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Conserved domains on  [gi|515498090|ref|WP_016931344|]
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MULTISPECIES: tRNA epoxyqueuosine(34) reductase QueG [Staphylococcus]

Protein Classification

epoxyqueuosine reductase( domain architecture ID 11489053)

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 ...
10-342 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: 507.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   10 IIDYAYSIGIDSIGFTTADPFDELKKKLEDYHANGYAS--GFEESDISLRTEPKLSLPTARSIIAIAVGYPNKLKGAPKS 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   88 VRGDRRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDTGVLSDRAVAERAGLGFAGRNGFIINPDLGTWS 167
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  168 YLGELLVSIPFEPDDPLLDSCGDCTICVDRCPTGALVGNGQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLYGCDTCQQV 246
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  247 CPRNRGINTT-HDDIILEPEILKPRLVPLLQMSNKEFKQTYGHLAGAWRGKKTIQRNAIIALAHFNEETAIPELKEVALN 325
Cdd:TIGR00276 241 CPWNKFADAThEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320
                         330
                  ....*....|....*..
gi 515498090  326 DPRPMIRGTAYWAIGQI 342
Cdd:TIGR00276 321 DPSPLVREHAAWALGQL 337
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
316-370 2.46e-03

HEAT repeats; This family includes multiple HEAT repeats.


:

Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 36.55  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515498090  316 IPELKEVALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEAL 55
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
10-342 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: 507.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   10 IIDYAYSIGIDSIGFTTADPFDELKKKLEDYHANGYAS--GFEESDISLRTEPKLSLPTARSIIAIAVGYPNKLKGAPKS 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   88 VRGDRRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDTGVLSDRAVAERAGLGFAGRNGFIINPDLGTWS 167
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  168 YLGELLVSIPFEPDDPLLDSCGDCTICVDRCPTGALVGNGQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLYGCDTCQQV 246
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  247 CPRNRGINTT-HDDIILEPEILKPRLVPLLQMSNKEFKQTYGHLAGAWRGKKTIQRNAIIALAHFNEETAIPELKEVALN 325
Cdd:TIGR00276 241 CPWNKFADAThEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320
                         330
                  ....*....|....*..
gi 515498090  326 DPRPMIRGTAYWAIGQI 342
Cdd:TIGR00276 321 DPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
2-346 1.79e-157

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: 446.19  E-value: 1.79e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   2 DYNWLKQEIIDYAYSIGIDSIGFTTADPFDELKKKLEDYHANGYA--SGFEESDISLRTEPKLSLPTARSIIAIAVGYPN 79
Cdd:COG1600    3 DLMELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHgeMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  80 KLKGAPKSvrgdrRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDTGVLSDRAVAERAGLGFAGRNGFII 159
Cdd:COG1600   83 EEEVSDPD-----RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 160 NPDLGTWSYLGELLVSIPFEPDDPLLDSCGDCTICVDRCPTGALVGNGQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLY 238
Cdd:COG1600  158 TPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNRIY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 239 GCDTCQQVCPRNRGINTT-HDDIILEPEILKPRLVPLLQMSNKEFKQTYGHLAGAWRGKKTIQRNAIIALAHFNEETAIP 317
Cdd:COG1600  238 GCDDCQDVCPWNRFAQPTrEPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAAVP 317
                        330       340
                 ....*....|....*....|....*....
gi 515498090 318 ELKEvALNDPRPMIRGTAYWAIGQIQGED 346
Cdd:COG1600  318 ALEA-LLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
57-135 8.28e-25

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: 96.07  E-value: 8.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498090   57 RTEPKLSLPTARSIIAIAVGYpnKLKGAPKSVRGDRRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDT 135
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNY--YPPKDPPALLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
190-273 4.84e-05

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: 43.01  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 190 DCTICVDRCPTGALV-----------GNGQLNSQKCISFLTQTkgylqdeyrykignrlyGCDTCQQVCPrnrgintTHD 258
Cdd:cd16373   58 CCDACVEVCPTGALRpldleeqkvkmGVAVIDKDRCLAWQGGT-----------------DCGVCVEACP-------TEA 113
                         90
                 ....*....|....*.
gi 515498090 259 -DIILEPEILKPRLVP 273
Cdd:cd16373  114 iAIVLEDDVLRPVVDE 129
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
316-370 2.46e-03

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 36.55  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515498090  316 IPELKEVALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEAL 55
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
10-342 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: 507.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   10 IIDYAYSIGIDSIGFTTADPFDELKKKLEDYHANGYAS--GFEESDISLRTEPKLSLPTARSIIAIAVGYPNKLKGAPKS 87
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKERLLAWLEAGYHGemGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   88 VRGDRRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDTGVLSDRAVAERAGLGFAGRNGFIINPDLGTWS 167
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  168 YLGELLVSIPFEPDDPLLDSCGDCTICVDRCPTGALVGNGQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLYGCDTCQQV 246
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTiELKGPIPEEFRPLIGNRIYGCDDCQLV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  247 CPRNRGINTT-HDDIILEPEILKPRLVPLLQMSNKEFKQTYGHLAGAWRGKKTIQRNAIIALAHFNEETAIPELKEVALN 325
Cdd:TIGR00276 241 CPWNKFADAThEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320
                         330
                  ....*....|....*..
gi 515498090  326 DPRPMIRGTAYWAIGQI 342
Cdd:TIGR00276 321 DPSPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
2-346 1.79e-157

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: 446.19  E-value: 1.79e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090   2 DYNWLKQEIIDYAYSIGIDSIGFTTADPFDELKKKLEDYHANGYA--SGFEESDISLRTEPKLSLPTARSIIAIAVGYPN 79
Cdd:COG1600    3 DLMELKEEIKAWARELGFDLVGIAPADPLPEAEERLEEWLAAGYHgeMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  80 KLKGAPKSvrgdrRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDTGVLSDRAVAERAGLGFAGRNGFII 159
Cdd:COG1600   83 EEEVSDPD-----RGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 160 NPDLGTWSYLGELLVSIPFEPDDPLLDSCGDCTICVDRCPTGALVGNGQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLY 238
Cdd:COG1600  158 TPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTiELKGPIPEELRPKMGNRIY 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 239 GCDTCQQVCPRNRGINTT-HDDIILEPEILKPRLVPLLQMSNKEFKQTYGHLAGAWRGKKTIQRNAIIALAHFNEETAIP 317
Cdd:COG1600  238 GCDDCQDVCPWNRFAQPTrEPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSGDPAAVP 317
                        330       340
                 ....*....|....*....|....*....
gi 515498090 318 ELKEvALNDPRPMIRGTAYWAIGQIQGED 346
Cdd:COG1600  318 ALEA-LLDDPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
57-135 8.28e-25

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: 96.07  E-value: 8.28e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498090   57 RTEPKLSLPTARSIIAIAVGYpnKLKGAPKSVRGDRRGMFARASWGQDYHSIMRKRLDKLADFIQSKVPDVELKSMVDT 135
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNY--YPPKDPPALLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
188-250 2.95e-23

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 91.78  E-value: 2.95e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498090  188 CGDCTICVDRCPTGALVGN-GQLNSQKCISFLT-QTKGYLQDEYRYKIGNRLYGCDTCQQVCPRN 250
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTiEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
299-362 3.15e-09

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 53.50  E-value: 3.15e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498090  299 IQRNAIIALAHFNEETAIPELKEvALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEV 362
Cdd:pfam13646  16 VRAAAIRALGRIGDPEAVPALLE-LLKDEDPAVRRAAAEALGKIGDPEALPALLELLRDDDDDV 78
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
142-262 4.64e-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: 57.06  E-value: 4.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  142 AVAERAGLGFAGRNG-FIINPDLGTWSYLGELLVS-IPFEPDDP----LLDSCGDCTICVDRCPTGAL------VGNGQL 209
Cdd:TIGR02486 155 AFAVLAGLGEHGRMGqAIISPEYGPRVRIAKVILTdLPLVPTKPidagMAKFCETCGKCADECPSGAIskggepTWDPED 234
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515498090  210 NSQKCISFLTQTKGYLQDEYR----YKIGNRLYGCDTCQQVCPRNRGINTTHDDIIL 262
Cdd:TIGR02486 235 SNGDPPGENNPGLKWQYDGWRcllfRCYNEGGGGCGVCQAVCPFNKKPNSWIHDVVR 291
HEAT COG1413
HEAT repeat [General function prediction only];
299-370 9.36e-08

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 50.78  E-value: 9.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498090 299 IQRNAIIALAHFNEETAIPELKEvALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:COG1413   32 VRAAAARALGRLGDPRAVPALLE-ALKDPDPEVRAAAAEALGRIGDPEAVPALIAALKDEDPEVRRAAAEAL 102
HEAT COG1413
HEAT repeat [General function prediction only];
299-370 5.41e-07

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 48.47  E-value: 5.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498090 299 IQRNAIIALAHFNEETAIPELKEvALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:COG1413    1 VRRAAARALGRLGDPAAVPALIA-ALADEDPDVRAAAARALGRLGDPRAVPALLEALKDPDPEVRAAAAEAL 71
HEAT COG1413
HEAT repeat [General function prediction only];
299-370 1.14e-06

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 47.32  E-value: 1.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498090 299 IQRNAIIALAHFNEETAIPELKEvALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:COG1413   63 VRAAAAEALGRIGDPEAVPALIA-ALKDEDPEVRRAAAEALGRLGDPAAVPALLEALKDPDWEVRRAAARAL 133
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
190-273 4.84e-05

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: 43.01  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 190 DCTICVDRCPTGALV-----------GNGQLNSQKCISFLTQTkgylqdeyrykignrlyGCDTCQQVCPrnrgintTHD 258
Cdd:cd16373   58 CCDACVEVCPTGALRpldleeqkvkmGVAVIDKDRCLAWQGGT-----------------DCGVCVEACP-------TEA 113
                         90
                 ....*....|....*.
gi 515498090 259 -DIILEPEILKPRLVP 273
Cdd:cd16373  114 iAIVLEDDVLRPVVDE 129
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
299-340 5.87e-05

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 41.17  E-value: 5.87e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 515498090  299 IQRNAIIALAHFNEETAIPELKEVALNDPRPMIRGTAYWAIG 340
Cdd:pfam13646  47 VRRAAAEALGKIGDPEALPALLELLRDDDDDVVRAAAAEALA 88
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
186-248 1.83e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 39.26  E-value: 1.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498090 186 DSCGDCTICVDRCPTGAL-VGNGQL--NSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCP 248
Cdd:COG2221   15 EKCIGCGLCVAVCPTGAIsLDDGKLviDEEKCI-----------------------GCGACIRVCP 57
HEAT COG1413
HEAT repeat [General function prediction only];
299-342 2.03e-04

HEAT repeat [General function prediction only];


Pssm-ID: 441023 [Multi-domain]  Cd Length: 137  Bit Score: 41.15  E-value: 2.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 515498090 299 IQRNAIIALAHFNEETAIPELKEvALNDPRPMIRGTAYWAIGQI 342
Cdd:COG1413   94 VRRAAAEALGRLGDPAAVPALLE-ALKDPDWEVRRAAARALGRL 136
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
186-250 2.47e-04

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 42.36  E-value: 2.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498090 186 DSCGDCTICVDRCPTGALVGNGQLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:COG0348  210 GDCIDCGLCVKVCPMGIDIRKGEINQSECI-----------------------NCGRCIDACPKD 251
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
186-250 3.72e-04

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 41.85  E-value: 3.72e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498090  186 DSCGDCticVDRCPTGAL-VGNGQL--NSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:TIGR04041  44 DHCGDC---VAGCPAGALsLVDGKVvwDKERCI-----------------------GCDTCIKVCPHQ 85
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
186-248 6.53e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 37.79  E-value: 6.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498090 186 DSCGDCTICVDRCPTGAL-VGNG--QLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCP 248
Cdd:COG2768   11 EKCIGCGACVKVCPVGAIsIEDGkaVIDPEKCI-----------------------GCGACIEVCP 53
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
188-250 8.36e-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: 37.12  E-value: 8.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498090  188 CGDCTICVDRCPTGALVgngqlnsqkcISFLTQTKGylqdEYRYKIGNRL-YGCDTCQQVCPRN 250
Cdd:pfam12838   1 CIGCGACVAACPVGAIT----------LDEVGEKKG----TKTVVIDPERcVGCGACVAVCPTG 50
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
186-248 1.07e-03

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 37.33  E-value: 1.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498090 186 DSCGDCTICVDRCPTGALVGNG---QLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCP 248
Cdd:COG4231   22 DKCTGCGACVKVCPADAIEEGDgkaVIDPDLCI-----------------------GCGSCVQVCP 64
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
186-250 1.55e-03

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 36.63  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498090 186 DSCGDCTICVDRCPTGAL-VGNG---QLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:COG1149   11 EKCIGCGLCVEVCPEGAIkLDDGgapVVDPDLCT-----------------------GCGACVGVCPTG 56
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
186-250 1.76e-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: 39.59  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498090 186 DSCGDCTICVDRCPTGALVGNGQL----NSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:COG2878  137 YGCIGCGDCIKACPFDAIVGAAKGmhtvDEDKCT-----------------------GCGLCVEACPVD 182
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
186-250 2.10e-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: 2.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498090 186 DSCGDCTICVDRCPTGALVGNGQL----NSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:cd10549   78 EKCIGCGLCVKVCPVDAITLEDELeiviDKEKCI-----------------------GCGICAEVCPVN 123
HEAT_2 pfam13646
HEAT repeats; This family includes multiple HEAT repeats.
316-370 2.46e-03

HEAT repeats; This family includes multiple HEAT repeats.


Pssm-ID: 433376 [Multi-domain]  Cd Length: 88  Bit Score: 36.55  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515498090  316 IPELKEVALNDPRPMIRGTAYWAIGQIQGEDAREFIVANYENEIEEVQNEMIKGL 370
Cdd:pfam13646   1 LPALLQALLRDPDPEVRAAAIRALGRIGDPEAVPALLELLKDEDPAVRRAAAEAL 55
Fer4_9 pfam13187
4Fe-4S dicluster domain;
188-250 4.92e-03

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 34.84  E-value: 4.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090  188 CGDCTICVDRCPTGALVG-------NGQLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCPRN 250
Cdd:pfam13187   2 CTGCGACVAACPAGAIVPdlvgqtiRGDIAGLACI-----------------------GCGACVDACPRG 48
HEAT_EZ pfam13513
HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats ...
299-342 5.43e-03

HEAT-like repeat; The HEAT repeat family is related to armadillo/beta-catenin-like repeats (see pfam00514). These EZ repeats are found in subunits of cyanobacterial phycocyanin lyase and other proteins and probably carry out a scaffolding role.


Pssm-ID: 463906 [Multi-domain]  Cd Length: 55  Bit Score: 34.65  E-value: 5.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515498090  299 IQRNAIIALAHFNEET----------AIPELkEVALNDPRPMIRGTAYWAIGQI 342
Cdd:pfam13513   3 VREAAALALGSLAEGGpdllapavpeLLPAL-LPLLNDDSDLVREAAAWALGRL 55
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
191-248 6.64e-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: 6.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498090 191 CTICVDR-----CPTGALV---GNGQLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCP 248
Cdd:COG1142   52 CRHCEDApcaevCPVGAITrddGAVVVDEEKCI-----------------------GCGLCVLACP 94
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
186-248 8.93e-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: 34.72  E-value: 8.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498090 186 DSCGDCTICVDRCPTGALVGNG-------QLNSQKCIsfltqtkgylqdeyrykignrlyGCDTCQQVCP 248
Cdd:COG1143    2 DKCIGCGLCVRVCPVDAITIEDgepgkvyVIDPDKCI-----------------------GCGLCVEVCP 48
 
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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