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Conserved domains on  [gi|1952201886|ref|WP_199530296|]
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tRNA epoxyqueuosine(34) reductase QueG [Pseudoalteromonas sp. bablab_jr010]

Protein Classification

epoxyqueuosine reductase family protein( domain architecture ID 1002072)

epoxyqueuosine reductase family protein such as epoxyqueuosine reductase, which catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr)

EC:  1.17.99.6
Gene Ontology:  GO:0052693|GO:0051539|GO:0008616|GO:0046872|GO:0008033
SCOP:  4007034|4007775

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 15-351 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


:

Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 608.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  15 IKQWGKDLGFAEVGITDIDLTKHEAQ-LQRWLDLGYHGEMEYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFARN 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  94 LKQTDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDSAPVLERQLAEKAGLGWRGKNSLLINKEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 174 FLGELFVDIPLPIDEENSfEGCGKCVACMTLCPTGAIVEPYVVDARKCISYLTIELQGAIPEEYRPLLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 254 VCPWNRYGQLTDEADFHPRKQLKDQDLLTLFAWDEATFLKNTEGSPIRRIGHERWLRNLAVGLGNADYNEQIIEALEQRL 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1952201886 334 TTASALVAEHIEWALDQQ 351
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 15-351 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 608.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  15 IKQWGKDLGFAEVGITDIDLTKHEAQ-LQRWLDLGYHGEMEYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFARN 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  94 LKQTDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDSAPVLERQLAEKAGLGWRGKNSLLINKEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 174 FLGELFVDIPLPIDEENSfEGCGKCVACMTLCPTGAIVEPYVVDARKCISYLTIELQGAIPEEYRPLLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 254 VCPWNRYGQLTDEADFHPRKQLKDQDLLTLFAWDEATFLKNTEGSPIRRIGHERWLRNLAVGLGNADYNEQIIEALEQRL 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1952201886 334 TTASALVAEHIEWALDQQ 351
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 7-355 0e+00

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: 549.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886   7 DYEQLALQIKQWGKDLGFAEVGITDID-LTKHEAQLQRWLDLGYHGEMEYMAAHGMKRARPAELVPGTQRVISVKMNYLP 85
Cdd:COG1600     3 DLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  86 PDAsfarnLKQTDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDSAPVLERQLAEKAGLGWRGKNSLLI 165
Cdd:COG1600    83 EEE-----VSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 166 NKEAGSWFFLGELFVDIPLPIDEENSfEGCGKCVACMTLCPTGAIVEPYVVDARKCISYLTIELQGAIPEEYRPLLGNRV 245
Cdd:COG1600   158 TPEFGSWFFLGEILTDLELPPDEPVE-DHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 246 YGCDDCQLVCPWNRYGQLTDEADFHPRKQLKDQDLLTLFAWDEATFLKNTEGSPIRRIGHERWLRNLAVGLGNAdYNEQI 325
Cdd:COG1600   237 YGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNS-GDPAA 315

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952201886 326 IEALEQRLTTASALVAEHIEWALDQQKNKR 355
Cdd:COG1600   316 VPALEALLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 63-141 7.06e-33

Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in Epoxyqueuosine reductase QueG, an iron-sulfur cluster-binding protein, together with the 4Fe-4S binding domain (pfam00037). QueG catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).


Pssm-ID: 462431 [Multi-domain]  Cd Length: 77  Bit Score: 117.64  E-value: 7.06e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201886  63 RARPAELVPGTQRVISVKMNYLPPDASFARNLKqtDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDS 141
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLDP--DRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 186-258 4.90e-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: 42.77  E-value: 4.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201886 186 IDEEnsfeGCGKCVACMTLCPTGAIV----EPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:cd10549    75 IDEE----KCIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVN 123
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 15-351 0e+00

epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there is new information that bacterial members are epoxyqueuosine reductase, QueG, involved in queuosine biosynthesis for tRNA maturation. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 608.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  15 IKQWGKDLGFAEVGITDIDLTKHEAQ-LQRWLDLGYHGEMEYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFARN 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  94 LKQTDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDSAPVLERQLAEKAGLGWRGKNSLLINKEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 174 FLGELFVDIPLPIDEENSfEGCGKCVACMTLCPTGAIVEPYVVDARKCISYLTIELQGAIPEEYRPLLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 254 VCPWNRYGQLTDEADFHPRKQLKDQDLLTLFAWDEATFLKNTEGSPIRRIGHERWLRNLAVGLGNADYNEQIIEALEQRL 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319

                         330
                  ....*....|....*...
gi 1952201886 334 TTASALVAEHIEWALDQQ 351
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 7-355 0e+00

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: 549.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886   7 DYEQLALQIKQWGKDLGFAEVGITDID-LTKHEAQLQRWLDLGYHGEMEYMAAHGMKRARPAELVPGTQRVISVKMNYLP 85
Cdd:COG1600     3 DLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  86 PDAsfarnLKQTDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDSAPVLERQLAEKAGLGWRGKNSLLI 165
Cdd:COG1600    83 EEE-----VSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 166 NKEAGSWFFLGELFVDIPLPIDEENSfEGCGKCVACMTLCPTGAIVEPYVVDARKCISYLTIELQGAIPEEYRPLLGNRV 245
Cdd:COG1600   158 TPEFGSWFFLGEILTDLELPPDEPVE-DHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 246 YGCDDCQLVCPWNRYGQLTDEADFHPRKQLKDQDLLTLFAWDEATFLKNTEGSPIRRIGHERWLRNLAVGLGNAdYNEQI 325
Cdd:COG1600   237 YGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNS-GDPAA 315

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952201886 326 IEALEQRLTTASALVAEHIEWALDQQKNKR 355
Cdd:COG1600   316 VPALEALLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 63-141 7.06e-33

Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in Epoxyqueuosine reductase QueG, an iron-sulfur cluster-binding protein, together with the 4Fe-4S binding domain (pfam00037). QueG catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).


Pssm-ID: 462431 [Multi-domain]  Cd Length: 77  Bit Score: 117.64  E-value: 7.06e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952201886  63 RARPAELVPGTQRVISVKMNYLPPDASFARNLKqtDKAYISRYALGRDYHKLIRNRLKKLGQQIEQHIGQLGFRPFVDS 141
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLDP--DRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
195-258 2.67e-29

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 107.96  E-value: 2.67e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201886 195 CGKCVACMTLCPTGAIVEP-YVVDARKCISYLTIELQGAIPEEYRPLLGNRVYGCDDCQLVCPWN 258
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 186-256 3.17e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 44.27  E-value: 3.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201886 186 IDEENsFEGCGKCVAcmtLCPTGAIV---EPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCP 256
Cdd:COG2221    12 IDEEK-CIGCGLCVA---VCPTGAISlddGKLVIDEEKCI------------------------GCGACIRVCP 57
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 186-258 4.90e-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: 42.77  E-value: 4.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201886 186 IDEEnsfeGCGKCVACMTLCPTGAIV----EPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:cd10549    75 IDEE----KCIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVN 123
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 194-256 5.15e-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: 40.87  E-value: 5.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201886 194 GCGKCVAcmtLCPTGAIV----EPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCP 256
Cdd:COG1149    15 GCGLCVE---VCPEGAIKlddgGAPVVDPDLCT------------------------GCGACVGVCP 54
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
186-256 6.17e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 40.87  E-value: 6.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201886 186 IDEENsfegCGKCVACMTLCPTGAIV---EPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCP 256
Cdd:COG2768     8 VDEEK----CIGCGACVKVCPVGAISiedGKAVIDPEKCI------------------------GCGACIEVCP 53
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 2-258 7.31e-05

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


Pssm-ID: 274158  Cd Length: 314  Bit Score: 44.35  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886   2 TTPaidyEQLALQIKQWGKDLGFAEVGI---TDIDLTKHEAQLQRWLDLGYHGEMEYMAAHGMKRARP-----AELVPGT 73
Cdd:TIGR02486   4 GTP----EENSRMVRAAARFLGADDVGIaelDDNWVFKLFYEHSTDPMDGPTSTTENKDIEKKYVFEDvdeeyTTTEPDT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886  74 QRVISVKMNY-------LPPDASFARnlkqTDKAYISRYALGRDYHklirnRLKKLGQQIEQHIGQLGFRPFV---DSAP 143
Cdd:TIGR02486  80 KLVIPNKPKYvivatieMDYETYLRS----PGSSIIASAASFKAYS-----RFGYVAVRLQQFIRNLGYNAVPsgnGNGL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 144 VLERQLAEKAGLGWRGKN-SLLINKEAGSWFFLGELFV-DIPL----PIDEeNSFEGCGKCVACMTLCPTGAIVE--PYV 215
Cdd:TIGR02486 151 GSSVAFAVLAGLGEHGRMgQAIISPEYGPRVRIAKVILtDLPLvptkPIDA-GMAKFCETCGKCADECPSGAISKggEPT 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1952201886 216 VDARK--------CISYLTIELQGAIPEEYRPlLGNRVYGCDDCQLVCPWN 258
Cdd:TIGR02486 230 WDPEDsngdppgeNNPGLKWQYDGWRCLLFRC-YNEGGGGCGVCQAVCPFN 279
NapF COG1145
Ferredoxin [Energy production and conversion];
186-258 4.29e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 41.63  E-value: 4.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952201886 186 IDEENsfegCGKCVACMTLCPTGAIVE-----PYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:COG1145   179 IDAEK----CIGCGLCVKVCPTGAIRLkdgkpQIVVDPDKCI------------------------GCGACVKVCPVG 228
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 186-258 1.09e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.33  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201886 186 IDEENsfegCGKCVACMTLCPTGAIVE---PYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:COG4231    19 IDEDK----CTGCGACVKVCPADAIEEgdgKAVIDPDLCI------------------------GCGSCVQVCPVD 66
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 193-256 2.03e-03

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: 37.76  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 193 EGCGKCVACMTLCPTGAI--------VEPYVVDARKCI---------SYLTIELQGaIPEEYRPLLGNRVY------GCD 249
Cdd:cd10549     6 EKCIGCGICVKACPTDAIelgpngaiARGPEIDEDKCVfcgacvevcPTGAIELTP-EGKEYVPKEKEAEIdeekciGCG 84


                  ....*..
gi 1952201886 250 DCQLVCP 256
Cdd:cd10549    85 LCVKVCP 91
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 194-258 2.49e-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: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 35.58  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952201886 194 GCGKCVAcmtLCPTGAIVEPYVVDARKCISYltielqgaipeEYRPllgNRVYGCDDCQLVCPWN 258
Cdd:pfam12838   3 GCGACVA---ACPVGAITLDEVGEKKGTKTV-----------VIDP---ERCVGCGACVAVCPTG 50
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 200-258 2.71e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 37.56  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952201886 200 ACMTLCPTGAI-VEP----YVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:cd10550    56 PCVEACPVGAIsRDEetgaVVVDEDKCI------------------------GCGMCVEACPFG 95
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 194-268 2.80e-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: 38.05  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952201886 194 GCGKCV--ACMTLCPTGAI-------VepyVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN--RYGQ 262
Cdd:cd10562    69 QCMHCTdaACVKVCPTGALyktengaV---VVDEDKCI------------------------GCGYCVAACPFDvpRYDE 121


                  ....*.
gi 1952201886 263 LTDEAD 268
Cdd:cd10562   122 TTNKIT 127
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 195-257 6.10e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 36.77  E-value: 6.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952201886 195 CGKCV--ACMTLCPTGA-------IVepyVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPW 257
Cdd:cd16371    54 CNHCEnpACVKVCPTGAitkredgIV---VVDQDKCI------------------------GCGYCVWACPY 98
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 193-256 6.18e-03

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


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 35.11  E-value: 6.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1952201886 193 EGCGKCVACMTLCPTGAI-------VEPYVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCP 256
Cdd:COG1143     2 DKCIGCGLCVRVCPVDAItiedgepGKVYVIDPDKCI------------------------GCGLCVEVCP 48
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 200-258 7.53e-03

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 37.23  E-value: 7.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1952201886 200 ACMTLCPTGA-------IVepyVVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCPWN 258
Cdd:COG0437    67 PCVKVCPTGAtykredgIV---LVDYDKCI------------------------GCRYCVAACPYG 105
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 194-256 8.98e-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: 37.28  E-value: 8.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1952201886 194 GCGKCVAcmtLCPTGAIV-EPY---VVDARKCIsyltielqgaipeeyrpllgnrvyGCDDCQLVCP 256
Cdd:COG2878   141 GCGDCIK---ACPFDAIVgAAKgmhTVDEDKCT------------------------GCGLCVEACP 180
 
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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