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Conserved domains on  [gi|222625883|gb|EEE60015|]
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hypothetical protein OsJ_12764 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 91-565 0e+00

5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5.


:

Pssm-ID: 461733  Cd Length: 445  Bit Score: 684.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883   91 MRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMDRHKYVKVA 170
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVEKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  171 YHGFREMSKEEKVSAYGSTLIRDSFDEPDYALIDTLFSLGEAYLFAQLVDFMDNNPGKVPsgtDYPLMYRDVRSAVDLCH 250
Cdd:pfam05761  81 YHGFRPLSDEEVRELYGNTFIPLSFDEPRYVQLNTLFSLPEAYLLAQLVDYFDNGGNIDY---DYESLYQDVREAVDLVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  251 RDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCrpytsDVSSSHNHKWLGYFDVVIT 330
Cdd:pfam05761 158 RDGSLKKEVAADPEKYIEKDPELPPLLERLREAGKKLFLLTNSDYDYTNKGMNYLL-----GGFLPKYKDWRDLFDVVIV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  331 GSAKPGFFHDGNRagLFEVEPDSGKLLnADLHIGSPRSGQqpsrpihkIYQGGNVGHLHRLLSvASSSQILYVGDHIYGD 410
Cdd:pfam05761 233 GARKPLFFTEGRP--LREVDTETGRLL-WGNVTGPLEKGK--------VYQGGSLDHFHKLLG-WRGSEVLYVGDHIYGD 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  411 ILRSKKVLGWRTMLVIPELEQEVKLLSESKStRKELRHLRMERDSIEDKIHRLEWSLKFENLTEDEKeklfsehdiLLQK 490
Cdd:pfam05761 301 ILRSKKKLGWRTALVIPELEREIEVLNSKRY-RKELAELQTLRELLEDEYKDLDSSLAQQSDEKLEE---------LPAD 370

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  491 KEHVRRLHQEAQRQHHHKFHKVWGQLMKTGYQNSRFAHQVERFACLYSSQVTNFALYSPNKYYRPSEDYMPHEFD 565
Cdd:pfam05761 371 LEELRKEIRELRREMKELFNPQWGSLFRTGSNPSYFARQVERYADLYTSSVSNLLNYSPNYYFRPPRDLLPHEST 445
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
657-815 1.53e-93

NADH-quinone oxidoreductase subunit NuoI;


:

Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 289.86  E-value: 1.53e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 657 FERSINTLFLTEMVRGLMLTLKYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAE 736
Cdd:PRK05888   1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 737 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAANLESESLYR 815
Cdd:PRK05888  81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYR 159
 
Name Accession Description Interval E-value
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 91-565 0e+00

5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5.


Pssm-ID: 461733  Cd Length: 445  Bit Score: 684.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883   91 MRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMDRHKYVKVA 170
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVEKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  171 YHGFREMSKEEKVSAYGSTLIRDSFDEPDYALIDTLFSLGEAYLFAQLVDFMDNNPGKVPsgtDYPLMYRDVRSAVDLCH 250
Cdd:pfam05761  81 YHGFRPLSDEEVRELYGNTFIPLSFDEPRYVQLNTLFSLPEAYLLAQLVDYFDNGGNIDY---DYESLYQDVREAVDLVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  251 RDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCrpytsDVSSSHNHKWLGYFDVVIT 330
Cdd:pfam05761 158 RDGSLKKEVAADPEKYIEKDPELPPLLERLREAGKKLFLLTNSDYDYTNKGMNYLL-----GGFLPKYKDWRDLFDVVIV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  331 GSAKPGFFHDGNRagLFEVEPDSGKLLnADLHIGSPRSGQqpsrpihkIYQGGNVGHLHRLLSvASSSQILYVGDHIYGD 410
Cdd:pfam05761 233 GARKPLFFTEGRP--LREVDTETGRLL-WGNVTGPLEKGK--------VYQGGSLDHFHKLLG-WRGSEVLYVGDHIYGD 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  411 ILRSKKVLGWRTMLVIPELEQEVKLLSESKStRKELRHLRMERDSIEDKIHRLEWSLKFENLTEDEKeklfsehdiLLQK 490
Cdd:pfam05761 301 ILRSKKKLGWRTALVIPELEREIEVLNSKRY-RKELAELQTLRELLEDEYKDLDSSLAQQSDEKLEE---------LPAD 370

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  491 KEHVRRLHQEAQRQHHHKFHKVWGQLMKTGYQNSRFAHQVERFACLYSSQVTNFALYSPNKYYRPSEDYMPHEFD 565
Cdd:pfam05761 371 LEELRKEIRELRREMKELFNPQWGSLFRTGSNPSYFARQVERYADLYTSSVSNLLNYSPNYYFRPPRDLLPHEST 445
HAD-IG-Ncltidse TIGR02244
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ...
 83-446 5.64e-173

HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5'-nucleotidase specific for purines (IMP and GMP). These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognized by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG". This domain appears to consist of a mixed alpha/beta fold. A Pfam model (pfam05761) detects an identical range of sequences above the trusted cutoff, but does not model the N-terminal motif 1 region. A TIGRFAMs model (TIGR01993) represents a (putative) family of _pyrimidine_ 5'-nucleotidases which are also subfamily I HAD's, which should not be confused with the current model.


Pssm-ID: 274052  Cd Length: 343  Bit Score: 501.85  E-value: 5.64e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883   83 IFCNRSLNMRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMD 162
Cdd:TIGR02244   1 VFVNRELNLEKIQVFGFDMDYTLAQYKSPELEALIYDLAKERLVKRFGYPEELLSFAYDPTFAIRGLVFDKLKGNLLKLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  163 RHKYVKVAYHGFREMSKEEKVSAYGSTLIRDSFDEpDYALIDTLFSLGEAYLFAQLVDFMDNNPgKVPSGTDYPLMYRDV 242
Cdd:TIGR02244  81 RFGNILRGYHGLRPLSDKEVQEIYGNKYISRSNGD-RYYLLDTLFSLPEACLIAQLVDYFDDHP-KGPLAFDYRQIYQDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  243 RSAVDLCHRDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCRPYTsdvsssHNHKWL 322
Cdd:TIGR02244 159 RDALDWVHRKGSLKKKVMENPEKYVLRDPKLPLFLSKLKEHGKKLFLLTNSDYDYTDKGMKYLLGPFL------GEHDWR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  323 GYFDVVITGSAKPGFFHDGNRAGLFEVEPDSGKLLNAD-LHIGsprsgqqpsrpihKIYQGGNVGHLHRLLSVAsSSQIL 401
Cdd:TIGR02244 233 DYFDVVIVDARKPGFFTEGRPFRQVDVETGSLKWGEVDgLEPG-------------KVYSGGSLKQFHELLKWR-GKEVL 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 222625883  402 YVGDHIYGDILRSKKVLGWRTMLVIPELEQEVKLLSESKSTRKEL 446
Cdd:TIGR02244 299 YFGDHIYGDLLRSKKKRGWRTAAIIPELEQEVGILTNSKSLREEL 343
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 84-450 8.60e-144

cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase domain-containing protein 1) and NT5DC2; Cytosolic 5'-nucleotidase II (cN-II), also known as purine 5'-nucleotidase, IMP-GMP specific nucleotidase, or high Km 5prime-nucleotidase, catalyzes the dephosphorylation of 6-hydroxypurine nucleoside monophosphates. It is ubiquitously expressed and likely to play an important role in the regulation of purine nucleotide interconversions and in the regulation of IMP and GMP pools within the cell. It is also acts as a phosphotransferase, catalyzing the reverse reaction, the transfer of a phosphate from a monophosphate substrate to a nucleoside acceptor, to form a nucleoside monophosphate. The nucleoside acceptor is preferentially inosine and deoxyinosine, phosphate donors include any 6-hydroxypurine monophosphate substrate of the nucleotidase reaction. Both the dephosphorylation and phosphotransferase reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319824  Cd Length: 352  Bit Score: 427.46  E-value: 8.60e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  84 FCNRSLNMRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMDR 163
Cdd:cd07522    1 FVNRSLNLEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDYDPNFPVRGLVFDKEKGNLLKLDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 164 HKYVKVAYHGFREMSKEEKVSAYGSTLIRDSFDEPDYALIDTLFSLGEAYLFAQLVDFMDNNPGKvpSGTDYPLMYRDVR 243
Cdd:cd07522   81 YGQILRAYHGTRPLSDEEVREIYGSNNTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLE--SDMSYRSIYQDVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 244 SAVDLCHRDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCRPYTSDVSSshnhkWLG 323
Cdd:cd07522  159 AAVDWVHSKGLLKKKIMQDPERYVLRDPELPLLLSRLREAGKKLFLLTNSDYSYTNKGMKYLLGGFLPKHRD-----WRD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 324 YFDVVITGSAKPGFFHDGNRagLFEVEPDSGKLlnADLHIGSPRSGqqpsrpihKIYQGGNVGHLHRLLSvASSSQILYV 403
Cdd:cd07522  234 YFDVVIVDARKPGFFTEGTP--FREVDTETGQL--KITKVGPLEKG--------KVYSGGNLKQFTELLG-WRGKEVLYF 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 222625883 404 GDHIYGDILRSKKVLGWRTMLVIPELEQEVKLLseSKSTRKELRHLR 450
Cdd:cd07522  301 GDHIYSDILKSKKRHGWRTALIVPELGSLFRTG--SNPTYFSSQVER 345
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
657-815 1.53e-93

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 289.86  E-value: 1.53e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 657 FERSINTLFLTEMVRGLMLTLKYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAE 736
Cdd:PRK05888   1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 737 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAANLESESLYR 815
Cdd:PRK05888  81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYR 159
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 672-793 2.25e-65

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 213.43  E-value: 2.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  672 GLMLTLKYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDID 751
Cdd:TIGR01971   1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 222625883  752 MTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKL 793
Cdd:TIGR01971  81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 713-785 4.80e-26

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: 101.75  E-value: 4.80e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEERedgsrrTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFATETHEE 785
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEP------GKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 713-771 5.45e-18

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: 80.90  E-value: 5.45e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 771
Cdd:cd10549   77 EEKCIGCGLCVKVCPVDAITLEDE---------LEIVIDKEKCIGCGICAEVCPVNAIK 126
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 716-769 1.05e-15

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: 71.79  E-value: 1.05e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 222625883  716 CIACKLCEAICPAQAITIEAEEREDGsrrTTRYDIDMTKCIYCGFCQEACPVDA 769
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 678-770 8.18e-07

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 51.01  E-value: 8.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 678 KYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAEEREDGSrrttrydidmtKCIY 757
Cdd:NF038196 149 KKGPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGKPVWGH-----------NCTH 217

                         90
                 ....*....|...
gi 222625883 758 CGFCQEACPVDAI 770
Cdd:NF038196 218 CLACIHRCPKEAI 230
 
Name Accession Description Interval E-value
5_nucleotid pfam05761
5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, ...
 91-565 0e+00

5' nucleotidase family; This family of eukaryotic proteins includes 5' nucleotidase enzymes, such as purine 5'-nucleotidase EC:3.1.3.5.


Pssm-ID: 461733  Cd Length: 445  Bit Score: 684.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883   91 MRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMDRHKYVKVA 170
Cdd:pfam05761   1 LDNIKAYGFDMDYTLAQYKSPTFESLAYDLAKERLVEKLGYPEELLELEYDPDFAIRGLVYDKKRGNLLKVDRFGYIQVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  171 YHGFREMSKEEKVSAYGSTLIRDSFDEPDYALIDTLFSLGEAYLFAQLVDFMDNNPGKVPsgtDYPLMYRDVRSAVDLCH 250
Cdd:pfam05761  81 YHGFRPLSDEEVRELYGNTFIPLSFDEPRYVQLNTLFSLPEAYLLAQLVDYFDNGGNIDY---DYESLYQDVREAVDLVH 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  251 RDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCrpytsDVSSSHNHKWLGYFDVVIT 330
Cdd:pfam05761 158 RDGSLKKEVAADPEKYIEKDPELPPLLERLREAGKKLFLLTNSDYDYTNKGMNYLL-----GGFLPKYKDWRDLFDVVIV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  331 GSAKPGFFHDGNRagLFEVEPDSGKLLnADLHIGSPRSGQqpsrpihkIYQGGNVGHLHRLLSvASSSQILYVGDHIYGD 410
Cdd:pfam05761 233 GARKPLFFTEGRP--LREVDTETGRLL-WGNVTGPLEKGK--------VYQGGSLDHFHKLLG-WRGSEVLYVGDHIYGD 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  411 ILRSKKVLGWRTMLVIPELEQEVKLLSESKStRKELRHLRMERDSIEDKIHRLEWSLKFENLTEDEKeklfsehdiLLQK 490
Cdd:pfam05761 301 ILRSKKKLGWRTALVIPELEREIEVLNSKRY-RKELAELQTLRELLEDEYKDLDSSLAQQSDEKLEE---------LPAD 370

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  491 KEHVRRLHQEAQRQHHHKFHKVWGQLMKTGYQNSRFAHQVERFACLYSSQVTNFALYSPNKYYRPSEDYMPHEFD 565
Cdd:pfam05761 371 LEELRKEIRELRREMKELFNPQWGSLFRTGSNPSYFARQVERYADLYTSSVSNLLNYSPNYYFRPPRDLLPHEST 445
HAD-IG-Ncltidse TIGR02244
HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5 ...
 83-446 5.64e-173

HAD superfamily (subfamily IG) hydrolase, 5'-nucleotidase; This model includes a 5'-nucleotidase specific for purines (IMP and GMP). These enzymes are members of the Haloacid Dehalogenase (HAD) superfamily. HAD members are recognized by three short motifs {hhhhDxDx(T/V)}, {hhhh(T/S)}, and either {hhhh(D/E)(D/E)x(3-4)(G/N)} or {hhhh(G/N)(D/E)x(3-4)(D/E)} (where "h" stands for a hydrophobic residue). Crystal structures of many HAD enzymes has verified PSI-PRED predictions of secondary structural elements which show each of the "hhhh" sequences of the motifs as part of beta sheets. This subfamily of enzymes is part of "Subfamily I" of the HAD superfamily by virtue of a "cap" domain in between motifs 1 and 2. This subfamily's cap domain has a different predicted secondary structure than all other known HAD enzymes and thus has been designated "subfamily IG". This domain appears to consist of a mixed alpha/beta fold. A Pfam model (pfam05761) detects an identical range of sequences above the trusted cutoff, but does not model the N-terminal motif 1 region. A TIGRFAMs model (TIGR01993) represents a (putative) family of _pyrimidine_ 5'-nucleotidases which are also subfamily I HAD's, which should not be confused with the current model.


Pssm-ID: 274052  Cd Length: 343  Bit Score: 501.85  E-value: 5.64e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883   83 IFCNRSLNMRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMD 162
Cdd:TIGR02244   1 VFVNRELNLEKIQVFGFDMDYTLAQYKSPELEALIYDLAKERLVKRFGYPEELLSFAYDPTFAIRGLVFDKLKGNLLKLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  163 RHKYVKVAYHGFREMSKEEKVSAYGSTLIRDSFDEpDYALIDTLFSLGEAYLFAQLVDFMDNNPgKVPSGTDYPLMYRDV 242
Cdd:TIGR02244  81 RFGNILRGYHGLRPLSDKEVQEIYGNKYISRSNGD-RYYLLDTLFSLPEACLIAQLVDYFDDHP-KGPLAFDYRQIYQDV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  243 RSAVDLCHRDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCRPYTsdvsssHNHKWL 322
Cdd:TIGR02244 159 RDALDWVHRKGSLKKKVMENPEKYVLRDPKLPLFLSKLKEHGKKLFLLTNSDYDYTDKGMKYLLGPFL------GEHDWR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  323 GYFDVVITGSAKPGFFHDGNRAGLFEVEPDSGKLLNAD-LHIGsprsgqqpsrpihKIYQGGNVGHLHRLLSVAsSSQIL 401
Cdd:TIGR02244 233 DYFDVVIVDARKPGFFTEGRPFRQVDVETGSLKWGEVDgLEPG-------------KVYSGGSLKQFHELLKWR-GKEVL 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 222625883  402 YVGDHIYGDILRSKKVLGWRTMLVIPELEQEVKLLSESKSTRKEL 446
Cdd:TIGR02244 299 YFGDHIYGDLLRSKKKRGWRTAAIIPELEQEVGILTNSKSLREEL 343
HAD_cN-II cd07522
cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase ...
 84-450 8.60e-144

cytosolic 5'-nucleotidase II (cN-II) similar to human NT5DC1 (5'-nucleotidase domain-containing protein 1) and NT5DC2; Cytosolic 5'-nucleotidase II (cN-II), also known as purine 5'-nucleotidase, IMP-GMP specific nucleotidase, or high Km 5prime-nucleotidase, catalyzes the dephosphorylation of 6-hydroxypurine nucleoside monophosphates. It is ubiquitously expressed and likely to play an important role in the regulation of purine nucleotide interconversions and in the regulation of IMP and GMP pools within the cell. It is also acts as a phosphotransferase, catalyzing the reverse reaction, the transfer of a phosphate from a monophosphate substrate to a nucleoside acceptor, to form a nucleoside monophosphate. The nucleoside acceptor is preferentially inosine and deoxyinosine, phosphate donors include any 6-hydroxypurine monophosphate substrate of the nucleotidase reaction. Both the dephosphorylation and phosphotransferase reactions are allosterically activated by adenine-based nucleotides and 2,3-bisphosphoglycerate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319824  Cd Length: 352  Bit Score: 427.46  E-value: 8.60e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  84 FCNRSLNMRNITAVGFDMDYTLAQYKPETFEALAYHGTIEKLVKDLGYPEELLTWQFDWKYMVRGLVLDKKRGNILKMDR 163
Cdd:cd07522    1 FVNRSLNLEKIKVFGFDMDYTLARYNSPELESLIYDLAKERLVEEKGYPEELLKFDYDPNFPVRGLVFDKEKGNLLKLDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 164 HKYVKVAYHGFREMSKEEKVSAYGSTLIRDSFDEPDYALIDTLFSLGEAYLFAQLVDFMDNNPGKvpSGTDYPLMYRDVR 243
Cdd:cd07522   81 YGQILRAYHGTRPLSDEEVREIYGSNNTGVRDDESRYYFLNTLFSLPEACLLAQLVDYFDNNPLE--SDMSYRSIYQDVR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 244 SAVDLCHRDGTLKRMVAKDPSRYINEDLAIVPMLEMIRKSGRSTFLVTNSLWDYTDVVMNYLCRPYTSDVSSshnhkWLG 323
Cdd:cd07522  159 AAVDWVHSKGLLKKKIMQDPERYVLRDPELPLLLSRLREAGKKLFLLTNSDYSYTNKGMKYLLGGFLPKHRD-----WRD 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 324 YFDVVITGSAKPGFFHDGNRagLFEVEPDSGKLlnADLHIGSPRSGqqpsrpihKIYQGGNVGHLHRLLSvASSSQILYV 403
Cdd:cd07522  234 YFDVVIVDARKPGFFTEGTP--FREVDTETGQL--KITKVGPLEKG--------KVYSGGNLKQFTELLG-WRGKEVLYF 300

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 222625883 404 GDHIYGDILRSKKVLGWRTMLVIPELEQEVKLLseSKSTRKELRHLR 450
Cdd:cd07522  301 GDHIYSDILKSKKRHGWRTALIVPELGSLFRTG--SNPTYFSSQVER 345
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
657-815 1.53e-93

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 289.86  E-value: 1.53e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 657 FERSINTLFLTEMVRGLMLTLKYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAE 736
Cdd:PRK05888   1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 737 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAANLESESLYR 815
Cdd:PRK05888  81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANYR 159
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 672-793 2.25e-65

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 213.43  E-value: 2.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883  672 GLMLTLKYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDID 751
Cdd:TIGR01971   1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 222625883  752 MTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKL 793
Cdd:TIGR01971  81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 713-785 4.80e-26

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: 101.75  E-value: 4.80e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEERedgsrrTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFATETHEE 785
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAITIEDGEP------GKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 669-798 3.10e-19

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 85.85  E-value: 3.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 669 MVRGLMLTLKYffeKNVTINYPFEKGPLSPRFRG--EHALrryptgeERCIACKLCEAICPAQAITIEAEEredgSRRTT 746
Cdd:PRK12387   1 MFKLIKKVIKT---GTATSSYPLEPIAVDKNFRGkpEYNP-------QQCIGCAACVNACPSNALTVETDL----ATGEL 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 222625883 747 RYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFAtetheelLYDKEKLLENGD 798
Cdd:PRK12387  67 AWEFNLGRCIFCGRCEEVCPTAAIKLSQEFELA-------VWKKEDLLQQSE 111
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 713-771 5.45e-18

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: 80.90  E-value: 5.45e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 771
Cdd:cd10549   77 EEKCIGCGLCVKVCPVDAITLEDE---------LEIVIDKEKCIGCGICAEVCPVNAIK 126
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 684-790 2.66e-17

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 80.57  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 684 NVTINYPFEKGPLSPRFRGEHALrryptGEERCIACKLCEAICPAQAITIEAEErEDGSRRttrYDIDMTKCIYCGFCQE 763
Cdd:PRK08222  13 TATVKYPFAPLEVSPGFRGKPDL-----MPSQCIACGACTCACPANALTIQTDD-QQNSRT---WQLYLGRCIYCGRCEE 83

                         90       100
                 ....*....|....*....|....*..
gi 222625883 764 ACPVDAIVEGPNFEFATeTHEELLYDK 790
Cdd:PRK08222  84 VCPTRAIQLTNNFELTV-TNKADLYTR 109
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
704-777 3.96e-17

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 76.31  E-value: 3.96e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222625883 704 HALRRYPTGEERCIACKLCEAICPAQAITIEAEeredgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGPNFE 777
Cdd:COG2768    1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDG----------KAVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 713-792 1.58e-16

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: 76.67  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCEAICPAQAITIEaeerEDGSRRTTRyDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEK 792
Cdd:cd10549    5 PEKCIGCGICVKACPTDAIELG----PNGAIARGP-EIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDEEK 79
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 713-778 3.02e-16

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 73.93  E-value: 3.02e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEF 778
Cdd:COG2221   14 EEKCIGCGLCVAVCPTGAISLDDG----------KLVIDEEKCIGCGACIRVCPTGAIKGEKPKKF 69
ndhI CHL00014
NADH dehydrogenase subunit I
 671-790 3.52e-16

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 76.72  E-value: 3.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 671 RGLMLTLKYFFEKNVTINYPFEKGPLSPRFRGehalrRYPTGEERCIACKLCEAICPAQAITIEAE-EREDGSRRTTRYD 749
Cdd:CHL00014  21 QGFMITLSHANRLPVTIQYPYEKLITSERFRG-----RIHFEFDKCIACEVCVRVCPIDLPVVDWKlETDIRKKRLLNYS 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 222625883 750 IDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDK 790
Cdd:CHL00014  96 IDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQ 136
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 716-769 1.05e-15

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: 71.79  E-value: 1.05e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 222625883  716 CIACKLCEAICPAQAITIEAEEREDGsrrTTRYDIDMTKCIYCGFCQEACPVDA 769
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 713-770 2.75e-15

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: 73.20  E-value: 2.75e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEaEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10549   39 EDKCVFCGACVEVCPTGAIELT-PEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
NapF COG1145
Ferredoxin [Energy production and conversion];
713-770 2.81e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 73.22  E-value: 2.81e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREdgsrrttrYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG1145  181 AEKCIGCGLCVKVCPTGAIRLKDGKPQ--------IVVDPDKCIGCGACVKVCPVGAI 230
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 713-771 3.33e-14

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 68.15  E-value: 3.33e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 713 EERCIACKLCEAICPAQAITIEaeereDGSRRttrydIDMTKCIYCGFCQEACPVDAIV 771
Cdd:COG4231   21 EDKCTGCGACVKVCPADAIEEG-----DGKAV-----IDPDLCIGCGSCVQVCPVDAIK 69
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 713-774 1.19e-13

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 66.29  E-value: 1.19e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 222625883 713 EERCIACKLCEAICPAQAITIEaeerEDGsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGP 774
Cdd:COG1149   10 EEKCIGCGLCVEVCPEGAIKLD----DGG-----APVVDPDLCTGCGACVGVCPTGAITLEE 62
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 713-771 2.61e-13

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: 65.84  E-value: 2.61e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 771
Cdd:COG1144   29 EDKCIGCGLCWIVCPDGAIRVDDG---------KYYGIDYDYCKGCGICAEVCPVKAIE 78
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 713-770 3.98e-13

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 64.73  E-value: 3.98e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgSRRTTRYDIDmtKCIYCGFCQEACPVDAI 770
Cdd:COG1146    7 TDKCIGCGACVEVCPVDVLELDEE-----GKKALVINPE--ECIGCGACELVCPVGAI 57
PRK13984 PRK13984
putative oxidoreductase; Provisional
 678-765 6.51e-12

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 69.03  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 678 KYFFEKNVTINYPFEKGPLSPRFRGEHAlrrypTGEERCIACKLCEAICPAQAIT-IEAEE--REDGSrRTTRYDIDMTK 754
Cdd:PRK13984  14 KFLFRKPVTIKVPNVKREAAERYRGFHI-----NDWEKCIGCGTCSKICPTDAITmVEVPDlpQEYGK-KPQRPVIDYGR 87

                         90
                 ....*....|.
gi 222625883 755 CIYCGFCQEAC 765
Cdd:PRK13984  88 CSFCALCVDIC 98
Fer4_9 pfam13187
4Fe-4S dicluster domain;
715-770 1.05e-11

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 60.26  E-value: 1.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883  715 RCIACKLCEAICPAQAItieaeeREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:pfam13187   1 KCTGCGACVAACPAGAI------VPDLVGQTIRGDIAGLACIGCGACVDACPRGAI 50
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 677-795 1.76e-10

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 59.08  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 677 LKYFFEKNVTINYP-FEKGPLSPRFRGEHALRRyptgeERCIACKLCEAICPAQAITIEAEERedgsrrttRYDIDMTKC 755
Cdd:PRK08348   9 LRNLFKKPATNLFPaTEPVPVPEDFRGKILYDV-----DKCVGCRMCVTVCPAGVFVYLPEIR--------KVALWTGRC 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 222625883 756 IYCGFCQEACPVDAIVEGPNFEFATETH--EELLYDKEKLLE 795
Cdd:PRK08348  76 VFCGQCVDVCPTGALQMSDDFLLASYDRfdEKFIPLKPEKVE 117
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
713-792 4.41e-10

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 62.74  E-value: 4.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREdgsrrttrydIDMTKCIYCGFCQEACPVDAIVEgpnfefATETHE--ELLYDK 790
Cdd:COG4624   90 KEKCKNCYPCVRACPVKAIKVDDGKAE----------IDEEKCISCGQCVAVCPFGAITE------KSDIEKvkKALKDP 153


                 ..
gi 222625883 791 EK 792
Cdd:COG4624  154 EK 155
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
716-772 6.55e-10

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 60.72  E-value: 6.55e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 716 CIACKLCEAICPAQAITIE---AEeredgsrrttrydIDMTKCIYCGFCQEACPVDAIVE 772
Cdd:PRK07118 215 CIGCGKCVKACPAGAITMEnnlAV-------------IDQEKCTSCGKCVEKCPTKAIRI 261
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 703-771 5.59e-09

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: 55.09  E-value: 5.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 703 EHALRRYPTG-----EERCIACKLCEAICPAQAITIEAEEREdgsrrttrydidMTKCIYCGF---------CQEACPVD 768
Cdd:cd04410   64 TGAIYKDEDGivlidEDKCIGCGSCVEACPYGAIVFDPEPGK------------AVKCDLCGDrldeglepaCVKACPTG 131


                 ...
gi 222625883 769 AIV 771
Cdd:cd04410  132 ALT 134
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 704-771 1.12e-08

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 55.72  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 704 HALRRYPTG-----EERCIACKLCEAICPAQAITIeaeEREDGSrrttrydidMTKCIYCGF---------CQEACPVDA 769
Cdd:COG0437   75 GATYKREDGivlvdYDKCIGCRYCVAACPYGAPRF---NPETGV---------VEKCTFCADrldegllpaCVEACPTGA 142


                 ..
gi 222625883 770 IV 771
Cdd:COG0437  143 LV 144
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
716-770 1.39e-08

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 54.28  E-value: 1.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222625883 716 CIACKL--CEAICPAQAITieaeeREDGsrrttRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG1142   52 CRHCEDapCAEVCPVGAIT-----RDDG-----AVVVDEEKCIGCGLCVLACPFGAI 98
PRK06273 PRK06273
ferredoxin; Provisional
 713-795 5.30e-08

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 53.18  E-value: 5.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCEAICPAQAIT---IEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIvegpnFEFATETH-----E 784
Cdd:PRK06273  48 EELCIGCGGCANVCPTKAIEmipVEPVKITEGYVKTKIPKIDYEKCVYCLYCHDFCPVFAL-----FNEISPIHprdvgE 122

                         90
                 ....*....|.
gi 222625883 785 ELLYDKEKLLE 795
Cdd:PRK06273 123 DIEVDVSKLLE 133
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
716-766 6.17e-08

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 50.18  E-value: 6.17e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  716 CIACKLCEAICPAQAITIEAEEREdgSRRTTRYDIDMTK--------------CIYCGFCQEACP 766
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGVLD--ARRCISYLTIEKKglipdelrcllgnrCYGCDICQDVCP 63
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
713-770 6.28e-08

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 56.02  E-value: 6.28e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG1148  495 PEKCTGCGRCVEVCPYGAISIDEK---------GVAEVNPALCKGCGTCAAACPSGAI 543
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
713-771 6.31e-08

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 52.35  E-value: 6.31e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDGSrrttrydidmTKCIYCGF------CQEACPVDAIV 771
Cdd:COG1142   80 EEKCIGCGLCVLACPFGAITMVGEKSRAVA----------VKCDLCGGreggpaCVEACPTGALR 134
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 713-766 6.93e-08

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: 49.56  E-value: 6.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  713 EERCIACKLCEAICPAQAITIEA-EEREDGSRRttryDIDMTKCIYCGFCQEACP 766
Cdd:pfam13237   6 PDKCIGCGRCTAACPAGLTRVGAiVERLEGEAV----RIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 713-771 1.00e-07

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: 52.26  E-value: 1.00e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIA------CKLCEAICPAQAITIEAEereDGSRRTTrydIDMTKCIYCGFCQEACPVD---AIV 771
Cdd:cd16373   90 KDRCLAwqggtdCGVCVEACPTEAIAIVLE---DDVLRPV---VDEDKCVGCGLCEYVCPVEppkAIV 151
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 707-771 1.03e-07

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: 51.42  E-value: 1.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 707 RRYPTGEERCIACKLCE-----AICPAQAITIEAEereDGSRRttrydIDMTKCIYCGFCQEACPVDAIV 771
Cdd:cd10550   37 RFEPEGLDVPVVCRQCEdapcvEACPVGAISRDEE---TGAVV-----VDEDKCIGCGMCVEACPFGAIR 98
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 713-770 1.28e-07

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: 51.49  E-value: 1.28e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIdMTKCIYCGF------CQEACPVDAI 770
Cdd:cd10554   84 EERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAV-AVKCDLCAGreggpaCVEACPTKAL 146
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 714-772 2.02e-07

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


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 54.14  E-value: 2.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883  714 ERCIACKLCE------AI----------CPAQAITIEaeerEDGsrrttRYDIDMTKCIYCGFCQEACPVDAIVE 772
Cdd:TIGR04105 142 EKCIECGKCKkacpynAIveierpcekaCPVGAISSD----EDG-----RAVIDYDKCISCGACMVACPFGAISD 207
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 714-779 2.05e-07

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: 51.76  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 714 ERCIACKLCEAICPAQAITI---EAEEREDGSRRTTRYdidMTKCIYC------G---FCQEACPVDAIVEG----PNFE 777
Cdd:cd10551   83 DKCIGCRYCMAACPYGARYFnpeEPHEFGEVPVRPKGV---VEKCTFCyhrldeGllpACVEACPTGARIFGdlddPNSE 159


                 ..
gi 222625883 778 FA 779
Cdd:cd10551  160 VS 161
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 748-770 4.14e-07

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: 46.47  E-value: 4.14e-07
                          10        20
                  ....*....|....*....|...
gi 222625883  748 YDIDMTKCIYCGFCQEACPVDAI 770
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAI 23
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 705-770 5.89e-07

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: 49.11  E-value: 5.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 705 ALRR-YPTG-----EERCIACKLCEAICPAQAITIEAEEREdgsrrttrydidMTKCIYCG---FCQEACPVDAI 770
Cdd:cd10550   65 AISRdEETGavvvdEDKCIGCGMCVEACPFGAIRVDPETGK------------AIKCDLCGgdpACVKVCPTGAL 127
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 722-770 6.39e-07

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 50.33  E-value: 6.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 222625883 722 CEAICPAQAITIeaeeREDGSRRttrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG0437   68 CVKVCPTGATYK----REDGIVL-----VDYDKCIGCRYCVAACPYGAP 107
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 717-770 6.80e-07

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: 49.16  E-value: 6.80e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 222625883 717 IACKLCEAICPAQAITIEAeeREDGSRRTTrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10564   86 VECRSCQDACPTQAIRFRP--RLGGIALPE---LDADACTGCGACVSVCPVGAI 134
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
713-770 7.10e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 51.60  E-value: 7.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQaITIEAEEredgsrrttrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG0348  209 RGDCIDCGLCVKVCPMG-IDIRKGE------------INQSECINCGRCIDACPKDAI 253
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 678-770 8.18e-07

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 51.01  E-value: 8.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 678 KYFFEKNVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAICPAQAITIEAEEREDGSrrttrydidmtKCIY 757
Cdd:NF038196 149 KKGPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGKPVWGH-----------NCTH 217

                         90
                 ....*....|...
gi 222625883 758 CGFCQEACPVDAI 770
Cdd:NF038196 218 CLACIHRCPKEAI 230
NapF COG1145
Ferredoxin [Energy production and conversion];
712-775 9.52e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.88  E-value: 9.52e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222625883 712 GEERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPN 775
Cdd:COG1145  141 EAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDG 204
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 715-770 1.34e-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: 48.79  E-value: 1.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 715 RCIACKLCEAICPAQAITIEAeeREDGSR--RTTRYDIDMTKCIYCG-FCQEACPVDAI 770
Cdd:cd16373   15 LCIRCGLCVEACPTGVIQPAG--LEDGLEggRTPYLDPREGPCDLCCdACVEVCPTGAL 71
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 716-770 1.44e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 48.04  E-value: 1.44e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 222625883 716 CIACKL--CEAICPAQAItieaEEREDGSrrtTRYDIDmtKCIYCGFCQEACPVDAI 770
Cdd:cd16370   53 CRACEDppCAEACPTGAL----EPRKGGG---VVLDKE--KCIGCGNCVKACIVGAI 100
PRK13795 PRK13795
hypothetical protein; Provisional
 669-767 1.73e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 51.53  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 669 MVRGLMLTLKYFFEKNVTInYPFEKGPLSPRFR-GEHALRRyptgEERCIACKLCEAICPAQAITIEAEERedgsrrttR 747
Cdd:PRK13795 540 MVLTKKGTVKVFASGNIWA-RSEDKEAAASLFKdAARLLRR----AAECVGCGVCVGACPTGAIRIEEGKR--------K 606

                         90       100
                 ....*....|....*....|
gi 222625883 748 YDIDMTKCIYCGFCQEACPV 767
Cdd:PRK13795 607 ISVDEEKCIHCGKCTEVCPV 626
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 715-770 2.18e-06

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 50.38  E-value: 2.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 715 RCIACKLCEAICPAQAItIEAEEREDGSR----RTTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:PRK14028 248 KCIMCRKCWLYCPDDAI-IEAWREAEGPRgrkfRMKMIDFDYQYCKGCGVCAEVCPTGAI 306
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
713-770 2.30e-06

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 46.86  E-value: 2.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIeaeeREDGSrrttrYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:PRK09623  50 ESKCVKCYICWKFCPEPAIYI----KEDGY-----VAIDYDYCKGCGICANECPTKAI 98
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 750-785 2.59e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 45.47  E-value: 2.59e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 222625883 750 IDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEE 785
Cdd:COG1146    5 IDTDKCIGCGACVEVCPVDVLELDEEGKKALVINPE 40
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 702-741 2.72e-06

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 45.47  E-value: 2.72e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 222625883 702 GEHALRRYPtgeERCIACKLCEAICPAQAITIEAEEREDG 741
Cdd:COG1146   31 GKKALVINP---EECIGCGACELVCPVGAITVEDDEPEEQ 67
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 717-771 4.10e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 47.17  E-value: 4.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 717 IACKLCE-----AICPAQAITIeaeeREDGsrrTTRYDIDmtKCIYCGFCQEACPVDAIV 771
Cdd:cd16371   52 MSCNHCEnpacvKVCPTGAITK----REDG---IVVVDQD--KCIGCGYCVWACPYGAPQ 102
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 715-770 4.51e-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: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 46.88  E-value: 4.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 715 RCIACK--LCEAICPAQAITIEaeerEDGSRRttrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd16374   42 RCRHCEdaPCMEVCPTGAIYRD----EDGAVL-----VDPDKCIGCGMCAMACPFGVP 90
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 705-770 4.75e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 46.50  E-value: 4.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222625883 705 ALRRYPTG-----EERCIACKLCEAICPAQAITIEAEeredgsrrtTRYDIdmtKCIYCGFCQEACPVDAI 770
Cdd:cd16370   69 ALEPRKGGgvvldKEKCIGCGNCVKACIVGAIFWDEE---------TNKPI---ICIHCGYCARYCPHDVL 127
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 716-774 5.00e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.87  E-value: 5.00e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 716 CIACKLCEAICPAQAITIEAEERedgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGP 774
Cdd:PRK12771 512 CFECDNCYGACPQDAIIKLGPGR--------RYHFDYDKCTGCHICADVCPCGAIEMGP 562
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 744-775 5.12e-06

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.03  E-value: 5.12e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 222625883 744 RTT--RYDIDMTKCIYCGFCQEACPVDAIVEGPN 775
Cdd:COG4231   11 RTTamRYVIDEDKCTGCGACVKVCPADAIEEGDG 44
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 715-768 5.17e-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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 44.61  E-value: 5.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222625883  715 RCIACKLCEAICPA---------QAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVD 768
Cdd:pfam13183   1 RCIRCGACLAACPVylvtggrfpGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVG 63
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 714-770 5.21e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 46.42  E-value: 5.21e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 714 ERCIACKLCEAIC---------PAQA-ITIEAEEREDgsrrttrYDIDMTkCIYCG--FCQEACPVDAI 770
Cdd:cd10550    6 EKCTGCRTCELACslkhegvfnPSLSrIRVVRFEPEG-------LDVPVV-CRQCEdaPCVEACPVGAI 66
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 722-770 8.23e-06

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: 47.14  E-value: 8.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 222625883 722 CEAICPAQAITIeaeeREDGsrrttRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10551   61 CVKVCPTGATYK----REDG-----IVLVDYDKCIGCRYCMAACPYGAR 100
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 735-781 8.87e-06

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: 44.66  E-value: 8.87e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 222625883 735 AEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI--VEGPNFEFATE 781
Cdd:COG1144   12 TAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIrvDDGKYYGIDYD 60
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
715-770 1.26e-05

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 48.48  E-value: 1.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883 715 RCIACKLCEAICPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG4624   53 RCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAI 108
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 705-781 1.68e-05

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: 45.34  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 705 ALRRYPTG-----EERCIACKLCEAICPAQAITIEAEEREdgsrrttrydidMTKCIYCG---------FCQEACPVDAI 770
Cdd:cd16374   59 AIYRDEDGavlvdPDKCIGCGMCAMACPFGVPRFDPSLKV------------AVKCDLCIdrrregklpACVEACPTGAL 126

                         90
                 ....*....|.
gi 222625883 771 VEGPNFEFATE 781
Cdd:cd16374  127 KFGDIEELLKE 137
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 713-771 1.76e-05

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: 45.07  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCE--------------------------------------------AICPAQAItieaEEREDGsrrttRY 748
Cdd:cd04410    5 LDRCIGCGTCEvackqehglrpgpdwsrikviegggleraflpvscmhcedppcvKACPTGAI----YKDEDG-----IV 75

                         90       100
                 ....*....|....*....|...
gi 222625883 749 DIDMTKCIYCGFCQEACPVDAIV 771
Cdd:cd04410   76 LIDEDKCIGCGSCVEACPYGAIV 98
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 750-771 2.34e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.79  E-value: 2.34e-05
                         10        20
                 ....*....|....*....|..
gi 222625883 750 IDMTKCIYCGFCQEACPVDAIV 771
Cdd:COG1149    8 IDEEKCIGCGLCVEVCPEGAIK 29
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 716-770 2.53e-05

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: 44.25  E-value: 2.53e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 716 CIACKLCEAICPAQAItIEAEEREDGSrrttrydidmtKCIYCGFCQEACPVDAI 770
Cdd:cd16372   79 CVGCLMCVGFCPEGAM-FKHEDYPEPF-----------KCIACGICVKACPTGAL 121
PRK09898 PRK09898
ferredoxin-like protein;
713-770 3.23e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 45.60  E-value: 3.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDgsrrttrydidmTKCIYCGFCQEACPVDAI 770
Cdd:PRK09898 153 HKRCIGCSACTTACPWMMATVNTESKKS------------SKCVLCGECANACPTGAL 198
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 713-741 3.86e-05

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.41  E-value: 3.86e-05
                         10        20
                 ....*....|....*....|....*....
gi 222625883 713 EERCIACKLCEAICPAQAITIeaEEREDG 741
Cdd:COG1149   40 PDLCTGCGACVGVCPTGAITL--EEREAG 66
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 711-775 4.43e-05

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: 43.86  E-value: 4.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222625883 711 TGEERCIACKLCEAICpAQAITIEaEEREDGSRRTTRYD--IDMTKCIYCGFCQEACPVDAIVEGPN 775
Cdd:cd16372    5 TDPEKCIGCLQCEEAC-SKTFFKE-EDREKSCIRITETEggYAINVCNQCGECIDVCPTGAITRDAN 69
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 716-771 5.64e-05

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: 43.48  E-value: 5.64e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 716 CIACKLCEAICPAQAITieaeeredgsrRTTR--YDIDMTKCIYCGFCQEACPVDAIV 771
Cdd:cd16372   49 CNQCGECIDVCPTGAIT-----------RDANgvVMINKKLCVGCLMCVGFCPEGAMF 95
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 713-770 5.84e-05

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: 45.37  E-value: 5.84e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 713 EERCIACKLCEAICPAQAITIEaeerEDGSRRttrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG2878  136 EYGCIGCGDCIKACPFDAIVGA----AKGMHT-----VDEDKCTGCGLCVEACPVDCI 184
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 713-771 6.96e-05

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: 44.02  E-value: 6.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883  713 EERCIACKLCEAICPAQAITieaeeredGSRRTTRYDIdMTKCIYCGFCQEACPVDAIV 771
Cdd:TIGR01944 112 EDNCIGCTKCIQACPVDAIV--------GAAKAMHTVI-ADECTGCDLCVEPCPTDCIE 161
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 707-770 7.81e-05

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: 43.39  E-value: 7.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 707 RRYPTGEE-----RCIACKLCEAICPAQAITIeaeeredGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10564    1 RPPWAVDEalfldLCTRCGDCVEACPEGIIVR-------GDGGFPELDFSRGECTFCGACAEACPEGAL 62
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 713-771 8.42e-05

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 42.32  E-value: 8.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEredgsrrttrYDI-DMTKCIYCGFCQEACPVDAIV 771
Cdd:PRK09624  50 RDKCVRCYLCYIYCPEPAIYLDEEG----------YPVfDYDYCKGCGICANECPTKAIE 99
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
645-768 1.06e-04

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 45.12  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 645 LAKEIAKDWNAVFerSINTLFLTEMVRGLMLTLKYFFEKNVTIN---YP---FEKGPLSPRFRGEHALRRYPTGEerCIA 718
Cdd:PRK12576  81 LVLDVAKKYNSVI--TIEPMDYFKVVKDLIVDFDEFYERMFKVKprlYRakeVLEGKAEHRLKPEDQKELWKFAQ--CIW 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 719 CKLCEAICPAQAITIE--------------AEEREDGSRRTTRYDIDMT-KCIYCGFCQEACPVD 768
Cdd:PRK12576 157 CGLCVSACPVVAIDPEflgpaahakgyrflADPRDTITEERMKILIDSSwRCTYCYSCSNVCPRD 221
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 713-739 1.19e-04

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 41.18  E-value: 1.19e-04
                         10        20
                 ....*....|....*....|....*..
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEERE 739
Cdd:COG4231   50 PDLCIGCGSCVQVCPVDAIKLEKRVPE 76
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 713-732 1.26e-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: 39.54  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|
gi 222625883  713 EERCIACKLCEAICPAQAIT 732
Cdd:pfam00037   5 EEKCIGCGACVEVCPVGAIT 24
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
713-748 1.40e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.87  E-value: 1.40e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDGSRRTTRY 748
Cdd:COG2768   39 PEKCIGCGACIEVCPVGAIKIEWEEDEEFQEKMAEY 74
PRK06991 PRK06991
electron transport complex subunit RsxB;
701-774 2.00e-04

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 44.01  E-value: 2.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 701 RGEHALRRYPTGEERCIAcKLCEAI-CPAqaITIEAEEREDGSRRTTRydIDMTKCIYCGFCQEACPVDAIVEGP 774
Cdd:PRK06991  37 AGEANYNRCPPGGAEGIA-RLAALLgKPV--IPLDPANGVERPRAVAV--IDEQLCIGCTLCMQACPVDAIVGAP 106
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 700-775 2.02e-04

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: 42.29  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 700 FRGEHALRRyptGEERCIACKLCEAICpaqaitieaEEREDGS----RRTTRYD-IDM-TKCIYC--GFCQEACPVDAIV 771
Cdd:cd16367    8 IQGTNLLVI---DLDRCIRCDNCEKAC---------ADTHDGHsrldRNGLRFGnLLVpTACRHCvdPVCMIGCPTGAIH 75


                 ....
gi 222625883 772 EGPN 775
Cdd:cd16367   76 RDDG 79
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 717-770 2.32e-04

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: 42.25  E-value: 2.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 717 IACKLCE-----AICPAQAITieaeeREDGSRRttrydIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10554   54 VQCRQCEdapcaNVCPVGAIS-----QEDGVVQ-----VDEERCIGCKLCVLACPFGAI 102
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 749-790 2.34e-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: 41.61  E-value: 2.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 222625883 749 DIDMTKCIYCGFCQEACPVDAIVEGPNfeFATETHEELLYDK 790
Cdd:cd10549    2 KYDPEKCIGCGICVKACPTDAIELGPN--GAIARGPEIDEDK 41
NapF COG1145
Ferredoxin [Energy production and conversion];
713-739 2.56e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 43.56  E-value: 2.56e-04
                         10        20
                 ....*....|....*....|....*..
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEERE 739
Cdd:COG1145  212 PDKCIGCGACVKVCPVGAISLEPKEIE 238
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 705-771 2.84e-04

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: 41.86  E-value: 2.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 705 ALRRYP-TG-----EERCIACKLCEAICPAQAITIEAEEREdgsrrttrydidMTKCIYCGF-----CQEACPVDAIV 771
Cdd:cd10563   73 AMHKDPeTGivihdEEKCVGCWMCVMVCPYGAIRPDKERKV------------ALKCDLCPDretpaCVEACPTGALV 138
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 722-770 3.20e-04

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: 41.90  E-value: 3.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 222625883 722 CEAICPAQAITIEaeerEDGSrrttrYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:cd10562   78 CVKVCPTGALYKT----ENGA-----VVVDEDKCIGCGYCVAACPFDVP 117
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 745-770 4.50e-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: 4.50e-04
                         10        20
                 ....*....|....*....|....*.
gi 222625883 745 TTRYDIDMTKCIYCGFCQEACPVDAI 770
Cdd:COG2221    7 TWPPKIDEEKCIGCGLCVAVCPTGAI 32
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
713-772 5.57e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 43.01  E-value: 5.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222625883 713 EERCIACKLCEAIC---PAQAITIEaeerEDGSRRttrYDIDMTKCIYCGFCQEACPVDAIVE 772
Cdd:PRK08318 341 QDKCIGCGRCYIACedtSHQAIEWD----EDGTRT---PEVIEEECVGCNLCAHVCPVEGCIT 396
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 750-776 5.66e-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: 41.32  E-value: 5.66e-04
                          10        20
                  ....*....|....*....|....*..
gi 222625883  750 IDMTKCIYCGFCQEACPVDAIVEGPNF 776
Cdd:TIGR01944 110 IDEDNCIGCTKCIQACPVDAIVGAAKA 136
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 713-734 6.94e-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: 40.46  E-value: 6.94e-04
                         10        20
                 ....*....|....*....|..
gi 222625883 713 EERCIACKLCEAICPAQAITIE 734
Cdd:cd10549  107 KEKCIGCGICAEVCPVNAIKLV 128
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 716-766 8.21e-04

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: 41.22  E-value: 8.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 222625883 716 CIACKL--CEAICPAQAITIEaeerEDGSRRTTrydiDMTKCIYCGFCQEACP 766
Cdd:cd16369   51 CMHCEDptCAEVCPADAIKVT----EDGVVQSA----LKPRCIGCSNCVNACP 95
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 705-773 1.21e-03

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: 40.08  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 705 ALRRYPTG-----EERCIACKLCEAICPAQAITIEAEeredgsrrttryDIDMTKCIYC------GF---CQEACPVDAI 770
Cdd:cd16366   86 AIIRTETGtvvvdPETCIGCGYCVNACPFDIPRFDEE------------TGRVAKCTLCydrisnGLqpaCVKTCPTGAL 153


                 ...
gi 222625883 771 VEG 773
Cdd:cd16366  154 TFG 156
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 713-784 1.31e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 38.93  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEeredgSRRTTRYDIDMT---KCIYCGFCQEACPVDAI--VEGPNFEFATETHE 784
Cdd:PRK09626  15 ESRCKACDICVSVCPAGVLAMRID-----PHAVLGKMIKVVhpeSCIGCRECELHCPDFAIyvADRKEFKFAKLSKE 86
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 713-770 1.33e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 42.43  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDGSRRTTRYdidmtKCIYCG------FCQEACPVDAI 770
Cdd:PRK12769  84 QQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH-----KCDLCAgrengpACVENCPADAL 142
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 715-768 1.33e-03

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: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 37.83  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883  715 RCIACKLCEAICP-AQAITIE----AEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVD 768
Cdd:pfam13534   1 RCIQCGCCVDECPrYLLNGDEpkklMRAAYLGDLEELQANKVANLCSECGLCEYACPMG 59
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 716-796 1.88e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 41.53  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 716 CIACKLCEAICPAQAIT-------------IEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnfefATET 782
Cdd:PRK06259 135 CIECLSCVSTCPARKVSdypgptfmrqlarFAFDPRDEGDREKEAFDEGLYNCTTCGKCVEVCPKEIDIPGK----AIEK 210

                         90
                 ....*....|....
gi 222625883 783 HEELLYDKEKLLEN 796
Cdd:PRK06259 211 LRALAFKKGLGLPA 224
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 750-770 1.93e-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: 36.05  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|.
gi 222625883  750 IDMTKCIYCGFCQEACPVDAI 770
Cdd:pfam12837   4 VDPDKCIGCGRCVVVCPYGAI 24
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 714-774 1.94e-03

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: 40.06  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222625883 714 ERCIACKLCEAICpaqaitiEAEEREDGSRRTTRYDID--------MTKCIYC--GFCQEACPVDAIVEGP 774
Cdd:cd16369    9 SRCIGCRACVAAC-------RECGTHRGKSMIHVDYIDrgestqtaPTVCMHCedPTCAEVCPADAIKVTE 72
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 713-731 1.95e-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: 36.05  E-value: 1.95e-03
                          10
                  ....*....|....*....
gi 222625883  713 EERCIACKLCEAICPAQAI 731
Cdd:pfam12837   6 PDKCIGCGRCVVVCPYGAI 24
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 714-776 2.03e-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: 39.55  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 222625883 714 ERCIACKLCEAICpAQAitieAEEREDGSRRTTRYDI----------DMTKCIYC-----GFCQEACPVDAIVEGPNF 776
Cdd:cd10554    7 DKCIGCRTCEVAC-AAA----HSGKGIFEAGTDGLPFlprlrvvktgEVTAPVQCrqcedAPCANVCPVGAISQEDGV 79
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 713-774 2.28e-03

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: 39.59  E-value: 2.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 222625883 713 EERCIACKLCEAICPAQAItieaeeredgsrRTTRYDIDMTKCIYC------GF---CQEACPVDAIVEGP 774
Cdd:cd10562   99 EDKCIGCGYCVAACPFDVP------------RYDETTNKITKCTLCfdrienGMqpaCVKTCPTGALTFGD 157
PRK06991 PRK06991
electron transport complex subunit RsxB;
713-770 2.40e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.55  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883 713 EERCIACKLCEAICPAQAI--------TIEAEEredgsrrttrydidmtkCIYCGFCQEACPVDAI 770
Cdd:PRK06991  84 EQLCIGCTLCMQACPVDAIvgapkqmhTVLADL-----------------CTGCDLCVPPCPVDCI 132
Fer COG1141
Ferredoxin [Energy production and conversion];
713-770 2.51e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440756 [Multi-domain]  Cd Length: 63  Bit Score: 36.78  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 222625883 713 EERCIACKLCEAICP----------AQAI--TIEAEEREDgsrrttrydidmtkciycgfCQEA---CPVDAI 770
Cdd:COG1141    7 RDTCIGCGLCVALAPevfeldddgkAVVLdeEVPEELEED--------------------VREAadaCPVGAI 59
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 713-777 2.58e-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: 40.36  E-value: 2.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883 713 EERCIACKLCEAICPAQAITIEAEEREDgSRRTTRYDIDMTKCIYC-GFCQEACPVDAIVEGPNFE 777
Cdd:COG2878  166 EDKCTGCGLCVEACPVDCIEMVPVSPTV-VVSSWDKGKAVRKVVGCiGLCCKKCCPAAAITVNNLA 230
PRK09898 PRK09898
ferredoxin-like protein;
714-766 2.75e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 39.82  E-value: 2.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 222625883 714 ERCIACK--LCEAICPAQAITIEAEEredGSrrttrYDIDMTKCIYCGFCQEACP 766
Cdd:PRK09898 121 DTCRQCKepQCMNVCPIGAITWQQKE---GC-----ITVDHKRCIGCSACTTACP 167
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 701-782 2.81e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 40.25  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 701 RG-EHA---------LRRYP--TGEERCIACKLCEAICPAQAITIEAEEREDGsrrttrydiDMTKCIYCGFCQEACPVD 768
Cdd:PRK00783 144 RGkEHAkwqpgsacgYKYYPriEVSEDCDECEKCVEACPRGVLELKEGKLVVT---------DLLNCSLCKLCERACPGK 214

                         90
                 ....*....|....*..
gi 222625883 769 AIVEG--PN-FEFATET 782
Cdd:PRK00783 215 AIRVSddENkFIFTVES 231
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 713-795 3.14e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 40.57  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222625883 713 EERCIACKLCEAICPAQAI---------------TIE------AEEREdgsrrttrydiDMTKCIY-CGFCQEACPVdai 770
Cdd:COG1600  183 EDHCGSCTRCLDACPTGAIvapyvldarrcisylTIElkgpipEELRP-----------KMGNRIYgCDDCQDVCPW--- 248

                         90       100
                 ....*....|....*....|....*
gi 222625883 771 vegpNfEFATETHEELLYDKEKLLE 795
Cdd:COG1600  249 ----N-RFAQPTREPDFQPRPELAA 268
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 715-780 3.26e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 37.62  E-value: 3.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 222625883  715 RCIACKLCEAICPAQAItieaeEREDGSRRTTRydIDMTKCIYCGFCQEACPVDAIveGPNFEFAT 780
Cdd:TIGR00402  35 VCTRCGECASACENNIL-----QLGQQGQPTVE--FDNAECDFCGKCAEACPTNAF--HPRFPGDW 91
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 719-778 3.83e-03

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: 38.78  E-value: 3.83e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 222625883 719 CKLCEAICPAQAITIEAEERED---GsrrTTRYDIDmtKCI-Y-----CGFCQEACPVDAIVEGPNFEF 778
Cdd:cd16373   59 CDACVEVCPTGALRPLDLEEQKvkmG---VAVIDKD--RCLaWqggtdCGVCVEACPTEAIAIVLEDDV 122
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 714-737 4.57e-03

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: 36.95  E-value: 4.57e-03
                         10        20
                 ....*....|....*....|....
gi 222625883 714 ERCIACKLCEAICPAQAITIEAEE 737
Cdd:COG1144   60 DYCKGCGICAEVCPVKAIEMVPEE 83
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 754-800 6.01e-03

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: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 36.13  E-value: 6.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 222625883  754 KCIYCGFCQEACPVdAIVEGPNFEFAT-ETHEELLYDKEKLLENGDRW 800
Cdd:pfam13183   1 RCIRCGACLAACPV-YLVTGGRFPGDPrGGAAALLGRLEALEGLAEGL 47
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 750-771 6.84e-03

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 38.39  E-value: 6.84e-03
                         10        20
                 ....*....|....*....|..
gi 222625883 750 IDMTKCIYCGFCQEACPVDAIV 771
Cdd:PRK05113 111 IDEDNCIGCTKCIQACPVDAIV 132
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 750-775 9.32e-03

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: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 35.33  E-value: 9.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 222625883  750 IDMTKCIYCGFCQEACP---VDAIVEGPN 775
Cdd:pfam14697   3 IDEDTCIGCGKCYIACPdtsHQAIVGDGK 31
 
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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