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Conserved domains on  [gi|658757187|ref|WP_029774050|]
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MULTISPECIES: tRNA epoxyqueuosine(34) reductase QueG [unclassified Pseudoalteromonas]

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 ...
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: 622.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   15 IKAWGQELGFSEVGITDIDLSKHEAQ-LQRWLDAGYHGSMDYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFAKT 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   94 LKNTEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDSAPVLERQLAEKAGLGWRGKHSLLINQEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  174 FLGELFVDLPLPIDNENTfEGCGKCVACITLCPTGAIVEPYVVDARKCISYLTIEHQGPIPEQYRALLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  254 VCPWNRYGQITDEQDFHPRTQLKNKDLLELFTWDEPTFLKNTEGSPIRRIGHERWLRNLAVGLGNADFSPSIINALESKH 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 658757187  334 ESSSQLVKEHIEWALEQQ 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: 622.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   15 IKAWGQELGFSEVGITDIDLSKHEAQ-LQRWLDAGYHGSMDYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFAKT 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   94 LKNTEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDSAPVLERQLAEKAGLGWRGKHSLLINQEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  174 FLGELFVDLPLPIDNENTfEGCGKCVACITLCPTGAIVEPYVVDARKCISYLTIEHQGPIPEQYRALLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  254 VCPWNRYGQITDEQDFHPRTQLKNKDLLELFTWDEPTFLKNTEGSPIRRIGHERWLRNLAVGLGNADFSPSIINALESKH 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 658757187  334 ESSSQLVKEHIEWALEQQ 351
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
6-355 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: 555.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   6 PNYQQLAKNIKAWGQELGFSEVGITDID-LSKHEAQLQRWLDAGYHGSMDYMAAHGMKRARPAELVPGTQRVISVKMNYL 84
Cdd:COG1600    2 SDLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  85 PPDAsfaktLKNTEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDSAPVLERQLAEKAGLGWRGKHSLL 164
Cdd:COG1600   82 PEEE-----VSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187 165 INQEAGSWFFLGELFVDLPLPIDNENTfEGCGKCVACITLCPTGAIVEPYVVDARKCISYLTIEHQGPIPEQYRALLGNR 244
Cdd:COG1600  157 ITPEFGSWFFLGEILTDLELPPDEPVE-DHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187 245 VYGCDDCQLVCPWNRYGQITDEQDFHPRTQLKNKDLLELFTWDEPTFLKNTEGSPIRRIGHERWLRNLAVGLGNADfSPS 324
Cdd:COG1600  236 IYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPA 314
                        330       340       350
                 ....*....|....*....|....*....|.
gi 658757187 325 IINALESKHESSSQLVKEHIEWALEQQNNKQ 355
Cdd:COG1600  315 AVPALEALLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
63-141 4.48e-34

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: 120.72  E-value: 4.48e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658757187   63 RARPAELVPGTQRVISVKMNYLPPDASFAKTLKntEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDS 141
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLDP--DRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
200-258 4.02e-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: 4.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658757187 200 ACITLCPTGAI-VEP----YVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPWN 258
Cdd:cd10550   56 PCVEACPVGAIsRDEetgaVVVDEDKCI------------------------GCGMCVEACPFG 95
 
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: 622.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   15 IKAWGQELGFSEVGITDIDLSKHEAQ-LQRWLDAGYHGSMDYMAAHGMKRARPAELVPGTQRVISVKMNYLPPDASFAKT 93
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   94 LKNTEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDSAPVLERQLAEKAGLGWRGKHSLLINQEAGSWF 173
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  174 FLGELFVDLPLPIDNENTfEGCGKCVACITLCPTGAIVEPYVVDARKCISYLTIEHQGPIPEQYRALLGNRVYGCDDCQL 253
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVT-DHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  254 VCPWNRYGQITDEQDFHPRTQLKNKDLLELFTWDEPTFLKNTEGSPIRRIGHERWLRNLAVGLGNADFSPSIINALESKH 333
Cdd:TIGR00276 240 VCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALL 319
                         330
                  ....*....|....*...
gi 658757187  334 ESSSQLVKEHIEWALEQQ 351
Cdd:TIGR00276 320 DDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
6-355 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: 555.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187   6 PNYQQLAKNIKAWGQELGFSEVGITDID-LSKHEAQLQRWLDAGYHGSMDYMAAHGMKRARPAELVPGTQRVISVKMNYL 84
Cdd:COG1600    2 SDLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  85 PPDAsfaktLKNTEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDSAPVLERQLAEKAGLGWRGKHSLL 164
Cdd:COG1600   82 PEEE-----VSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187 165 INQEAGSWFFLGELFVDLPLPIDNENTfEGCGKCVACITLCPTGAIVEPYVVDARKCISYLTIEHQGPIPEQYRALLGNR 244
Cdd:COG1600  157 ITPEFGSWFFLGEILTDLELPPDEPVE-DHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187 245 VYGCDDCQLVCPWNRYGQITDEQDFHPRTQLKNKDLLELFTWDEPTFLKNTEGSPIRRIGHERWLRNLAVGLGNADfSPS 324
Cdd:COG1600  236 IYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPA 314
                        330       340       350
                 ....*....|....*....|....*....|.
gi 658757187 325 IINALESKHESSSQLVKEHIEWALEQQNNKQ 355
Cdd:COG1600  315 AVPALEALLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
63-141 4.48e-34

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: 120.72  E-value: 4.48e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658757187   63 RARPAELVPGTQRVISVKMNYLPPDASFAKTLKntEKAYISRYALGRDYHKLMRNRLKKLGQKIEQEIGDYGFRPFVDS 141
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLDP--DRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
195-258 1.80e-29

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 108.35  E-value: 1.80e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658757187  195 CGKCVACITLCPTGAIVEP-YVVDARKCISYLTIEHQGPIPEQYRALLGNRVYGCDDCQLVCPWN 258
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
185-256 5.99e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.50  E-value: 5.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658757187 185 PIDNENTFEGCGKCVAcitLCPTGAIV---EPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 256
Cdd:COG2221   10 PKIDEEKCIGCGLCVA---VCPTGAISlddGKLVIDEEKCI------------------------GCGACIRVCP 57
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
194-256 2.77e-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: 41.64  E-value: 2.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658757187 194 GCGKCVAcitLCPTGAIV----EPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 256
Cdd:COG1149   15 GCGLCVE---VCPEGAIKlddgGAPVVDPDLCT------------------------GCGACVGVCP 54
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
117-258 3.33e-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: 45.12  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  117 NRLKKLGQKIEQEIGDYGFRPFV---DSAPVLERQLAEKAGLGWRGKH-SLLINQEAGSWFFLGELFV-DLPL----PID 187
Cdd:TIGR02486 121 SRFGYVAVRLQQFIRNLGYNAVPsgnGNGLGSSVAFAVLAGLGEHGRMgQAIISPEYGPRVRIAKVILtDLPLvptkPID 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187  188 nENTFEGCGKCVACITLCPTGAIVE--PYVVDARKCISYLTIEHQGPIPEQY---RALL----GNRVYGCDDCQLVCPWN 258
Cdd:TIGR02486 201 -AGMAKFCETCGKCADECPSGAISKggEPTWDPEDSNGDPPGENNPGLKWQYdgwRCLLfrcyNEGGGGCGVCQAVCPFN 279
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
193-256 3.89e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 41.25  E-value: 3.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658757187 193 EGCGKCVACITLCPTGAIV---EPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 256
Cdd:COG2768   11 EKCIGCGACVKVCPVGAISiedGKAVIDPEKCI------------------------GCGACIEVCP 53
NapF COG1145
Ferredoxin [Energy production and conversion];
193-258 4.48e-05

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 44.33  E-value: 4.48e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658757187 193 EGCGKCVACITLCPTGAIVE-----PYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPWN 258
Cdd:COG1145  182 EKCIGCGLCVKVCPTGAIRLkdgkpQIVVDPDKCI------------------------GCGACVKVCPVG 228
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
194-256 1.38e-03

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 37.00  E-value: 1.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658757187 194 GCGKCVAcitLCPTGAI------VEPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 256
Cdd:COG1146   12 GCGACVE---VCPVDVLeldeegKKALVINPEECI------------------------GCGACELVCP 53
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
193-258 1.88e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 36.56  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658757187 193 EGCGkcvACITLCPTGAIVE---PYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPWN 258
Cdd:COG4231   25 TGCG---ACVKVCPADAIEEgdgKAVIDPDLCI------------------------GCGSCVQVCPVD 66
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
195-258 2.97e-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: 2.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658757187  195 CGKCVACITLCPTGAIV----------EPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPWN 258
Cdd:pfam12838   1 CIGCGACVAACPVGAITldevgekkgtKTVVIDPERCV------------------------GCGACVAVCPTG 50
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
194-256 4.01e-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: 35.49  E-value: 4.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658757187 194 GCGKCVAcitLCPTGAI-------VEPYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 256
Cdd:COG1143    6 GCGLCVR---VCPVDAItiedgepGKVYVIDPDKCI------------------------GCGLCVEVCP 48
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
200-258 4.02e-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: 4.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658757187 200 ACITLCPTGAI-VEP----YVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPWN 258
Cdd:cd10550   56 PCVEACPVGAIsRDEetgaVVVDEDKCI------------------------GCGMCVEACPFG 95
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
201-264 6.87e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 36.56  E-value: 6.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658757187 201 CITLCPTGAIVE---PYVVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCPwnrYGQIT 264
Cdd:COG1142   60 CAEVCPVGAITRddgAVVVDEEKCI------------------------GCGLCVLACP---FGAIT 99
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
194-256 7.24e-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: 37.67  E-value: 7.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658757187 194 GCGKCVAcitLCPTGAIV-EPY---VVDARKCIsyltiehqgpipeqyrallgnrvyGCDDCQLVCP 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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