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Conserved domains on  [gi|899702687|gb|KMY40207|]
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hypothetical protein ACH48_00495 [Aeromonas caviae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
activase_YjjW super family cl37373
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 2-280 9.68e-147

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


The actual alignment was detected with superfamily member TIGR04041:

Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 412.41  E-value: 9.68e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    2 SRWLPFSCVDGPGNRLVLFLQGCNFRCPGCHNPHTMGLCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPR 81
Cdd:TIGR04041   5 NKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIKVCPH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   82 HASPKTRQMSVAEVLALLRRYGPLLTGVTVSGGEATTQLPFVIALFTAIKAapdlARLTCLLDSNGSLGETGWQRLLPVL 161
Cdd:TIGR04041  85 QSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKA----AGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  162 DGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATgaleEALTTFLLSLGP-VPIRLN 240
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEI----DGLARFLGDLPSdTRIKLI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 899702687  241 GFRHHGVRGEALSWPEAGSADLTVLANALKAKGFGSVMLP 280
Cdd:TIGR04041 237 AFRHHGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
 
Name Accession Description Interval E-value
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 2-280 9.68e-147

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


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 412.41  E-value: 9.68e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    2 SRWLPFSCVDGPGNRLVLFLQGCNFRCPGCHNPHTMGLCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPR 81
Cdd:TIGR04041   5 NKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIKVCPH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   82 HASPKTRQMSVAEVLALLRRYGPLLTGVTVSGGEATTQLPFVIALFTAIKAapdlARLTCLLDSNGSLGETGWQRLLPVL 161
Cdd:TIGR04041  85 QSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKA----AGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  162 DGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATgaleEALTTFLLSLGP-VPIRLN 240
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEI----DGLARFLGDLPSdTRIKLI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 899702687  241 GFRHHGVRGEALSWPEAGSADLTVLANALKAKGFGSVMLP 280
Cdd:TIGR04041 237 AFRHHGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 4-279 3.02e-60

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 191.17  E-value: 3.02e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   4 WLPFSCVDGPG-NRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWQaelcthcdrcldvcpRH 82
Cdd:COG1180   10 ISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEI---------------------------SQ---------------GR 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  83 ASPKTRQMSVAEVLALLRRYGPLLT---GVTVSGGEATTQLPFVIALFTAIKAApdlaRLTCLLDSNGSLGETGWQRLLP 159
Cdd:COG1180   48 PDAAGRELSPEELVEEALKDRGFLDscgGVTFSGGEPTLQPEFLLDLAKLAKEL----GLHTALDTNGYIPEEALEELLP 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687 160 VLDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDatgalE-EALTTFLLSLGPV-PI 237
Cdd:COG1180  124 YLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSEE-----ElEAIARFIAELGDViPV 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 899702687 238 RLNGFRHHgvrGEALSWPEAGSADLTVLANALKAKGFGSVML 279
Cdd:COG1180  199 HLLPFHPL---YKLEDVPPPSPETLERAREIAREYGLKYVYI 237
pflA PRK11145
pyruvate formate lyase 1-activating protein;
8-223 3.19e-21

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 89.70  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   8 SC--VDGPGNRLVLFLQGCNFRCPGCHNphtmglcdhcgdcvpgcpgralamqegRVSWQaelcTHcdrcldvcprhasp 85
Cdd:PRK11145  12 SCgtVDGPGIRFITFFQGCLMRCLYCHN---------------------------RDTWD----TH-------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  86 KTRQMSVAEVLALLRRYGPLLT----GVTVSGGEATTQLPFVIALFTAIKAApdlARLTClLDSNG-------SLGEtgw 154
Cdd:PRK11145  47 GGKEVTVEELMKEVVTYRHFMNasggGVTASGGEAILQAEFVRDWFRACKKE---GIHTC-LDTNGfvrrydpVIDE--- 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899702687 155 qrLLPVLDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATGALEE 223
Cdd:PRK11145 120 --LLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLAKRNQKTWIRYVVVPGWTDDDDSAHRLGE 186
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 10-132 1.26e-10

4Fe-4S single cluster 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: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 57.95  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   10 VDGPGNRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWqaelcthcdrcldvCPRHASPKTRQ 89
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPET---------------------------W--------------DFKYGKPFTEE 39

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 899702687   90 MsVAEVLALLRryGPLLTGVTVSGGEATTQLPFVIALFTAIKA 132
Cdd:pfam13353  40 L-EDEIIEDLA--KPYIQGLTLSGGEPLLNAEALLELVKRVRE 79
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 40-83 6.46e-06

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: 46.39  E-value: 6.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQAElCTHCDRCLDVCPRHA 83
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPVWGHN-CTHCLACIHRCPKEA 229
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 40-83 2.07e-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: 43.53  E-value: 2.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 899702687  40 CDHCGD--CVPGCPGRALAMQE-GRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:cd04410   50 CMHCEDppCVKACPTGAIYKDEdGIVLIDEDKCIGCGSCVEACPYGA 96
 
Name Accession Description Interval E-value
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 2-280 9.68e-147

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


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 412.41  E-value: 9.68e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    2 SRWLPFSCVDGPGNRLVLFLQGCNFRCPGCHNPHTMGLCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPR 81
Cdd:TIGR04041   5 NKIIPFSCVDGPGNRLAIFLQGCNFDCKYCHNPETINHCDHCGDCVAGCPAGALSLVDGKVVWDKERCIGCDTCIKVCPH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   82 HASPKTRQMSVAEVLALLRRYGPLLTGVTVSGGEATTQLPFVIALFTAIKAapdlARLTCLLDSNGSLGETGWQRLLPVL 161
Cdd:TIGR04041  85 QSSPKTKEYTVEELLDRIRKNMPFIRGITVSGGECTLQLDFLTELFKAIKA----AGLTCFIDSNGSLDLTGWPKLLPVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  162 DGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATgaleEALTTFLLSLGP-VPIRLN 240
Cdd:TIGR04041 161 DGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEI----DGLARFLGDLPSdTRIKLI 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 899702687  241 GFRHHGVRGEALSWPEAGSADLTVLANALKAKGFGSVMLP 280
Cdd:TIGR04041 237 AFRHHGVRGEALEWPSPTDEQMEELAEALIKRGFRDIILP 276
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 4-279 3.02e-60

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 191.17  E-value: 3.02e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   4 WLPFSCVDGPG-NRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWQaelcthcdrcldvcpRH 82
Cdd:COG1180   10 ISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEI---------------------------SQ---------------GR 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  83 ASPKTRQMSVAEVLALLRRYGPLLT---GVTVSGGEATTQLPFVIALFTAIKAApdlaRLTCLLDSNGSLGETGWQRLLP 159
Cdd:COG1180   48 PDAAGRELSPEELVEEALKDRGFLDscgGVTFSGGEPTLQPEFLLDLAKLAKEL----GLHTALDTNGYIPEEALEELLP 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687 160 VLDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDatgalE-EALTTFLLSLGPV-PI 237
Cdd:COG1180  124 YLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSEE-----ElEAIARFIAELGDViPV 198

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 899702687 238 RLNGFRHHgvrGEALSWPEAGSADLTVLANALKAKGFGSVML 279
Cdd:COG1180  199 HLLPFHPL---YKLEDVPPPSPETLERAREIAREYGLKYVYI 237
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
 7-213 6.23e-36

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 130.15  E-value: 6.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    7 FSCVDGPGNRLVLFLQGCNFRCPGCHNPHTM----------GLCDHCGDCVPGCP---GRALAMQEGRV--SWQAELCTH 71
Cdd:TIGR02494   7 YSVHDGPGIRTTVFLKGCPLRCKWCSNPESQrkspellfkeNRCLGCGKCVEVCPagtARLSELADGRNriIIRREKCTH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   72 CDRCLDVCPRHA-SPKTRQMSVAEVLALLRR----YGPLLTGVTVSGGEATTQLPFVIALFTAIKAAP-DLARLTCLLDS 145
Cdd:TIGR02494  87 CGKCTEACPSGAlSIVGEEMTVEEVMRVVLRdsifYRNSGGGVTLSGGEPLLQPEFALALLQACHERGiHTAVETSGFTP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899702687  146 NGSLgetgwQRLLPVLDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSD 213
Cdd:TIGR02494 167 WETI-----EKVLPYVDLFLFDIKHLDDERHKEVTGVDNEPILENLEALAAAGKNVVIRIPVIPGFND 229
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
 7-228 2.23e-34

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 124.40  E-value: 2.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    7 FSCVDGPGNRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWqaelcthcdrcldvCPRHASPk 86
Cdd:TIGR02493   8 MGTVDGPGIRFVVFMQGCPLRCQYCHNPDT---------------------------W--------------DLKGGTE- 45

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   87 trqMSVAEVLALLRRYGPLLT----GVTVSGGEATTQLPFVIALFTAIKAapdLARLTClLDSNGSLGETG--WQRLLPV 160
Cdd:TIGR02493  46 ---VTPEELIKEVGSYKDFFKasggGVTFSGGEPLLQPEFLSELFKACKE---LGIHTC-LDTSGFLGGCTeaADELLEY 118

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 899702687  161 LDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATGALEEALTTF 228
Cdd:TIGR02493 119 TDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRNKPIWIRYVLVPGYTDSEEDIEALAEFVKTL 186
pflA PRK11145
pyruvate formate lyase 1-activating protein;
8-223 3.19e-21

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 89.70  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   8 SC--VDGPGNRLVLFLQGCNFRCPGCHNphtmglcdhcgdcvpgcpgralamqegRVSWQaelcTHcdrcldvcprhasp 85
Cdd:PRK11145  12 SCgtVDGPGIRFITFFQGCLMRCLYCHN---------------------------RDTWD----TH-------------- 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  86 KTRQMSVAEVLALLRRYGPLLT----GVTVSGGEATTQLPFVIALFTAIKAApdlARLTClLDSNG-------SLGEtgw 154
Cdd:PRK11145  47 GGKEVTVEELMKEVVTYRHFMNasggGVTASGGEAILQAEFVRDWFRACKKE---GIHTC-LDTNGfvrrydpVIDE--- 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 899702687 155 qrLLPVLDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGRSDFLDATGALEE 223
Cdd:PRK11145 120 --LLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYLAKRNQKTWIRYVVVPGWTDDDDSAHRLGE 186
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 1-210 2.91e-16

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 75.09  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    1 MSRWLPFSCVDGPGN-RLVLFLQGCNFRCPGCHNPhtmglcdhcgdcvpgcpgrALAMQEGrvswqaelcthcdrcldvc 79
Cdd:TIGR02495   2 IAGLVPFSTVDYPGKlAFTIFLQGCNLKCPYCHNP-------------------LLIPRRG------------------- 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   80 prhaspkTRQMSVAEVLALLRRYGPLLTGVTVSGGEATTQLPFVIALFTAIKaapdlARLTCLLDSNGSLGETgWQRLLP 159
Cdd:TIGR02495  44 -------SGEIEVEELLEFLRRRRGLLDGVVITGGEPTLQAGLPDFLREVRE-----LGFEVKLDTNGSNPRR-LEELLE 110

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 899702687  160 --VLDGAMIDLKGWREPVHLALtgwGRE------RVLASLQLLAQAGKLAEVRLLLVPG 210
Cdd:TIGR02495 111 egLVDYVAMDVKAPPEKYGELY---GLEkngaakNILKSLEILLESGIPFELRTTVVRG 166
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 10-132 1.26e-10

4Fe-4S single cluster 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: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 57.95  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687   10 VDGPGNRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWqaelcthcdrcldvCPRHASPKTRQ 89
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPET---------------------------W--------------DFKYGKPFTEE 39

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 899702687   90 MsVAEVLALLRryGPLLTGVTVSGGEATTQLPFVIALFTAIKA 132
Cdd:pfam13353  40 L-EDEIIEDLA--KPYIQGLTLSGGEPLLNAEALLELVKRVRE 79
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 6-132 3.81e-10

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 57.36  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687    6 PFSCVDGPGNRLVLFLQGCNFRCPGCHNPHTmglcdhcgdcvpgcpgralamqegrvsWQaelcthcdrcldvcPRHASP 85
Cdd:TIGR02491   7 PDDIVNGEGIRVSLFVAGCKHHCEGCFNKET---------------------------WN--------------FNGGKE 45

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 899702687   86 KTRQMsVAEVLALLRRYgPLLTGVTVSGGEATTQ--LPFVIALFTAIKA 132
Cdd:TIGR02491  46 FTEAL-EKEIIRDLNDN-PLIDGLTLSGGDPLYPrnVEELIELVKKIKA 92
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 39-83 2.04e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 52.75  E-value: 2.04e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG2221   16 KCIGCGLCVAVCPTGAISLDDGKLVIDEEKCIGCGACIRVCPTGA 60
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 39-83 5.66e-09

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 51.65  E-value: 5.66e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEGR-VSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG1149   12 KCIGCGLCVEVCPEGAIKLDDGGaPVVDPDLCTGCGACVGVCPTGA 57
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 40-83 1.11e-08

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 51.20  E-value: 1.11e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG4231   24 CTGCGACVKVCPADAIEEGDGKAVIDPDLCIGCGSCVQVCPVDA 67
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
39-83 2.20e-08

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 50.11  E-value: 2.20e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG2768   12 KCIGCGACVKVCPVGAISIEDGKAVIDPEKCIGCGACIEVCPVGA 56
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 40-83 4.79e-08

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: 48.68  E-value: 4.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 899702687   40 CDHCGDCVPGCPGRALAMQE-----GRVSWQ--AELCTHCDRCLDVCPRHA 83
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEvgekkGTKTVVidPERCVGCGACVAVCPTGA 51
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
9-83 1.84e-07

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 51.95  E-value: 1.84e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899702687   9 CVDGPGNRLVLFLQGCNFRCPGCHNPHTmgLCDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG4624   64 CCVAISCIQVRGIIIIDKRGPSIIRDKE--KCKNCYPCVRACPVKAIKVDDGKAEIDEEKCISCGQCVAVCPFGA 136
NapF COG1145
Ferredoxin [Energy production and conversion];
40-83 1.99e-07

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 50.88  E-value: 1.99e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQ--AELCTHCDRCLDVCPRHA 83
Cdd:COG1145  184 CIGCGLCVKVCPTGAIRLKDGKPQIVvdPDKCIGCGACVKVCPVGA 229
PRK13795 PRK13795
hypothetical protein; Provisional
 39-80 6.26e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 50.38  E-value: 6.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEG--RVSWQAELCTHCDRCLDVCP 80
Cdd:PRK13795 582 ECVGCGVCVGACPTGAIRIEEGkrKISVDEEKCIHCGKCTEVCP 625
Fer4_9 pfam13187
4Fe-4S dicluster domain;
40-83 8.18e-07

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 45.24  E-value: 8.18e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 899702687   40 CDHCGDCVPGCP----GRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:pfam13187   2 CTGCGACVAACPagaiVPDLVGQTIRGDIAGLACIGCGACVDACPRGA 49
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 25-83 1.02e-06

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 48.10  E-value: 1.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899702687  25 NFRCPGCHNPHtmgLCDHCGDCVPGCPGRALAMQ----EGRVSWQAEL--CTHCDRCLDVCPRHA 83
Cdd:PRK12387  28 NFRGKPEYNPQ---QCIGCAACVNACPSNALTVEtdlaTGELAWEFNLgrCIFCGRCEEVCPTAA 89
PRK10076 PRK10076
pyruvate formate lyase II activase; Provisional
 74-246 4.96e-06

pyruvate formate lyase II activase; Provisional


Pssm-ID: 182224 [Multi-domain]  Cd Length: 213  Bit Score: 46.30  E-value: 4.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687  74 RCLDVCPRHASPKT-RQMSVAEVLALLRR----YGPLLTGVTVSGGEATTQLPFVIALFTAIKAAPdlarLTCLLDSNgs 148
Cdd:PRK10076   2 RDADECPSGAFERIgRDITLDALEREVMKddifFRTSGGGVTLSGGEVLMQAEFATRFLQRLRLWG----VSCAIETA-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 899702687 149 lGETGWQRLLPV---LDGAMIDLKGWREPVHLALTGWGRERVLASLQLLAQAGKLAEVRLLLVPGrsdFLDATGALEEAL 225
Cdd:PRK10076  76 -GDAPASKLLPLaklCDEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPG---FTLSRENMQQAL 151

                        170       180
                 ....*....|....*....|.
gi 899702687 226 tTFLLSLGPVPIRLNGFRHHG 246
Cdd:PRK10076 152 -DVLIPLGIKQIHLLPFHQYG 171
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 40-83 6.46e-06

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: 46.39  E-value: 6.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQAElCTHCDRCLDVCPRHA 83
Cdd:NF038196 187 CIGCGICAKVCPVNNIEMEDGKPVWGHN-CTHCLACIHRCPKEA 229
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 40-83 2.07e-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: 43.53  E-value: 2.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 899702687  40 CDHCGD--CVPGCPGRALAMQE-GRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:cd04410   50 CMHCEDppCVKACPTGAIYKDEdGIVLIDEDKCIGCGSCVEACPYGA 96
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 39-80 3.31e-05

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


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 40.70  E-value: 3.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 899702687   39 LCDHCGDCVPGCP-------GRALAMQEGRVSWQAELCTHCDRCLDVCP 80
Cdd:pfam13237   8 KCIGCGRCTAACPagltrvgAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 40-83 3.59e-05

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 44.11  E-value: 3.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQAEL-CTHCDRCLDVCPRHA 83
Cdd:PRK00783 171 CDECEKCVEACPRGVLELKEGKLVVTDLLnCSLCKLCERACPGKA 215
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
22-82 3.89e-05

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 44.15  E-value: 3.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 899702687  22 QGCNFRCPGChnphtmglcdhcGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRH 82
Cdd:PRK07118 135 KGCSYGCLGL------------GSCVAACPFDAIHIENGLPVVDEDKCTGCGACVKACPRN 183
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 39-83 6.83e-05

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 40.08  E-value: 6.83e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 899702687  39 LCDHCGDCVPGCPGRALAMQ-EGRVSWQA--ELCTHCDRCLDVCPRHA 83
Cdd:COG1146    9 KCIGCGACVEVCPVDVLELDeEGKKALVInpEECIGCGACELVCPVGA 56
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
38-83 7.03e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.13  E-value: 7.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 899702687  38 GLCDHCGDCVPGCPGRaLAMQEGRVSwQAElCTHCDRCLDVCPRHA 83
Cdd:COG0348  210 GDCIDCGLCVKVCPMG-IDIRKGEIN-QSE-CINCGRCIDACPKDA 252
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
6-40 7.71e-05

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 41.90  E-value: 7.71e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 899702687   6 PFSCVDGPGNRLVLFLQGCNFRCPGCHNPHTMGLC 40
Cdd:PRK11121   8 PVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLN 42
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 39-83 9.31e-05

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 41.23  E-value: 9.31e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEG---RVSwqAELCTHCDRCLDVCPRHA 83
Cdd:cd10549   79 KCIGCGLCVKVCPVDAITLEDEleiVID--KEKCIGCGICAEVCPVNA 124
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 40-80 1.03e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 43.48  E-value: 1.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 899702687  40 CDHCGD--CVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCP 80
Cdd:PRK12809  56 CHHCNNapCVTACPVNALTFQSDSVQLDEQKCIGCKRCAIACP 98
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 40-83 1.28e-04

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 41.66  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 899702687  40 CDHCGDCVPGCPGRALAM----QEGRVSWQAEL--CTHCDRCLDVCPRHA 83
Cdd:PRK08222  40 CIACGACTCACPANALTIqtddQQNSRTWQLYLgrCIYCGRCEEVCPTRA 89
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 40-83 1.96e-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: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEG-----RVSWQAELCTHCDRCLDVCPRHA 83
Cdd:cd10549    8 CIGCGICVKACPTDAIELGPNgaiarGPEIDEDKCVFCGACVEVCPTGA 56
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
40-83 2.98e-04

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 41.46  E-value: 2.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:PRK07118 215 CIGCGKCVKACPAGAITMENNLAVIDQEKCTSCGKCVEKCPTKA 258
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
39-83 4.59e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 39.64  E-value: 4.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 899702687  39 LCDHCGD--CVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG1142   51 QCRHCEDapCAEVCPVGAITRDDGAVVVDEEKCIGCGLCVLACPFGA 97
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 39-80 5.91e-04

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: 39.15  E-value: 5.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEG---RVSWQAELCTHCDRCLDVCP 80
Cdd:cd10564   14 LCTRCGDCVEACPEGIIVRGDGgfpELDFSRGECTFCGACAEACP 58
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 39-80 6.65e-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: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 38.79  E-value: 6.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 899702687  39 LCDHCGDCVPGCPGRALAMQEGrvSWQAELCTHCDRCLDVCP 80
Cdd:cd16370   84 KCIGCGNCVKACIVGAIFWDEE--TNKPIICIHCGYCARYCP 123
PhsB_like cd10553
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ...
 40-83 1.11e-03

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


Pssm-ID: 319875 [Multi-domain]  Cd Length: 146  Bit Score: 38.50  E-value: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 899702687  40 CDHCGD--CVPGCPGRALAMQE--GRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:cd10553   58 CFHCENpwCVKACPTGAMQKREkdGIVYVDQELCIGCKACIEACPWGI 105
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 33-83 1.14e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 38.09  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 899702687  33 NPHTMGLCDHCGDCVPGCPGRALAM-QEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:cd16372   42 GGYAINVCNQCGECIDVCPTGAITRdANGVVMINKKLCVGCLMCVGFCPEGA 93
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 40-80 1.30e-03

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


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 39.29  E-value: 1.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  40 CDHCGD--CVPGCP--GRALAMQEGRVSWQAELCTHCDRCLDVCP 80
Cdd:cd10558   70 CMHCADpgCLKACPspGAIVQYANGIVDFQSDKCIGCGYCIKGCP 114
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 40-80 1.54e-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: 36.29  E-value: 1.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 899702687   40 CDHCGDCVPGCP------------GRALAMQEGRVSWQ---AELCTHCDRCLDVCP 80
Cdd:pfam13534   2 CIQCGCCVDECPryllngdepkklMRAAYLGDLEELQAnkvANLCSECGLCEYACP 57
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 40-82 2.27e-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: 38.82  E-value: 2.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRVSW-QAELCTHCDRCLDVCPRH 82
Cdd:COG2878  139 CIGCGDCIKACPFDAIVGAAKGMHTvDEDKCTGCGLCVEACPVD 182
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 40-80 3.22e-03

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 38.52  E-value: 3.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 899702687  40 CDHCGDCVPGCP-------------GRALAMQE---GRVSWQAE--------LCTHCDRCLDVCP 80
Cdd:COG0247   80 CVGCGFCRAMCPsykatgdekdsprGRINLLREvleGELPLDLSeevyevldLCLTCKACETACP 144
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 40-80 3.52e-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: 37.28  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGD--CVPGCPGRALAMQE-GRVSWQAELCTHCDRCLDVCP 80
Cdd:cd10562   70 CMHCTDaaCVKVCPTGALYKTEnGAVVVDEDKCIGCGYCVAACP 113
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 26-80 5.74e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 38.19  E-value: 5.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 899702687  26 FRCPGCHNPHTmglCDHCGD--CVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCP 80
Cdd:PRK12769  45 IKHQQQRSAVT---CHHCEDapCARSCPNGAISHVDDSIQVNQQKCIGCKSCVVACP 98
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 40-83 5.97e-03

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


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 36.45  E-value: 5.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGDCVPGCPGRALAMQEGRvSWQ-----AELC-----THCDRCLDVCPRHA 83
Cdd:cd10564   47 CTFCGACAEACPEGALDPAREA-PWPlraeiGDSClalqgVECRSCQDACPTQA 99
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 40-80 6.90e-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: 36.22  E-value: 6.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 899702687  40 CDHCGD--CVPGCPGRALAMQE-GRVSWQAELCTHCDRCLDVCP 80
Cdd:cd16366   70 CMHCTDagCLAACPTGAIIRTEtGTVVVDPETCIGCGYCVNACP 113
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 39-80 7.00e-03

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 36.85  E-value: 7.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 899702687  39 LCDHCGD--CVPGCPGRALAMQE-GRVSWQAELCTHCDRCLDVCP 80
Cdd:COG0437   59 LCNHCDDppCVKVCPTGATYKREdGIVLVDYDKCIGCRYCVAACP 103
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
60-83 7.80e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 34.71  E-value: 7.80e-03
                         10        20
                 ....*....|....*....|....
gi 899702687  60 GRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:COG2768    4 GKPYVDEEKCIGCGACVKVCPVGA 27
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 40-80 9.24e-03

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


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 36.08  E-value: 9.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 899702687  40 CDHCGD--CVPGCPGRALAMQEGRVSWQAELCTHCDRCLDVCP 80
Cdd:cd10554   56 CRQCEDapCANVCPVGAISQEDGVVQVDEERCIGCKLCVLACP 98
napH PRK09477
quinol dehydrogenase membrane component; Provisional
 40-83 9.34e-03

quinol dehydrogenase membrane component; Provisional


Pssm-ID: 236535 [Multi-domain]  Cd Length: 271  Bit Score: 36.80  E-value: 9.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 899702687  40 CDHCGDCVPGCPGR-----ALAMQEGRVSWQAELCTHCDRCLDVCPRHA 83
Cdd:PRK09477 210 CTRCMDCFHVCPEPqvlrpPLKGKQSPSQVTSGDCITCGRCIDVCSEDV 258
 
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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