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Conserved domains on  [gi|488832017|ref|WP_002744423|]
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MULTISPECIES: tRNA epoxyqueuosine(34) reductase QueG [Microcystis]

Protein Classification

epoxyqueuosine reductase( domain architecture ID 11446674)

epoxyqueuosine reductase 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
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-311 1.10e-170

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: 477.00  E-value: 1.10e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017   1 MVTETQIKEKALELGFHGVGIASVDSQDLAVSHLKSWLERGYHADMDWMTN--PKRQDIKTLWPEVRSLICLALNYYTPQ 78
Cdd:COG1600    5 MELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHGEMGYMERhiEKRADPRELLPGAKSVISLALNYLPEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  79 QHSQEQnHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGS 158
Cdd:COG1600   85 EVSDPD-RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLITPEFGS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 159 WVFLGEILTNLPLEPDQPHSAHCGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtLPTKIAKNLQGWVAGCDIC 238
Cdd:COG1600  164 WFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGP-IPEELRPKMGNRIYGCDDC 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488832017 239 QDVCPWNqRFAQVTDVEDFQPRLENLSPKLEELANLTIEEWDRRFISSALRRIKPQQWRRNAQANLAHSPHPA 311
Cdd:COG1600  243 QDVCPWN-RFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPA 314
 
Name Accession Description Interval E-value
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-311 1.10e-170

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: 477.00  E-value: 1.10e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017   1 MVTETQIKEKALELGFHGVGIASVDSQDLAVSHLKSWLERGYHADMDWMTN--PKRQDIKTLWPEVRSLICLALNYYTPQ 78
Cdd:COG1600    5 MELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHGEMGYMERhiEKRADPRELLPGAKSVISLALNYLPEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  79 QHSQEQnHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGS 158
Cdd:COG1600   85 EVSDPD-RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLITPEFGS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 159 WVFLGEILTNLPLEPDQPHSAHCGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtLPTKIAKNLQGWVAGCDIC 238
Cdd:COG1600  164 WFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGP-IPEELRPKMGNRIYGCDDC 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488832017 239 QDVCPWNqRFAQVTDVEDFQPRLENLSPKLEELANLTIEEWDRRFISSALRRIKPQQWRRNAQANLAHSPHPA 311
Cdd:COG1600  243 QDVCPWN-RFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPA 314
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 7-308 1.03e-133

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: 383.03  E-value: 1.03e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017    7 IKEKALELGFHGVGIASVDSQDLAVSHLKSWLERGYHADMDWMTN--PKRQDIKTLWPEVRSLICLALNYYTPQ----QH 80
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGEMGFMARhgEKRARPAELLPGTRSVISVRMDYLPKLappaKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017   81 SQEQNHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGSWV 160
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  161 FLGEILTNLPLEPDQPHSAHCGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtLPTKIAKNLQGWVAGCDICQD 240
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGP-IPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488832017  241 VCPWNqRFAQVTDVEDFQPRLENLSPKLEELANLTIEEWDRRFISSALRRIKPQQWRRNAQANLAHSP 308
Cdd:TIGR00276 240 VCPWN-KFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAP 306
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 54-128 2.03e-35

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: 123.03  E-value: 2.03e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017   54 RQDIKTLWPEVRSLICLALNYYTPQQHSQEQ--NHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDT 128
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLdpDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 181-245 9.95e-06

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: 44.31  E-value: 9.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488832017 181 CGTCSRCLSACPTQAIVS----PSVVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCPWN 245
Cdd:cd10549   80 CIGCGLCVKVCPVDAITLedelEIVIDKEKCI-------------------------GCGICAEVCPVN 123
PRK06991 PRK06991
electron transport complex subunit RsxB;
169-243 1.01e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 169 LPLEP----DQPHS------AHCGTCSRCLSACPTQAIVSpsvvdANRciAYHTIenravtlptkiaknLQGWVAGCDIC 238
Cdd:PRK06991  65 IPLDPangvERPRAvavideQLCIGCTLCMQACPVDAIVG-----APK--QMHTV--------------LADLCTGCDLC 123


                 ....*
gi 488832017 239 QDVCP 243
Cdd:PRK06991 124 VPPCP 128
 
Name Accession Description Interval E-value
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-311 1.10e-170

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: 477.00  E-value: 1.10e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017   1 MVTETQIKEKALELGFHGVGIASVDSQDLAVSHLKSWLERGYHADMDWMTN--PKRQDIKTLWPEVRSLICLALNYYTPQ 78
Cdd:COG1600    5 MELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHGEMGYMERhiEKRADPRELLPGAKSVISLALNYLPEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  79 QHSQEQnHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGS 158
Cdd:COG1600   85 EVSDPD-RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLITPEFGS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 159 WVFLGEILTNLPLEPDQPHSAHCGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtLPTKIAKNLQGWVAGCDIC 238
Cdd:COG1600  164 WFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGP-IPEELRPKMGNRIYGCDDC 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488832017 239 QDVCPWNqRFAQVTDVEDFQPRLENLSPKLEELANLTIEEWDRRFISSALRRIKPQQWRRNAQANLAHSPHPA 311
Cdd:COG1600  243 QDVCPWN-RFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPA 314
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 7-308 1.03e-133

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: 383.03  E-value: 1.03e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017    7 IKEKALELGFHGVGIASVDSQDLAVSHLKSWLERGYHADMDWMTN--PKRQDIKTLWPEVRSLICLALNYYTPQ----QH 80
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGEMGFMARhgEKRARPAELLPGTRSVISVRMDYLPKLappaKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017   81 SQEQNHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGSWV 160
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  161 FLGEILTNLPLEPDQPHSAHCGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtLPTKIAKNLQGWVAGCDICQD 240
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGP-IPEEFRPLIGNRIYGCDDCQL 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488832017  241 VCPWNqRFAQVTDVEDFQPRLENLSPKLEELANLTIEEWDRRFISSALRRIKPQQWRRNAQANLAHSP 308
Cdd:TIGR00276 240 VCPWN-KFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAP 306
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 54-128 2.03e-35

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: 123.03  E-value: 2.03e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017   54 RQDIKTLWPEVRSLICLALNYYTPQQHSQEQ--NHGKISRYAWGRDYHKVLSKKLKALSQWLESQGEQIQTRYYVDT 128
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLdpDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
181-245 6.48e-26

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 97.56  E-value: 6.48e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488832017  181 CGTCSRCLSACPTQAIVSPS-VVDANRCIAYHTIENRAVTlPTKIAKNLQGWVAGCDICQDVCPWN 245
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEgVLDARRCISYLTIEKKGLI-PDELRCLLGNRCYGCDICQDVCPWN 65
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 136-245 9.34e-11

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: 61.68  E-value: 9.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017  136 WAQRAGIGWIAKNGN-LITRNYGSWVFLGE-ILTNLPLEPDQPHSA----HCGTCSRCLSACPTQAI-----VSPSVVDA 204
Cdd:TIGR02486 156 FAVLAGLGEHGRMGQaIISPEYGPRVRIAKvILTDLPLVPTKPIDAgmakFCETCGKCADECPSGAIskggePTWDPEDS 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488832017  205 NRCiayhtienravTLPTKIAKNLQGW--------------VAGCDICQDVCPWN 245
Cdd:TIGR02486 236 NGD-----------PPGENNPGLKWQYdgwrcllfrcynegGGGCGVCQAVCPFN 279
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 177-243 4.32e-07

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: 49.03  E-value: 4.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017  177 HSAHCGTCSRCLSACPTQAIVSpsvvdANRciAYHTIenravtlptkiaknLQGWVAGCDICQDVCP 243
Cdd:TIGR01944 111 DEDNCIGCTKCIQACPVDAIVG-----AAK--AMHTV--------------IADECTGCDLCVEPCP 156
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 181-245 9.95e-06

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: 44.31  E-value: 9.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488832017 181 CGTCSRCLSACPTQAIVS----PSVVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCPWN 245
Cdd:cd10549   80 CIGCGLCVKVCPVDAITLedelEIVIDKEKCI-------------------------GCGICAEVCPVN 123
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 181-245 2.21e-05

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: 41.36  E-value: 2.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488832017  181 CGTCSRCLSACPTQAIVSPSVVDANRCIAYHTIENRAVtlptkiaknlqgwvaGCDICQDVCPWN 245
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVIDPERCV---------------GCGACVAVCPTG 50
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 171-243 1.15e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 41.86  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 171 LEPDQPHSAHCgtCSRCLSACPTQAIVSPS-----------VVDANRCIAYHtienravtlptkiaknlqgWVAGCDICQ 239
Cdd:cd16373   48 LDPREGPCDLC--CDACVEVCPTGALRPLDleeqkvkmgvaVIDKDRCLAWQ-------------------GGTDCGVCV 106


                 ....
gi 488832017 240 DVCP 243
Cdd:cd16373  107 EACP 110
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 181-243 2.12e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.88  E-value: 2.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488832017 181 CGTCSRCLSACPTQAIV---SPSVVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCP 243
Cdd:COG2221   17 CIGCGLCVAVCPTGAISlddGKLVIDEEKCI-------------------------GCGACIRVCP 57
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 184-243 5.47e-04

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: 37.80  E-value: 5.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017 184 CSRCLSACPTQAI-------VSPSVVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCP 243
Cdd:COG1143    7 CGLCVRVCPVDAItiedgepGKVYVIDPDKCI-------------------------GCGLCVEVCP 48
PRK06991 PRK06991
electron transport complex subunit RsxB;
169-243 1.01e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 169 LPLEP----DQPHS------AHCGTCSRCLSACPTQAIVSpsvvdANRciAYHTIenravtlptkiaknLQGWVAGCDIC 238
Cdd:PRK06991  65 IPLDPangvERPRAvavideQLCIGCTLCMQACPVDAIVG-----APK--QMHTV--------------LADLCTGCDLC 123


                 ....*
gi 488832017 239 QDVCP 243
Cdd:PRK06991 124 VPPCP 128
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 187-248 2.36e-03

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: 38.28  E-value: 2.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488832017 187 CLSACPTQA-------IVspsVVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCPWNQRF 248
Cdd:cd10551   61 CVKVCPTGAtykredgIV---LVDYDKCI-------------------------GCRYCMAACPYGARY 101
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
180-243 2.66e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.33  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 180 HCGTCSrCLSACPTQAIV---SPSVVDANRCIA---------YHTIENRAVTLPTKIAKnlqgwvagCDICQD------- 240
Cdd:COG1142   54 HCEDAP-CAEVCPVGAITrddGAVVVDEEKCIGcglcvlacpFGAITMVGEKSRAVAVK--------CDLCGGreggpac 124


                 ....*
gi 488832017 241 --VCP 243
Cdd:COG1142  125 veACP 129
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 187-245 3.10e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 37.17  E-value: 3.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488832017 187 CLSACPTQAI-VSPS----VVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCPWN 245
Cdd:cd10550   57 CVEACPVGAIsRDEEtgavVVDEDKCI-------------------------GCGMCVEACPFG 95
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
 180-243 4.58e-03

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: 38.00  E-value: 4.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017  180 HCGTCSRCLSACPTQA--IVSPSVV-DANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCP 243
Cdd:TIGR04041  42 HCDHCGDCVAGCPAGAlsLVDGKVVwDKERCI-------------------------GCDTCIKVCP 83
FDH-O_like cd10560
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ...
 108-197 6.78e-03

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


Pssm-ID: 319882 [Multi-domain]  Cd Length: 225  Bit Score: 37.37  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488832017 108 ALSQW--LESQGEQIQTRYYVDTGPVQDKVWAQRAGIGWIAKNGNLITRNYGSWVFLgeiltnlplepdqphSAHCGTCS 185
Cdd:cd10560   18 ACKQWnqLPADGYDFSGMSYDNTGDLSASTWRHVKFIERPTEDGPANEGGDLQWLFM---------------SDVCKHCT 82

                         90
                 ....*....|....
gi 488832017 186 R--CLSACPTQAIV 197
Cdd:cd10560   83 DagCLEACPTGAIF 96
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 181-243 9.60e-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: 34.64  E-value: 9.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488832017 181 CGTCSRCLSACPTQAIVSPS----VVDANRCIayhtienravtlptkiaknlqgwvaGCDICQDVCP 243
Cdd:COG1144   32 CIGCGLCWIVCPDGAIRVDDgkyyGIDYDYCK-------------------------GCGICAEVCP 73
 
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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