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Conserved domains on  [gi|1914114257|ref|WP_192083315|]
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tRNA epoxyqueuosine(34) reductase QueG [Stenotrophomonas sp. CFBP 13724]

Protein Classification

epoxyqueuosine reductase( domain architecture ID 11489040)

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)

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 ...
21-357 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: 575.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  21 IRALARAHGFQRCGIAGVDLAEDE-AHLADWLSQGLYGTMDWMARHGTLRARPAELLPGTVRVISLGMDYSHKDDTEAWa 99
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 100 TLADPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDSAPVLERALGRDAGLGWIGKHTCLIDRHGGSW 179
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 180 FFLGEIYIDLPLPIDQPASAHCGTCTRCIEVCPTQAIIAPQRLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDCQL 259
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 260 VCPWNKFAKRTDEADFRARNNLDRARLDELFSWDEAEFLQRTEGSPIRRSGHERWLRNIAVALGNAPTSPQVVEALFTRS 339
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 1914114257 340 THDSALVREHVQWALGQH 357
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 ...
21-357 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: 575.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  21 IRALARAHGFQRCGIAGVDLAEDE-AHLADWLSQGLYGTMDWMARHGTLRARPAELLPGTVRVISLGMDYSHKDDTEAWa 99
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 100 TLADPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDSAPVLERALGRDAGLGWIGKHTCLIDRHGGSW 179
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 180 FFLGEIYIDLPLPIDQPASAHCGTCTRCIEVCPTQAIIAPQRLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDCQL 259
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 260 VCPWNKFAKRTDEADFRARNNLDRARLDELFSWDEAEFLQRTEGSPIRRSGHERWLRNIAVALGNAPTSPQVVEALFTRS 339
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 1914114257 340 THDSALVREHVQWALGQH 357
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
19-360 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: 538.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  19 QRIRALARAHGFQRCGIAGVD-LAEDEAHLADWLSQGLYGTMDWMARHGTLRARPAELLPGTVRVISLGMDYSHKDDTEa 97
Cdd:COG1600     9 EEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEEEVS- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  98 watlaDPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDSAPVLERALGRDAGLGWIGKHTCLIDRHGG 177
Cdd:COG1600    88 -----DPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLITPEFG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 178 SWFFLGEIYIDLPLPIDQPASAHCGTCTRCIEVCPTQAIIAPQRLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDC 257
Cdd:COG1600   163 SWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRIYGCDDC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 258 QLVCPWNKFAKRTDEADFRARNNLDRARLDELFSWDEAEFLQRTEGSPIRRSGHERWLRNIAVALGNAPtSPQVVEALFT 337
Cdd:COG1600   243 QDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPAAVPALEA 321
                         330       340
                  ....*....|....*....|...
gi 1914114257 338 RSTHDSALVREHVQWALGQHGAA 360
Cdd:COG1600   322 LLDDPSPLVREHAAWALGRLGGR 344
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
201-264 3.92e-31

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 112.58  E-value: 3.92e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914114257 201 CGTCTRCIEVCPTQAIIAPQ-RLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDCQLVCPWN 264
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEgVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
200-262 6.61e-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: 39.30  E-value: 6.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914114257 200 HCGTCTRCIEVCPTQAIiapqrldarrcisYLTIEHDGAIPEPMRALIGNRI-YGCDDCQLVCP 262
Cdd:cd10549    41 KCVFCGACVEVCPTGAI-------------ELTPEGKEYVPKEKEAEIDEEKcIGCGLCVKVCP 91
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
21-357 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: 575.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  21 IRALARAHGFQRCGIAGVDLAEDE-AHLADWLSQGLYGTMDWMARHGTLRARPAELLPGTVRVISLGMDYSHKDDTEAWa 99
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 100 TLADPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDSAPVLERALGRDAGLGWIGKHTCLIDRHGGSW 179
Cdd:TIGR00276  80 SLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 180 FFLGEIYIDLPLPIDQPASAHCGTCTRCIEVCPTQAIIAPQRLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDCQL 259
Cdd:TIGR00276 160 FFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 260 VCPWNKFAKRTDEADFRARNNLDRARLDELFSWDEAEFLQRTEGSPIRRSGHERWLRNIAVALGNAPTSPQVVEALFTRS 339
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 1914114257 340 THDSALVREHVQWALGQH 357
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
19-360 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: 538.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  19 QRIRALARAHGFQRCGIAGVD-LAEDEAHLADWLSQGLYGTMDWMARHGTLRARPAELLPGTVRVISLGMDYSHKDDTEa 97
Cdd:COG1600     9 EEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEEEVS- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  98 watlaDPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDSAPVLERALGRDAGLGWIGKHTCLIDRHGG 177
Cdd:COG1600    88 -----DPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLITPEFG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 178 SWFFLGEIYIDLPLPIDQPASAHCGTCTRCIEVCPTQAIIAPQRLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDC 257
Cdd:COG1600   163 SWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRIYGCDDC 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 258 QLVCPWNKFAKRTDEADFRARNNLDRARLDELFSWDEAEFLQRTEGSPIRRSGHERWLRNIAVALGNAPtSPQVVEALFT 337
Cdd:COG1600   243 QDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPAAVPALEA 321
                         330       340
                  ....*....|....*....|...
gi 1914114257 338 RSTHDSALVREHVQWALGQHGAA 360
Cdd:COG1600   322 LLDDPSPLVREHAAWALGRLGGR 344
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
201-264 3.92e-31

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 112.58  E-value: 3.92e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914114257 201 CGTCTRCIEVCPTQAIIAPQ-RLDARRCISYLTIEHDGAIPEPMRALIGNRIYGCDDCQLVCPWN 264
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEgVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
69-148 1.15e-29

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: 108.78  E-value: 1.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257  69 RARPAELLPGTVRVISLGMDYSHKDDTEAWAtlaDPGRAYVARYALGRDYHKLMRNRLQKLAAQISDEVAPLGFRVFVDS 148
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALL---DPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
140-265 1.12e-09

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: 58.99  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914114257 140 LGFRVFV---DSAPVLERALGRDAGLGWIGKH--TCLIDRHGGSWFFLGEIYIDLPLPIDQPASA----HCGTCTRCIEV 210
Cdd:TIGR02486 137 LGYNAVPsgnGNGLGSSVAFAVLAGLGEHGRMgqAIISPEYGPRVRIAKVILTDLPLVPTKPIDAgmakFCETCGKCADE 216
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914114257 211 CPTQAI--IAPQRLDARRCISYLTIEHDGAIPEP---MRALI----GNRIYGCDDCQLVCPWNK 265
Cdd:TIGR02486 217 CPSGAIskGGEPTWDPEDSNGDPPGENNPGLKWQydgWRCLLfrcyNEGGGGCGVCQAVCPFNK 280
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
199-262 2.99e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 40.94  E-value: 2.99e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914114257 199 AHCGTCTRCIEVCPTQAIIapqrldarrcisyltiehdGAiPEPMRALIGNRIYGCDDCQLVCP 262
Cdd:TIGR01944 113 DNCIGCTKCIQACPVDAIV-------------------GA-AKAMHTVIADECTGCDLCVEPCP 156
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
201-264 5.85e-04

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: 37.51  E-value: 5.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914114257 201 CGTCTRCIEVCPTQAIIAPQRLDARRCIsylTIEHDgaipePMRALignriyGCDDCQLVCPWN 264
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTK---TVVID-----PERCV------GCGACVAVCPTG 50
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
200-262 6.61e-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: 39.30  E-value: 6.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914114257 200 HCGTCTRCIEVCPTQAIiapqrldarrcisYLTIEHDGAIPEPMRALIGNRI-YGCDDCQLVCP 262
Cdd:cd10549    41 KCVFCGACVEVCPTGAI-------------ELTPEGKEYVPKEKEAEIDEEKcIGCGLCVKVCP 91
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
201-264 1.14e-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: 38.53  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914114257 201 CGTCTRCIEVCPTQAI----IAPQRLDARRCIsyltiehdgaipepmralignriyGCDDCQLVCPWN 264
Cdd:cd10549    80 CIGCGLCVKVCPVDAItledELEIVIDKEKCI------------------------GCGICAEVCPVN 123
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
201-262 3.52e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.80  E-value: 3.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914114257 201 CGTCTRCIEVCPTQAII---APQRLDARRCIsyltiehdgaipepmralignriyGCDDCQLVCP 262
Cdd:COG2221    17 CIGCGLCVAVCPTGAISlddGKLVIDEEKCI------------------------GCGACIRVCP 57
 
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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