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Conserved domains on  [gi|1421773436|ref|WP_111877162|]
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tRNA epoxyqueuosine(34) reductase QueG [Paracidovorax anthurii]

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)

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 ...
 4-356 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: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436   4 WARELGFSQIGIAGVDLSSAE-PGLMQWLAQGFHGEMHYMEAHGLRRARPAELVPGTVSVITARMDYLPhatldrgaare 82
Cdd:TIGR00276   4 WAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLP----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  83 geeggagwQAVEFA-RLERPREGIVSVYARGRDYHKVLRARLQKLADRIAAAIGPFGHRVFTDSAPVLEAELARRSGQGW 161
Cdd:TIGR00276  73 --------KLAPPAkSLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 162 RGKHTLVLNREAGSMFFLGEIYVDLPLAPSEPVTAHCGSCQACIDVCPTQAIVAPHRVDARRCISYLTIEHAGPIPEAMR 241
Cdd:TIGR00276 145 IGKHTLLINREAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFR 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 242 PLMGNRVYGCDDCQLACPWNKFAQPSRLPDFDERPDLAGRPLAEWFAWDEPTFLRRTEGGPIRRIGHERWLRNVAVALGN 321
Cdd:TIGR00276 225 PLIGNRIYGCDDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGN 304

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1421773436 322 alrATHDPTLRAALASRAEDPSALVREHVAWALGE 356
Cdd:TIGR00276 305 ---APGSPAIIEALEALLDDPSPLVREHAAWALGQ 336
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 4-356 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: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436   4 WARELGFSQIGIAGVDLSSAE-PGLMQWLAQGFHGEMHYMEAHGLRRARPAELVPGTVSVITARMDYLPhatldrgaare 82
Cdd:TIGR00276   4 WAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLP----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  83 geeggagwQAVEFA-RLERPREGIVSVYARGRDYHKVLRARLQKLADRIAAAIGPFGHRVFTDSAPVLEAELARRSGQGW 161
Cdd:TIGR00276  73 --------KLAPPAkSLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 162 RGKHTLVLNREAGSMFFLGEIYVDLPLAPSEPVTAHCGSCQACIDVCPTQAIVAPHRVDARRCISYLTIEHAGPIPEAMR 241
Cdd:TIGR00276 145 IGKHTLLINREAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFR 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 242 PLMGNRVYGCDDCQLACPWNKFAQPSRLPDFDERPDLAGRPLAEWFAWDEPTFLRRTEGGPIRRIGHERWLRNVAVALGN 321
Cdd:TIGR00276 225 PLIGNRIYGCDDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGN 304

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1421773436 322 alrATHDPTLRAALASRAEDPSALVREHVAWALGE 356
Cdd:TIGR00276 305 ---APGSPAIIEALEALLDDPSPLVREHAAWALGQ 336
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 4-359 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: 529.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436   4 WARELGFSQIGIAGVD-LSSAEPGLMQWLAQGFHGEMHYMEAHGLRRARPAELVPGTVSVITARMDYLPHAtldrgaare 82
Cdd:COG1600    14 WARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEE--------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  83 geeggagwqavefaRLERPREGIVSVYARGRDYHKVLRARLQKLADRIAAAIGPFGHRVFTDSAPVLEAELARRSGQGWR 162
Cdd:COG1600    85 --------------EVSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 163 GKHTLVLNREAGSMFFLGEIYVDLPLAPSEPVTAHCGSCQACIDVCPTQAIVAPHRVDARRCISYLTIEHAGPIPEAMRP 242
Cdd:COG1600   151 GKNTNLITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 243 LMGNRVYGCDDCQLACPWNKFAQPSRLPDFDERPDLAGRPLAEWFAWDEPTFLRRTEGGPIRRIGHERWLRNVAVALGNA 322
Cdd:COG1600   231 KMGNRIYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNS 310

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1421773436 323 lratHDPTLRAALASRAEDPSALVREHVAWALGEKAP 359
Cdd:COG1600   311 ----GDPAAVPALEALLDDPSPLVREHAAWALGRLGG 343
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
198-261 1.52e-31

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 113.35  E-value: 1.52e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1421773436 198 CGSCQACIDVCPTQAIVAP-HRVDARRCISYLTIEHAGPIPEAMRPLMGNRVYGCDDCQLACPWN 261
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 198-261 6.71e-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: 45.08  E-value: 6.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773436 198 CGSCQACIDVCPTQAIV----APHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACPWN 261
Cdd:cd10549    80 CIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVN 123
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 4-356 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: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436   4 WARELGFSQIGIAGVDLSSAE-PGLMQWLAQGFHGEMHYMEAHGLRRARPAELVPGTVSVITARMDYLPhatldrgaare 82
Cdd:TIGR00276   4 WAKELGFDKIGITDADLFPEEkERLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLP----------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  83 geeggagwQAVEFA-RLERPREGIVSVYARGRDYHKVLRARLQKLADRIAAAIGPFGHRVFTDSAPVLEAELARRSGQGW 161
Cdd:TIGR00276  73 --------KLAPPAkSLKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGW 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 162 RGKHTLVLNREAGSMFFLGEIYVDLPLAPSEPVTAHCGSCQACIDVCPTQAIVAPHRVDARRCISYLTIEHAGPIPEAMR 241
Cdd:TIGR00276 145 IGKHTLLINREAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFR 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 242 PLMGNRVYGCDDCQLACPWNKFAQPSRLPDFDERPDLAGRPLAEWFAWDEPTFLRRTEGGPIRRIGHERWLRNVAVALGN 321
Cdd:TIGR00276 225 PLIGNRIYGCDDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGN 304

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1421773436 322 alrATHDPTLRAALASRAEDPSALVREHVAWALGE 356
Cdd:TIGR00276 305 ---APGSPAIIEALEALLDDPSPLVREHAAWALGQ 336
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 4-359 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: 529.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436   4 WARELGFSQIGIAGVD-LSSAEPGLMQWLAQGFHGEMHYMEAHGLRRARPAELVPGTVSVITARMDYLPHAtldrgaare 82
Cdd:COG1600    14 WARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEE--------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  83 geeggagwqavefaRLERPREGIVSVYARGRDYHKVLRARLQKLADRIAAAIGPFGHRVFTDSAPVLEAELARRSGQGWR 162
Cdd:COG1600    85 --------------EVSDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 163 GKHTLVLNREAGSMFFLGEIYVDLPLAPSEPVTAHCGSCQACIDVCPTQAIVAPHRVDARRCISYLTIEHAGPIPEAMRP 242
Cdd:COG1600   151 GKNTNLITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 243 LMGNRVYGCDDCQLACPWNKFAQPSRLPDFDERPDLAGRPLAEWFAWDEPTFLRRTEGGPIRRIGHERWLRNVAVALGNA 322
Cdd:COG1600   231 KMGNRIYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNS 310

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1421773436 323 lratHDPTLRAALASRAEDPSALVREHVAWALGEKAP 359
Cdd:COG1600   311 ----GDPAAVPALEALLDDPSPLVREHAAWALGRLGG 343
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
198-261 1.52e-31

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 113.35  E-value: 1.52e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1421773436 198 CGSCQACIDVCPTQAIVAP-HRVDARRCISYLTIEHAGPIPEAMRPLMGNRVYGCDDCQLACPWN 261
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 49-145 5.59e-26

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: 99.15  E-value: 5.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436  49 RARPAELVPGTVSVITARMDYLPhatldrgaaregEEGGAGWQAvefarlerPREGIVSVYARGRDYHKVLRARLQKLAD 128
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYP------------PKDPPALLD--------PDRGKISRYAWGRDYHDVLKKRLKALAA 60

                          90
                  ....*....|....*..
gi 1421773436 129 RIAAAIGPFGHRVFTDS 145
Cdd:pfam08331  61 WLEAEVPGGEYRVFVDT 77
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 182-262 3.53e-08

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: 54.36  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1421773436 182 IYVDLPLAPSEPVTA----HCGSCQACIDVCPTQAI--VAPHRVDARRCISYLTIEHAG---PIPEAMRPL----MGNRV 248
Cdd:TIGR02486 187 ILTDLPLVPTKPIDAgmakFCETCGKCADECPSGAIskGGEPTWDPEDSNGDPPGENNPglkWQYDGWRCLlfrcYNEGG 266

                          90
                  ....*....|....
gi 1421773436 249 YGCDDCQLACPWNK 262
Cdd:TIGR02486 267 GGCGVCQAVCPFNK 280
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 198-261 6.71e-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: 45.08  E-value: 6.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1421773436 198 CGSCQACIDVCPTQAIV----APHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACPWN 261
Cdd:cd10549    80 CIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVN 123
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 198-259 9.61e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 40.03  E-value: 9.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1421773436 198 CGSCQACIDVCPTQAIV---APHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACP 259
Cdd:COG2221    17 CIGCGLCVAVCPTGAISlddGKLVIDEEKCI------------------------GCGACIRVCP 57
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
194-259 1.35e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 39.71  E-value: 1.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773436 194 VTAHCGSCQACIDVCPTQAIVA---PHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACP 259
Cdd:COG2768     9 DEEKCIGCGACVKVCPVGAISIedgKAVIDPEKCI------------------------GCGACIEVCP 53
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 198-261 2.00e-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: 38.66  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773436 198 CGSCQACIDVCPTQAIVAPHRVDARRCISYltiehagpipeAMRPlmgNRVYGCDDCQLACPWN 261
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTV-----------VIDP---ERCVGCGACVAVCPTG 50
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 198-259 3.49e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.56  E-value: 3.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1421773436 198 CGSCQACIDVCPTQAIV----APHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACP 259
Cdd:COG1149    13 CIGCGLCVEVCPEGAIKlddgGAPVVDPDLCT------------------------GCGACVGVCP 54
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 196-259 5.45e-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: 40.17  E-value: 5.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1421773436 196 AHCGSCQACIDVCPTQAIVAPhrvdarrcisyltiehagpiPEAMRPLMGNRVYGCDDCQLACP 259
Cdd:TIGR01944 113 DNCIGCTKCIQACPVDAIVGA--------------------AKAMHTVIADECTGCDLCVEPCP 156
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 200-261 2.42e-03

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


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 38.39  E-value: 2.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1421773436 200 SCQ-----ACIDVCPTQAIVapHR------VDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACPWN 261
Cdd:COG0437    59 LCNhcddpPCVKVCPTGATY--KRedgivlVDYDKCI------------------------GCRYCVAACPYG 105
NapF COG1145
Ferredoxin [Energy production and conversion];
198-261 2.94e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.94  E-value: 2.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1421773436 198 CGSCQACIDVCPTQAIV-----APHRVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACPWN 261
Cdd:COG1145   184 CIGCGLCVKVCPTGAIRlkdgkPQIVVDPDKCI------------------------GCGACVKVCPVG 228
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 200-259 4.15e-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: 37.90  E-value: 4.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421773436 200 SCQ-----ACIDVCPTQA-------IVAphrVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACP 259
Cdd:cd10551    52 LCNhcenpPCVKVCPTGAtykredgIVL---VDYDKCI------------------------GCRYCMAACP 96
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 197-261 7.47e-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: 36.90  E-value: 7.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1421773436 197 HCGSCqACIDVCPTQAI-------VAphrVDARRCIsyltiehagpipeamrplmgnrvyGCDDCQLACPWN 261
Cdd:cd10562    72 HCTDA-ACVKVCPTGALyktengaVV---VDEDKCI------------------------GCGYCVAACPFD 115
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 198-225 7.85e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 35.02  E-value: 7.85e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1421773436 198 CGSCQACIDVCPTQAIVA---PHRVDARRCI 225
Cdd:COG4231    24 CTGCGACVKVCPADAIEEgdgKAVIDPDLCI 54
 
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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