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Conserved domains on  [gi|985493516|ref|WP_060791489|]
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MULTISPECIES: tRNA epoxyqueuosine(34) reductase QueG [Enterococcus]

Protein Classification

epoxyqueuosine reductase family protein( domain architecture ID 1002072)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIGR00276 super family cl36614
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 7-344 4.59e-162

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]


The actual alignment was detected with superfamily member TIGR00276:

Pssm-ID: 272993 [Multi-domain]  Cd Length: 337  Bit Score: 458.14  E-value: 4.59e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516    7 IIAESKRLGIDKIGFASAEPFLALEPSLWEQKAKGHTS--GFEHPVIEERIYPERTFENPQTIIAIALAYPTKIKE--KV 82
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPpaKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   83 PRDEKRGMFARASWGIDYHDILRERLDRLIAFIKEQAQtmeeqvEWRFAPQVDTGELVDVAAAQRAGLGFIGRNGLLITE 162
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVG------DFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  163 EFGSFVYLGEIVTNISLEPDEEVPFGCGDCMRCVTACPTKALLGDGRMNAQRCLSYQT-QTKGMMPEEYRKKMHNVIYGC 241
Cdd:TIGR00276 155 EAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGC 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  242 DICQLVCPYNRGKDFHFHQEMEPEVDTVYPKLQPMLSLSNKAFKAQFGHLSGSWRGKKPLQRNAIIALANVGDRSALPAI 321
Cdd:TIGR00276 235 DDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEA 314

                         330       340
                  ....*....|....*....|...
gi 985493516  322 WRCATEDVRPVIRGTAYWAIGQL 344
Cdd:TIGR00276 315 LEALLDDPSPLVREHAAWALGQL 337
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 7-344 4.59e-162

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: 458.14  E-value: 4.59e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516    7 IIAESKRLGIDKIGFASAEPFLALEPSLWEQKAKGHTS--GFEHPVIEERIYPERTFENPQTIIAIALAYPTKIKE--KV 82
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPpaKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   83 PRDEKRGMFARASWGIDYHDILRERLDRLIAFIKEQAQtmeeqvEWRFAPQVDTGELVDVAAAQRAGLGFIGRNGLLITE 162
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVG------DFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  163 EFGSFVYLGEIVTNISLEPDEEVPFGCGDCMRCVTACPTKALLGDGRMNAQRCLSYQT-QTKGMMPEEYRKKMHNVIYGC 241
Cdd:TIGR00276 155 EAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGC 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  242 DICQLVCPYNRGKDFHFHQEMEPEVDTVYPKLQPMLSLSNKAFKAQFGHLSGSWRGKKPLQRNAIIALANVGDRSALPAI 321
Cdd:TIGR00276 235 DDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEA 314

                         330       340
                  ....*....|....*....|...
gi 985493516  322 WRCATEDVRPVIRGTAYWAIGQL 344
Cdd:TIGR00276 315 LEALLDDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-348 1.65e-154

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: 439.25  E-value: 1.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   1 MSLKEKIIAESKRLGIDKIGFASAEPFLALEPSLWEQKAKGH--TSGFEHPVIEERIYPERTFENPQTIIAIALAYPTKI 78
Cdd:COG1600    5 MELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYhgEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  79 KEKVPRdekRGMFARASWGIDYHDILRERLDRLIAFIKEQAqtmeEQVEWRfaPQVDTGELVDVAAAQRAGLGFIGRNGL 158
Cdd:COG1600   85 EVSDPD---RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEG----PGVGYR--VFVDTAPVLERALAERAGLGWIGKNTN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 159 LITEEFGSFVYLGEIVTNISLEPDEEVPFGCGDCMRCVTACPTKALLGDGRMNAQRCLSYQT-QTKGMMPEEYRKKMHNV 237
Cdd:COG1600  156 LITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 238 IYGCDICQLVCPYNRGKDFHFHQEMEPEVDTVYPKLQPMLSLSNKAFKAQFGHLSGSWRGKKPLQRNAIIALANVGDRSA 317
Cdd:COG1600  236 IYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAA 315

                        330       340       350
                 ....*....|....*....|....*....|.
gi 985493516 318 LPAIWRCAtEDVRPVIRGTAYWAIGQLGVKE 348
Cdd:COG1600  316 VPALEALL-DDPSPLVREHAAWALGRLGGRE 345
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
189-251 2.47e-24

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 94.86  E-value: 2.47e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985493516  189 CGDCMRCVTACPTKALLGD-GRMNAQRCLSYQT-QTKGMMPEEYRKKMHNVIYGCDICQLVCPYN 251
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTiEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 177-251 2.20e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 37.76  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 177 ISLEPDEEVPFG-------CGDCMRCVTACPTKALlgdgrmnaqrclsYQTQTKGMMPEEYRKKM--HNVIYGCDICQLV 247
Cdd:cd10549   23 IELGPNGAIARGpeidedkCVFCGACVEVCPTGAI-------------ELTPEGKEYVPKEKEAEidEEKCIGCGLCVKV 89


                 ....
gi 985493516 248 CPYN 251
Cdd:cd10549   90 CPVD 93
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 7-344 4.59e-162

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: 458.14  E-value: 4.59e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516    7 IIAESKRLGIDKIGFASAEPFLALEPSLWEQKAKGHTS--GFEHPVIEERIYPERTFENPQTIIAIALAYPTKIKE--KV 82
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPpaKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   83 PRDEKRGMFARASWGIDYHDILRERLDRLIAFIKEQAQtmeeqvEWRFAPQVDTGELVDVAAAQRAGLGFIGRNGLLITE 162
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVG------DFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  163 EFGSFVYLGEIVTNISLEPDEEVPFGCGDCMRCVTACPTKALLGDGRMNAQRCLSYQT-QTKGMMPEEYRKKMHNVIYGC 241
Cdd:TIGR00276 155 EAGSWFFLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGC 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  242 DICQLVCPYNRGKDFHFHQEMEPEVDTVYPKLQPMLSLSNKAFKAQFGHLSGSWRGKKPLQRNAIIALANVGDRSALPAI 321
Cdd:TIGR00276 235 DDCQLVCPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEA 314

                         330       340
                  ....*....|....*....|...
gi 985493516  322 WRCATEDVRPVIRGTAYWAIGQL 344
Cdd:TIGR00276 315 LEALLDDPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-348 1.65e-154

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: 439.25  E-value: 1.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   1 MSLKEKIIAESKRLGIDKIGFASAEPFLALEPSLWEQKAKGH--TSGFEHPVIEERIYPERTFENPQTIIAIALAYPTKI 78
Cdd:COG1600    5 MELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYhgEMGYMERHIEKRADPRELLPGAKSVISLALNYLPEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  79 KEKVPRdekRGMFARASWGIDYHDILRERLDRLIAFIKEQAqtmeEQVEWRfaPQVDTGELVDVAAAQRAGLGFIGRNGL 158
Cdd:COG1600   85 EVSDPD---RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEG----PGVGYR--VFVDTAPVLERALAERAGLGWIGKNTN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 159 LITEEFGSFVYLGEIVTNISLEPDEEVPFGCGDCMRCVTACPTKALLGDGRMNAQRCLSYQT-QTKGMMPEEYRKKMHNV 237
Cdd:COG1600  156 LITPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 238 IYGCDICQLVCPYNRGKDFHFHQEMEPEVDTVYPKLQPMLSLSNKAFKAQFGHLSGSWRGKKPLQRNAIIALANVGDRSA 317
Cdd:COG1600  236 IYGCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAA 315

                        330       340       350
                 ....*....|....*....|....*....|.
gi 985493516 318 LPAIWRCAtEDVRPVIRGTAYWAIGQLGVKE 348
Cdd:COG1600  316 VPALEALL-DDPSPLVREHAAWALGRLGGRE 345
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
189-251 2.47e-24

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 94.86  E-value: 2.47e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 985493516  189 CGDCMRCVTACPTKALLGD-GRMNAQRCLSYQT-QTKGMMPEEYRKKMHNVIYGCDICQLVCPYN 251
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTiEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 54-136 2.25e-20

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: 84.51  E-value: 2.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516   54 RIYPERTFENPQTIIAIALAYPTKIKEKVPRDEKRGMFARASWGIDYHDILRERLDRLIAFIKEQAqtmeEQVEWRfaPQ 133
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPALLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEV----PGGEYR--VF 74


                  ...
gi 985493516  134 VDT 136
Cdd:pfam08331  75 VDT 77
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 142-268 2.92e-13

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: 69.77  E-value: 2.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516  142 VAAAQRAGLGFIGRNG-LLITEEFGSFVYLGE-IVTNISLEPDEEVPFG----CGDCMRCVTACPTKALLGDGRMNAQ-- 213
Cdd:TIGR02486 154 VAFAVLAGLGEHGRMGqAIISPEYGPRVRIAKvILTDLPLVPTKPIDAGmakfCETCGKCADECPSGAISKGGEPTWDpe 233

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985493516  214 --------RCLSYQTQTKGMMPEEYRKKMHNVIYGCDICQLVCPYNRGKDFHFHQEMEPEVDT 268
Cdd:TIGR02486 234 dsngdppgENNPGLKWQYDGWRCLLFRCYNEGGGGCGVCQAVCPFNKKPNSWIHDVVRSTVST 296
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 189-251 6.31e-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: 40.20  E-value: 6.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 985493516  189 CGDCMRCVTACPTKALLGDGRMNAQRCLSYQtqtkgMMPEEyrkkmhnvIYGCDICQLVCPYN 251
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGEKKGTKTVV-----IDPER--------CVGCGACVAVCPTG 50
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 301-342 1.66e-03

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 37.32  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 985493516  301 LQRNAIIALANVGDRSALPAIWRCATEDVRPVIRGTAYWAIG 342
Cdd:pfam13646  47 VRRAAAEALGKIGDPEALPALLELLRDDDDDVVRAAAAEALA 88
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
 301-345 1.81e-03

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 37.32  E-value: 1.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 985493516  301 LQRNAIIALANVGDRSALPAIWRCATEDvRPVIRGTAYWAIGQLG 345
Cdd:pfam13646  16 VRAAAIRALGRIGDPEAVPALLELLKDE-DPAVRRAAAEALGKIG 59
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 177-251 2.20e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 37.76  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 177 ISLEPDEEVPFG-------CGDCMRCVTACPTKALlgdgrmnaqrclsYQTQTKGMMPEEYRKKM--HNVIYGCDICQLV 247
Cdd:cd10549   23 IELGPNGAIARGpeidedkCVFCGACVEVCPTGAI-------------ELTPEGKEYVPKEKEAEidEEKCIGCGLCVKV 89


                 ....
gi 985493516 248 CPYN 251
Cdd:cd10549   90 CPVD 93
HEAT COG1413
HEAT repeat [General function prediction only];
301-345 3.21e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 37.69  E-value: 3.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 985493516 301 LQRNAIIALANVGDRSALPAIWRcATEDVRPVIRGTAYWAIGQLG 345
Cdd:COG1413   94 VRRAAAEALGRLGDPAAVPALLE-ALKDPDWEVRRAAARALGRLG 137
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 186-249 4.17e-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: 38.44  E-value: 4.17e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 985493516 186 PFGCGDCMRCVTACPTKALLGDGrmnaqrclsyqtqtkgmmpeeyrKKMHNVIY----GCDICQLVCP 249
Cdd:COG2878  136 EYGCIGCGDCIKACPFDAIVGAA-----------------------KGMHTVDEdkctGCGLCVEACP 180
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 189-249 4.24e-03

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.41  E-value: 4.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 985493516 189 CGDCMRCVTACPTKAL-LGDGRM--NAQRCLsyqtqtkgmmpeeyrkkmhnviyGCDICQLVCP 249
Cdd:COG2221   17 CIGCGLCVAVCPTGAIsLDDGKLviDEEKCI-----------------------GCGACIRVCP 57
HEAT COG1413
HEAT repeat [General function prediction only];
301-356 5.59e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 36.92  E-value: 5.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 985493516 301 LQRNAIIALANVGDRSALPAIWRcATEDVRPVIRGTAYWAIGQLGVKEPEMWLERL 356
Cdd:COG1413   63 VRAAAAEALGRIGDPEAVPALIA-ALKDEDPEVRRAAAEALGRLGDPAAVPALLEA 117
HEAT COG1413
HEAT repeat [General function prediction only];
301-356 5.75e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 36.92  E-value: 5.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 985493516 301 LQRNAIIALANVGDRSALPAIWRcATEDVRPVIRGTAYWAIGQLGVKEPEMWLERL 356
Cdd:COG1413    1 VRRAAARALGRLGDPAAVPALIA-ALADEDPDVRAAAARALGRLGDPRAVPALLEA 55
HEAT COG1413
HEAT repeat [General function prediction only];
302-348 8.26e-03

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 36.53  E-value: 8.26e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 985493516 302 QRNAIIALANVGDRSALPAIWRcATEDVRPVIRGTAYWAIGQLGVKE 348
Cdd:COG1413   33 RAAAARALGRLGDPRAVPALLE-ALKDPDPEVRAAAAEALGRIGDPE 78
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 191-268 9.94e-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: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 36.46  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985493516 191 DCMRCVTACPTKAL-----------LGDGRMNAQRCLSYQTQTkgmmpeeyrkkmhnviyGCDICQLVCPYNRGKDFHFH 259
Cdd:cd16373   58 CCDACVEVCPTGALrpldleeqkvkMGVAVIDKDRCLAWQGGT-----------------DCGVCVEACPTEAIAIVLED 120


                 ....*....
gi 985493516 260 QEMEPEVDT 268
Cdd:cd16373  121 DVLRPVVDE 129
 
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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