCLNPSCVASCPSGAIYKREEDGIVLIDQDKCRGWRMCVSGCPYKKVYFNWKSGK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 241 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS 320
Cdd:COG1140 240 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASTENEKDLYERQLDVFLDPHDPAVIEQARKDGIPDN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 321 VIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELG--SNGILPDVESLRIPVQYLANLLTAGD 398
Cdd:COG1140 320 WIEAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGGLGgeSDGILPAVESLRIPVQYLANLLTAGD 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 399 TKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGF 478
Cdd:COG1140 400 TEPVLSALKRMLAMRHYMRAITVEGKTDTRALEEVGLTEAQAEEMYRYLAIANYEDRFVIPTSHREEARDAFPERGGCGF 479
                       490       500       510
                ....*....|....*....|....*....|....
gi 16129188 479 TFGDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP 512
Cdd:COG1140 480 TFGDGCHGSDSKFNLFGSKRIDAINITWVVFRAE 513
 
Name Accession Description Interval E-value
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
359-438 5.63e-44

Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between subunits and shielding of the Fe-S clusters


Pssm-ID: 258848  Cd Length: 79  Bit Score: 150.68  E-value: 5.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   359 LSPIQSAADAGELGsNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEA 438
Cdd:pfam14711   1 LSPVQSAAEAGGSD-AGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALERLLAMRSYMRAKNVGGEPDEAILEAVGLTEE 79
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion]
1-512 0e+00

Nitrate reductase beta subunit [Energy production and conversion]


Pssm-ID: 224063 [Multi-domain]  Cd Length: 513  Bit Score: 1102.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGN 80
Cdd:COG1140   1 MKIRAQVGMVLNLDKCIGCHTCSVTCKNVWTNREGMEYAWFNNVETKPGVGYPKQWEDQEKWKGGWVRDKNGKLRPRMGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  81 RAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGsKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKN 160
Cdd:COG1140  81 RIEKLAKIFANPKLPGIDDYYEPFTYDYENLHSAPEG-KHQPTARPRSLITGERMDKIEWGPNWEDDLAGEFEKRAKDPN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 161 FDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK 240
Cdd:COG1140 160 FEKIQKEIYGQFENTFMMYLPRLCEHCLNPSCVASCPSGAIYKREEDGIVLIDQDKCRGWRMCVSGCPYKKVYFNWKSGK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 241 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS 320
Cdd:COG1140 240 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASTENEKDLYERQLDVFLDPHDPAVIEQARKDGIPDN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 321 VIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELG--SNGILPDVESLRIPVQYLANLLTAGD 398
Cdd:COG1140 320 WIEAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGGLGgeSDGILPAVESLRIPVQYLANLLTAGD 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 399 TKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGF 478
Cdd:COG1140 400 TEPVLSALKRMLAMRHYMRAITVEGKTDTRALEEVGLTEAQAEEMYRYLAIANYEDRFVIPTSHREEARDAFPERGGCGF 479
                       490       500       510
                ....*....|....*....|....*....|....
gi 16129188 479 TFGDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP 512
Cdd:COG1140 480 TFGDGCHGSDSKFNLFGSKRIDAINITWVVFRAE 513
Respiratory_nitrate_reductase_1_beta_chain TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
1-494 0e+00

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 1059.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188     1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGN 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188    81 RAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGsKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKN 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEG-KHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   161 FDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK 240
Cdd:TIGR01660 160 FDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   241 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS 320
Cdd:TIGR01660 240 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   321 VIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTK 400
Cdd:TIGR01660 320 VIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKVGANGIMPDVESLRIPVRYLANLLTAGDTK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   401 PVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTF 480
Cdd:TIGR01660 400 PVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSF 479
                         490
                  ....*....|....
gi 16129188   481 GDGCHGSDTKfNLF 494
Cdd:TIGR01660 480 GDGCHGSDTK-NLF 492
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
175-273 1.24e-61

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: 257603 [Multi-domain]  Cd Length: 99  Bit Score: 198.99  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   175 TFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAG 254
Cdd:pfam13247   1 VDWLYLPRQCRHCLNPPCVASCPSGAIYKDEETGIVLVDQKTCRGWRMCVSACPYKKPYFNWETGKAEKCDMCYDRVEAG 80
                          90
                  ....*....|....*....
gi 16129188   255 QPTVCSETCVGRIRYLGVL 273
Cdd:pfam13247  81 LPPACVETCPTGARYFGDR 99
PRK14993 PRK14993
tetrathionate reductase subunit B; Provisional
180-273 1.59e-25

tetrathionate reductase subunit B; Provisional


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 104.57  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  180 LPRLCEHCLNPACVATCPSGAIYKREeDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVC 259
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
                         90
                 ....*....|....
gi 16129188  260 SETCVGRIRYLGVL 273
Cdd:PRK14993 175 VESCVGGARIIGDI 188
 
Name Accession Description Interval E-value
Nitr_red_bet_C pfam14711
Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the ...
359-438 5.63e-44

Respiratory nitrate reductase beta C-terminal; This domain occurs near the C-terminus of the respiratory nitrate reductase beta chain. The nitrate reductase complex is a dimer of heterotrimers each consisting of an alpha, beta and gamma chain. This domain plays a role in the interactions between subunits and shielding of the Fe-S clusters


Pssm-ID: 258848  Cd Length: 79  Bit Score: 150.68  E-value: 5.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   359 LSPIQSAADAGELGsNGILPDVESLRIPVQYLANLLTAGDTKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEA 438
Cdd:pfam14711   1 LSPVQSAAEAGGSD-AGLFPAIDSLRIPVEYLANLLTAGDTEPVRRALERLLAMRSYMRAKNVGGEPDEAILEAVGLTEE 79
NarY COG1140
Nitrate reductase beta subunit [Energy production and conversion]
1-512 0e+00

Nitrate reductase beta subunit [Energy production and conversion]


Pssm-ID: 224063 [Multi-domain]  Cd Length: 513  Bit Score: 1102.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGN 80
Cdd:COG1140   1 MKIRAQVGMVLNLDKCIGCHTCSVTCKNVWTNREGMEYAWFNNVETKPGVGYPKQWEDQEKWKGGWVRDKNGKLRPRMGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  81 RAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGsKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKN 160
Cdd:COG1140  81 RIEKLAKIFANPKLPGIDDYYEPFTYDYENLHSAPEG-KHQPTARPRSLITGERMDKIEWGPNWEDDLAGEFEKRAKDPN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 161 FDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK 240
Cdd:COG1140 160 FEKIQKEIYGQFENTFMMYLPRLCEHCLNPSCVASCPSGAIYKREEDGIVLIDQDKCRGWRMCVSGCPYKKVYFNWKSGK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 241 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS 320
Cdd:COG1140 240 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADRVEEAASTENEKDLYERQLDVFLDPHDPAVIEQARKDGIPDN 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 321 VIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELG--SNGILPDVESLRIPVQYLANLLTAGD 398
Cdd:COG1140 320 WIEAAQRSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGGLGgeSDGILPAVESLRIPVQYLANLLTAGD 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 399 TKPVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGF 478
Cdd:COG1140 400 TEPVLSALKRMLAMRHYMRAITVEGKTDTRALEEVGLTEAQAEEMYRYLAIANYEDRFVIPTSHREEARDAFPERGGCGF 479
                       490       500       510
                ....*....|....*....|....*....|....
gi 16129188 479 TFGDGCHGSDTKFNLFNSRRIDAIDVTSKTEPHP 512
Cdd:COG1140 480 TFGDGCHGSDSKFNLFGSKRIDAINITWVVFRAE 513
Respiratory_nitrate_reductase_1_beta_chain TIGR01660
nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use ...
1-494 0e+00

nitrate reductase, beta subunit; The Nitrate reductase enzyme complex allows bacteria to use nitrate as an electron acceptor during anaerobic growth. The enzyme complex consists of a tetramer that has an alpha, beta and 2 gamma subunits. The alpha and beta subunits have catalytic activity and the gamma subunits attach the enzyme to the membrane and is a b-type cytochrome that receives electrons from the quinone pool and transfers them to the beta subunit. This model is specific for the beta subunit for nitrate reductase I (narH) and nitrate reductase II (narY) for gram positive and gram negative bacteria.A few thermophiles and archaea also match the model.The seed members used in this model are all experimentally characterized and include the following:SP:P11349, and SP:P19318, both E.Coli (NarH and NarY respectively), SP:P42176 from B. Subtilis, GP:11344602 from Psuedomonas fluorescens,GP:541762 from Paracoccus denitrificans, and GP:18413622 from Halomonas halodenitrificans. This model also matches Pfam pfam00037 for 4Fe-4S binding domain. [Energy metabolism, Anaerobic]


Pssm-ID: 211677 [Multi-domain]  Cd Length: 492  Bit Score: 1059.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188     1 MKIRSQVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENQEKYKGGWIRKINGKLQPRMGN 80
Cdd:TIGR01660   1 MKIRSQIGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGIGYPKDWENQDKYKGGWVRKRDGKLEPRIGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188    81 RAMLLGKIFANPHLPGIDDYYEPFDFDYQNLHTAPEGsKSQPIARPRSLITGERMAKIEKGPNWEDDLGGEFDKLAKDKN 160
Cdd:TIGR01660  81 KWRVLANIFANPDLPSIDDYYEPFDFDYQHLHTAPEG-KHQPTARPRSLITGERMEKIEWGPNWEDDLGGEFAKRRKDKN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   161 FDNIQKAMYSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGK 240
Cdd:TIGR01660 160 FDKIQKDIYGEFENTFMMYLPRLCEHCLNPACVASCPSGAIYKREEDGIVLIDQDKCRGWRMCISGCPYKKIYFNWKTGK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   241 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADAIERAASTENEKDLYQRQLDVFLDPNDPKVIEQAIKDGIPLS 320
Cdd:TIGR01660 240 SEKCIFCYPRIEAGQPTVCSETCVGRIRYLGVLLYDADKIEEAASTENEKDLYHRQLDVFLDPNDPEVIAQAKKDGIPLS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   321 VIEAAQQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADAGELGSNGILPDVESLRIPVQYLANLLTAGDTK 400
Cdd:TIGR01660 320 VIEAAQQSPVYKMAMDWKLALPLHPEYRTLPMVWYVPPLSPIQNAAEAGKVGANGIMPDVESLRIPVRYLANLLTAGDTK 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   401 PVLRALKRMLAMRHYKRAETVDGKVDTRALEEVGLTEAQAQEMYRYLAIANYEDRFVVPSSHRELAREAFPEKNGCGFTF 480
Cdd:TIGR01660 400 PVLLALKRMLAMRHYMRAETVDGVVDTEVLEDVGLTEQQIEEMYRYLAIANYEDRFVIPSSHREIARDAFPERGGCGFSF 479
                         490
                  ....*....|....
gi 16129188   481 GDGCHGSDTKfNLF 494
Cdd:TIGR01660 480 GDGCHGSDTK-NLF 492
Dimethylsulfide_dehydrogenase_subunit_beta TIGR03478
DMSO reductase family type II enzyme, iron-sulfur subunit; This model represents the ...
6-422 2.64e-108

DMSO reductase family type II enzyme, iron-sulfur subunit; This model represents the iron-sulfur subunit, typically called the beta subunit, of various proteins that also contain a molybdopterin subunit and a heme b subunit. The group includes two distinct but very closely related periplasmic proteins of anaerobic respiration, selenate reductase and chlorate reductase. Other members of this family include dimethyl sulphide dehydrogenase and ethylbenzene dehydrogenase. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 132518 [Multi-domain]  Cd Length: 321  Bit Score: 328.29  E-value: 2.64e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188     6 QVGMVLNLDKCIGCHTCSVTCKNVWTSREGVEYAWFNNVETKPGQGFPTDWENqekyKGGWIRKINGKLQPrmgnramll 85
Cdd:TIGR03478   3 QLAYVIDLNKCIGCQTCTVACKNLWTNRPGREYMYWNNVETYPGKGYPRNWER----KGGGFKRGGKLKQP--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188    86 GKIfanphlPGIDDYYEPFDFDYqnLHTAPEGSKSQpiARPRSlitgermaKIEKGPNWEDDLGGefdklakdknfdniq 165
Cdd:TIGR03478  70 GII------PTLIDYGDPWEFNH--EEVLYEGKDET--VRPHP--------TPTWGPNWDEDQGA--------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   166 kamySQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCI 245
Cdd:TIGR03478 117 ----GEYPNNYYFYLPRICNHCTNPACLAACPTGAIYKREEDGIVLVDQERCKGYRYCVEACPYKKVYFNPQSQKSEKCI 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   246 FCYPRIEAGQPTVCSETCVGRIRYLGvllydadaieraastenekdlyqrqldvFLDPndpkvieqaikdgiplsvieaa 325
Cdd:TIGR03478 193 GCYPRIEKGIAPACVKQCPGRIRFVG----------------------------YLDD---------------------- 222
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   326 QQSPVYKMAMEWKLALPLHPEYRTLPMVWYVPPLSPIQSAADaGELGsngilpdvESLRIPVQYLANLLTAGdTKPVLRA 405
Cdd:TIGR03478 223 EEGPVHKLVKRWKVALPLHPEYGTEPNVFYVPPMGPRGFGED-GEIT--------DKTRIPLDYLEGLFGPG-VKQALAT 292
                         410
                  ....*....|....*...
gi 16129188   406 LKR-MLAMRHYKRAETVD 422
Cdd:TIGR03478 293 LHTeREKKRKGQGSELMD 310
Fer4_11 pfam13247
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
175-273 1.24e-61

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: 257603 [Multi-domain]  Cd Length: 99  Bit Score: 198.99  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   175 TFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAG 254
Cdd:pfam13247   1 VDWLYLPRQCRHCLNPPCVASCPSGAIYKDEETGIVLVDQKTCRGWRMCVSACPYKKPYFNWETGKAEKCDMCYDRVEAG 80
                          90
                  ....*....|....*....
gi 16129188   255 QPTVCSETCVGRIRYLGVL 273
Cdd:pfam13247  81 LPPACVETCPTGARYFGDR 99
HybA COG0437
Fe-S-cluster-containing hydrogenase components 1 [Energy production and conversion]
170-271 4.69e-37

Fe-S-cluster-containing hydrogenase components 1 [Energy production and conversion]


Pssm-ID: 223514 [Multi-domain]  Cd Length: 203  Bit Score: 135.64  E-value: 4.69e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 170 SQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYP 249
Cdd:COG0437  55 WGSGTVEYYYLSISCMHCEDPPCVKVCPTGALFKREEDGIVLVDKDLCIGCGYCIAACPYGAPQFNPDKGVVDKCTFCVD 134
                        90       100
                ....*....|....*....|..
gi 16129188 250 RIEAGQPTVCSETCVGRIRYLG 271
Cdd:COG0437 135 RVAVGKLPACVEACPTGALIFG 156
anaerobic_dimethyl_sulfoxide_reductase_subunit_B TIGR02951
DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain ...
174-266 9.74e-29

DMSO reductase, iron-sulfur subunit; This family consists of the iron-sulfur subunit, or chain B, of an enzyme called the anaerobic dimethyl sulfoxide reductase. Chains A and B are catalytic, while chain C is a membrane anchor.


Pssm-ID: 131996 [Multi-domain]  Cd Length: 161  Bit Score: 111.36  E-value: 9.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   174 NTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEA 253
Cdd:TIGR02951  54 DVFAYYISISCNHCADPACVKNCPTGAMYKREEDGLVLVDQDKCIGCRYCVWACPYGAPQYDPQQGVMGKCDGCYDRVEK 133
                          90
                  ....*....|...
gi 16129188   254 GQPTVCSETCVGR 266
Cdd:TIGR02951 134 GLRPACVDACPMR 146
PRK14993 PRK14993
tetrathionate reductase subunit B; Provisional
180-273 1.59e-25

tetrathionate reductase subunit B; Provisional


Pssm-ID: 184955 [Multi-domain]  Cd Length: 244  Bit Score: 104.57  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  180 LPRLCEHCLNPACVATCPSGAIYKREeDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVC 259
Cdd:PRK14993  96 LPRLCNHCDNPPCVPVCPVQATFQRE-DGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPAC 174
                         90
                 ....*....|....
gi 16129188  260 SETCVGRIRYLGVL 273
Cdd:PRK14993 175 VESCVGGARIIGDI 188
PRK10882 PRK10882
hydrogenase 2 protein HybA; Provisional
179-306 9.47e-19

hydrogenase 2 protein HybA; Provisional


Pssm-ID: 236786 [Multi-domain]  Cd Length: 328  Bit Score: 85.88  E-value: 9.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  179 YLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKS--GKSEKCIFC----YPRIE 252
Cdd:PRK10882 107 YIKKQCMHCVDPNCVSVCPVSALTKDPKTGIVHYDKDVCTGCRYCMVACPFNVPKYDYNNpfGAIHKCELCnqkgVERLD 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16129188  253 AGQPTVCSETC-VGRIRYlGV---LLydADAIERAASTENEKDLYQRQLdvfLDPNDP 306
Cdd:PRK10882 187 KGGLPGCVEVCpTGAVIF-GTreeLL--AEAKRRLALKPGSEYHYPRQT---LKSGDT 238
cyt_nit_nrfC TIGR03149
cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S ...
169-263 8.05e-18

cytochrome c nitrite reductase, Fe-S protein; Members of this protein family are the Fe-S protein, NrfC, of a cytochrome c nitrite reductase system for which the pentaheme cytochrome c protein, NrfB (family TIGR03146) is an unambiguous marker. Members of this protein family show similarity to other ferredoxin-like proteins, including a subunit of a polysulfide reductase. [Energy metabolism, Electron transport]


Pssm-ID: 274451 [Multi-domain]  Cd Length: 225  Bit Score: 81.75  E-value: 8.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   169 YSQFENTFMMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCY 248
Cdd:TIGR03149  79 YGEFPDVEYRFFRKSCQHCDNAPCVAVCPTGASFKDEETGIVDVHKDLCVGCQYCIAACPYRVRFIHPVTKSADKCNFCR 158
                          90
                  ....*....|....*.
gi 16129188   249 -PRIEAGQPTVCSETC 263
Cdd:TIGR03149 159 dTNLAEGKLPACVESC 174
Formate_dehydrogenase_iron-sulfur_subunit TIGR01582
formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit ...
184-263 3.14e-15

formate dehydrogenase, beta subunit, Fe-S containing; This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 273705 [Multi-domain]  Cd Length: 283  Bit Score: 74.56  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   184 CEHCLNPACVATCPS-GAIYKREeDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFCYPRIEAGQPTVCSET 262
Cdd:TIGR01582  93 CMHCREPGCLKACPApGAIIQYQ-NGIVDFDHSKCIGCGYCIVGCPFNIPRYDKVDNRPYKCTLCIDRVSVGQEPACVKT 171

                  .
gi 16129188   263 C 263
Cdd:TIGR01582 172 C 172
PRK09898 PRK09898
hypothetical protein; Provisional
177-247 3.62e-13

hypothetical protein; Provisional


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 67.55  E-value: 3.62e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129188  177 MMYLPRLCEHCLNPACVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFC 247
Cdd:PRK09898 116 LNYTADTCRQCKEPQCMNVCPIGAITWQQKEGCITVDHKRCIGCSACTTACPWMMATVNTESKKSSKCVLC 186
HycB COG1142
Fe-S-cluster-containing hydrogenase components 2 [Energy production and conversion]
181-263 7.64e-13

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


Pssm-ID: 224065 [Multi-domain]  Cd Length: 165  Bit Score: 65.97  E-value: 7.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 181 PRLCEHCLNPACVATCPSGAIYkrEEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSE----KCIFCYPRiEAGQp 256
Cdd:COG1142  50 PVVCHHCEDAPCAEVCPVGAIT--RDDGAVQVDEEKCIGCKLCVVACPFGAITMVSYPVAAKavavKCDLCAGR-EVGP- 125

                ....*..
gi 16129188 257 tVCSETC 263
Cdd:COG1142 126 -ACVEAC 131
PRK10330 PRK10330
formate dehydrogenase-H ferredoxin subunit; Provisional
183-263 1.08e-07

formate dehydrogenase-H ferredoxin subunit; Provisional


Pssm-ID: 182382 [Multi-domain]  Cd Length: 181  Bit Score: 50.66  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  183 LCEHCLNPACVATCPSGAIYKreEDGIVLIDQDKCRGWRMCITGCPYKKIY-------------FNWKSGKSE--KCIFC 247
Cdd:PRK10330  57 VCRQCEDAPCANVCPNGAISR--DKGFVHVMQERCIGCKTCVVACPYGAMEvvvrpvirnsgagLNVRAEKAEanKCDLC 134
                         90
                 ....*....|....*.
gi 16129188  248 YPRiEAGqpTVCSETC 263
Cdd:PRK10330 135 NHR-EDG--PACMAAC 147
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
184-263 1.47e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 52.83  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  184 CEHCLNPACVATCPSGAIyKREEDGIVLIdQDKCRGWRMCITGCPYKKIYF-------NWKSGKSEKCIFCYPRiEAGQp 256
Cdd:PRK12769  56 CHHCEDAPCARSCPNGAI-SHVDDSIQVN-QQKCIGCKSCVVACPFGTMQIvltpvaaGKVKATAHKCDLCAGR-ENGP- 131

                 ....*..
gi 16129188  257 tVCSETC 263
Cdd:PRK12769 132 -ACVENC 137
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
179-228 3.64e-07

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: 257594 [Multi-domain]  Cd Length: 51  Bit Score: 47.37  E-value: 3.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129188   179 YLPRLCEHCLnpACVATCPS--GAIYKREEDGIVLIDQDKCRGWRMCITGCP 228
Cdd:pfam13237   2 IDPDKCIGCG--RCVAACPAhvGAGAIREEGEAVEIDPDRCIGCGACVEVCP 51
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
181-263 8.50e-07

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 50.02  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  181 PRLCEHCLNPACVATCPSGAIYKREEDgiVLIDQDKCRGWRMCITGCPYKKIyfNWKSGKSEKCIFCYPRIEAGQptVCS 260
Cdd:PRK12809  53 PVACHHCNNAPCVTACPVNALTFQSDS--VQLDEQKCIGCKRCAIACPFGVV--EMVDTIAQKCDLCNQRSSGTQ--ACI 126

                 ...
gi 16129188  261 ETC 263
Cdd:PRK12809 127 EVC 129
hypothetical_protein TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
184-247 1.77e-06

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 49.13  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   184 CEHCLNPACVATCPSGAIYKreEDGIVLIDQDKCRGWRMCITGCPY----------------KKIYFNwKSGKS----EK 243
Cdd:TIGR04105 113 CRGCLAHPCIEVCPKGAISM--VNGRAYIDQEKCIECGKCKKACPYnaiveierpcekacpvGAISSD-EDGRAvidyDK 189

                  ....
gi 16129188   244 CIFC 247
Cdd:TIGR04105 190 CISC 193
NapF COG1145
Ferredoxin [Energy production and conversion]
181-247 3.30e-06

Ferredoxin [Energy production and conversion]


Pssm-ID: 224068 [Multi-domain]  Cd Length: 99  Bit Score: 45.29  E-value: 3.30e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188 181 PRLCEHClnPACVATCPSGAIYKREE---DGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSEKCIFC 247
Cdd:COG1145  28 AEKCIGC--GLCVKVCPTGAIELIEEgllLPEVVIDPDLCVLCGACLKVCPVDALSIAEELVNAGEAKLR 95
PRK07118 PRK07118
ferredoxin; Validated
192-232 3.54e-06

ferredoxin; Validated


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 47.24  E-value: 3.54e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 16129188  192 CVATCPSGAIykREEDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:PRK07118 221 CVKACPAGAI--TMENNLAVIDQEKCTSCGKCVEKCPTKAI 259
Uncharacterized_protein_MJ0208 TIGR02700
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ...
178-232 5.74e-06

archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]


Pssm-ID: 131747 [Multi-domain]  Cd Length: 234  Bit Score: 46.40  E-value: 5.74e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16129188   178 MYLPRLCEHCLnpACVATCPSGAIYKReeDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:TIGR02700 144 MIDRKRCKGCG--ICVDACPRSAIDMV--DGKAFIRLLKCVGCGKCKEACPYNAI 194
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
184-230 8.93e-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: 257339 [Multi-domain]  Cd Length: 52  Bit Score: 43.33  E-value: 8.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 16129188   184 CEHCLnpACVATCPSGAIYKREEDGI-----VLIDQDKCRGWRMCITGCPYK 230
Cdd:pfam12838   2 CIGCG--ACVRACPYGAITLDEETEKkgkptVEIDPDKCTGCGRCVAVCPTG 51
vorD PRK09623
2-ketoisovalerate ferredoxin oxidoreductase subunit delta; Reviewed
192-232 2.67e-05

2-ketoisovalerate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 42.63  E-value: 2.67e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 16129188  192 CVATCPSGAIYKREeDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:PRK09623  59 CWKFCPEPAIYIKE-DGYVAIDYDYCKGCGICANECPTKAI 98
glycine_radical_enzyme_activase_YjjW_family TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
182-230 2.93e-05

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 44.55  E-value: 2.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 16129188   182 RLCEHClnPACVATCPSGAIYKreEDGIVLIDQDKCRGWRMCITGCPYK 230
Cdd:TIGR04041  41 NHCDHC--GDCVAGCPAGALSL--VDGKVVWDKERCIGCDTCIKVCPHQ 85
putative_pyruvate_formate-lyase_activating_enzyme TIGR04395
choline TMA-lyase-activating enzyme; Members of this family are CutD, a radical enzyme that ...
168-229 7.84e-05

choline TMA-lyase-activating enzyme; Members of this family are CutD, a radical enzyme that serves as an activase for choline TMA-lyase, CutC. CutC is a glycyl radical enzyme related to pyruvate formate-lyase, and this enzyme, CutD, is related to pyruvate formate-lyase activase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 275188 [Multi-domain]  Cd Length: 309  Bit Score: 43.17  E-value: 7.84e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129188   168 MYSQFEntfMMYLPRLCEHClnPACVATCPSGAIYKREEDGIVLIDQDK-CRGWRMCITGCPY 229
Cdd:TIGR04395  43 QERKFQ---VLFKKDICVDC--GACVAVCPVGIHKMLAEGGKHVIDRSIdCIGCRKCEEACPK 100
PRK13795 PRK13795
hypothetical protein; Provisional
192-235 1.64e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 42.67  E-value: 1.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 16129188  192 CVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKIYFN 235
Cdd:PRK13795 589 CVGACPTGAIRIEEGKRKISVDEEKCIHCGKCTEVCPVVKYKDK 632
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
183-228 2.77e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.17  E-value: 2.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 16129188  183 LCEHCLNpaCVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCP 228
Cdd:PRK12771 511 NCFECDN--CYGACPQDAIIKLGPGRRYHFDYDKCTGCHICADVCP 554
Pyruvate_synthase_subunit_PorD TIGR02179
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ...
184-232 2.82e-04

2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.


Pssm-ID: 131234 [Multi-domain]  Cd Length: 78  Bit Score: 39.24  E-value: 2.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 16129188   184 CEHCLNpaCVATCPSGAIYKREeDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:TIGR02179  27 CIKCKN--CWLYCPEGAIQEDE-GGFVGIDYDYCKGCGICANVCPVKAI 72
napG PRK09476
quinol dehydrogenase periplasmic component; Provisional
184-265 2.91e-04

quinol dehydrogenase periplasmic component; Provisional


Pssm-ID: 236534 [Multi-domain]  Cd Length: 254  Bit Score: 41.15  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188  184 CEHCLNPACVATCPSGAIYKREED------GI-VLIDQDKCRGWR-----MCITGCPY--KKIYF----NWKSGKSEKCI 245
Cdd:PRK09476  99 CEMCEDIPCVKACPSGALDRELVDiddarmGLaVLVDQENCLNFQglrcdVCYRVCPLidKAITLelerNERTGKHAFFL 178
                         90       100
                 ....*....|....*....|
gi 16129188  246 fcyprieagqPTVCSETCVG 265
Cdd:PRK09476 179 ----------PTVHSDACTG 188
PRK07118 PRK07118
ferredoxin; Validated
192-228 3.69e-04

ferredoxin; Validated


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.07  E-value: 3.69e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16129188  192 CVATCPSGAIykREEDGIVLIDQDKCRGWRMCITGCP 228
Cdd:PRK07118 147 CVAACPFDAI--HIENGLPVVDEDKCTGCGACVKACP 181
Rama_corrin_act TIGR04270
methylamine methyltransferase corrinoid protein reductive activase; Members of this family ...
184-237 1.04e-03

methylamine methyltransferase corrinoid protein reductive activase; Members of this family occur as paralogs in species capable of generating methane from mono-, di-, and tri-methylamine. Members include RamA (Reductive Activation of Methyltransfer, Amines) from Methanosarcina barkeri MS (DSM 800). Member proteins have two C-terminal motifs with four Cys each, likely to bind one 4Fe-4S cluster per motif.


Pssm-ID: 211993 [Multi-domain]  Cd Length: 535  Bit Score: 40.13  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16129188   184 CEHClnPACVATCPSGAIyKREEDGIVLIDQDKCRGW--RMCITGCPYKKiyFNWK 237
Cdd:TIGR04270 481 CIAC--QKCVKECPGKAL-SILESEPPRIDTDRCLGTacRRCERVCPEKV--FDIR 531
COG2768 COG2768
Uncharacterized Fe-S center protein [General function prediction only]
192-242 1.32e-03

Uncharacterized Fe-S center protein [General function prediction only]


Pssm-ID: 225358 [Multi-domain]  Cd Length: 354  Bit Score: 39.78  E-value: 1.32e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16129188 192 CVATCPSGAIykrEEDGIVLIDQDKCRGWRMCITGCPYKKIYFNWKSGKSE 242
Cdd:COG2768 201 CVKICPVGAI---TLTKVVKIDYEKCIGCGQCMEACPYGAVDQNWEEDSPE 248
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
184-232 3.63e-03

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 36.16  E-value: 3.63e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 16129188  184 CEHCLnpACVATCPSGAIYKREEdGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:PRK09624  53 CVRCY--LCYIYCPEPAIYLDEE-GYPVFDYDYCKGCGICANECPTKAI 98
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
179-228 4.27e-03

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 36.26  E-value: 4.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 16129188  179 YLPRLCEHCLNpaCVATCPSGAIYKREEDgIVLIDQDKCRGWRMCITGCP 228
Cdd:PRK09625  56 HNNEICINCFN--CWVYCPDAAILSRDKK-LKGVDYSHCKGCGVCVEVCP 102
COG4231 COG4231
Indolepyruvate ferredoxin oxidoreductase, alpha and beta subunits [Energy production and ...
184-232 4.42e-03

Indolepyruvate ferredoxin oxidoreductase, alpha and beta subunits [Energy production and conversion]


Pssm-ID: 226684 [Multi-domain]  Cd Length: 640  Bit Score: 38.12  E-value: 4.42e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 16129188 184 CEHCLnpACV--ATCPsgAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:COG4231 579 CTGCG--DCIvlSGCP--SIEPDPTFKKARIDPSSCNGCGSCVEVCPSFAI 625
COG1144 COG1144
Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, delta ...
184-232 8.12e-03

Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, delta subunit [Energy production and conversion]


Pssm-ID: 224067 [Multi-domain]  Cd Length: 91  Bit Score: 34.67  E-value: 8.12e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 16129188 184 CEHCLNpaCVATCPSGAIYKREEDGIVLIDQDKCRGWRMCITGCPYKKI 232
Cdd:COG1144  37 CINCKL--CWLYCPEPAILEEEGGYKVRIDYDYCKGCGICANVCPVKAI 83
putative_reductive_dehalogenase_partial TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
182-264 8.98e-03

reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S cluster-containing reductive dehalogenases found primarily in halorespiring microorganisms such as dehalococcoides ethenogenes which contains as many as 17 enzymes of this type with varying substrate ranges. One example of a characterized species is the tetrachloroethene reductive dehalogenase (1.97.1.8) which also acts on trichloroethene converting it to dichloroethene.


Pssm-ID: 274158 [Multi-domain]  Cd Length: 314  Bit Score: 37.03  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129188   182 RLCEHCLnpACVATCPSGAIykrEEDGIVLIDQDKCRGWRMciTGCPYKKIYFnWKSGKSekCIFCYPRIEAGQPTVCSE 261
Cdd:TIGR02486 205 KFCETCG--KCADECPSGAI---SKGGEPTWDPEDSNGDPP--GENNPGLKWQ-YDGWRC--LLFRCYNEGGGGCGVCQA 274

                  ...
gi 16129188   262 TCV 264
Cdd:TIGR02486 275 VCP 277
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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