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Conserved domains on  [gi|495053574|ref|WP_007778410|]
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tRNA epoxyqueuosine(34) reductase QueG [Cronobacter malonaticus]

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 ...
 14-348 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: 608.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   14 IKQWGAELGFQQVGITDTDLSASEGA-LQAWLDKQYHGEMEWMARHGMLRARPHELLPGTLRVISVRMNYLPANAAFAST 92
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   93 LKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDSAPILERPLAEKAGLGWTGKHSLILSRDAGSFF 172
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  173 FLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLMGNRIYGCDDCQLI 252
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQLV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  253 CPWNRFSQLTDEADFSPRKSLHAPKLIELFSWSEAHFLKVTEGSAIRRIGHLRWLRNIAVALGNAPWDEANITALRQRKG 332
Cdd:TIGR00276 241 CPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320

                         330
                  ....*....|....*..
gi 495053574  333 EH-PLLDEHIDWAIAQQ 348
Cdd:TIGR00276 321 DPsPLVREHAAWALGQL 337
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 14-348 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: 608.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   14 IKQWGAELGFQQVGITDTDLSASEGA-LQAWLDKQYHGEMEWMARHGMLRARPHELLPGTLRVISVRMNYLPANAAFAST 92
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   93 LKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDSAPILERPLAEKAGLGWTGKHSLILSRDAGSFF 172
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  173 FLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLMGNRIYGCDDCQLI 252
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQLV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  253 CPWNRFSQLTDEADFSPRKSLHAPKLIELFSWSEAHFLKVTEGSAIRRIGHLRWLRNIAVALGNAPWDEANITALRQRKG 332
Cdd:TIGR00276 241 CPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320

                         330
                  ....*....|....*..
gi 495053574  333 EH-PLLDEHIDWAIAQQ 348
Cdd:TIGR00276 321 DPsPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 6-352 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: 554.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   6 DLNQLAQKIKQWGAELGFQQVGITDTD-LSASEGALQAWLDKQYHGEMEWMARHGMLRARPHELLPGTLRVISVRMNYLP 84
Cdd:COG1600    3 DLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  85 ANAAfastlKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDSAPILERPLAEKAGLGWTGKHSLIL 164
Cdd:COG1600   83 EEEV-----SDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574 165 SRDAGSFFFLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLMGNRIY 244
Cdd:COG1600  158 TPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574 245 GCDDCQLICPWNRFSQLTDEADFSPRKSLHAPKLIELFSWSEAHFLKVTEGSAIRRIGHLRWLRNIAVALGNAPwDEANI 324
Cdd:COG1600  238 GCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPAAV 316

                        330       340
                 ....*....|....*....|....*....
gi 495053574 325 TALRQRKG-EHPLLDEHIDWAIAQQTDKR 352
Cdd:COG1600  317 PALEALLDdPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 62-140 9.27e-32

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: 114.94  E-value: 9.27e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495053574   62 RARPHELLPGTLRVISVRMNYLPANAAFAstLKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDS 140
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPA--LLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 190-258 2.05e-04

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 2.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495053574 190 EEGCGRCVACMTICPTGAIV----EPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICPWNRF 258
Cdd:cd10549   77 EEKCIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVNAI 125
 
Name Accession Description Interval E-value
TIGR00276 TIGR00276
epoxyqueuosine reductase; This model was rebuilt to exclude archaeal homologs, now that there ...
 14-348 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: 608.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   14 IKQWGAELGFQQVGITDTDLSASEGA-LQAWLDKQYHGEMEWMARHGMLRARPHELLPGTLRVISVRMNYLPANAAFAST 92
Cdd:TIGR00276   1 IKAWAKELGFDKIGITDADLFPEEKErLLAWLEAGYHGEMGFMARHGEKRARPAELLPGTRSVISVRMDYLPKLAPPAKS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   93 LKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDSAPILERPLAEKAGLGWTGKHSLILSRDAGSFF 172
Cdd:TIGR00276  81 LKDPERGYISRYALGRDYHKVLRKRLKKLAEFIEEEVGDFGYRVFVDTAPVLERALAERAGLGWIGKHTLLINREAGSWF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  173 FLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLMGNRIYGCDDCQLI 252
Cdd:TIGR00276 161 FLGEIFTNLPLPPDAPVTDHCGSCTACLDACPTGAIVAPYQLDARRCISYLTIELKGPIPEEFRPLIGNRIYGCDDCQLV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  253 CPWNRFSQLTDEADFSPRKSLHAPKLIELFSWSEAHFLKVTEGSAIRRIGHLRWLRNIAVALGNAPWDEANITALRQRKG 332
Cdd:TIGR00276 241 CPWNKFADATHEPDFQPRHELDAPSLIELLAWDEAEFLERFGGSAIRRIGKKRWLRNAAVALGNAPGSPAIIEALEALLD 320

                         330
                  ....*....|....*..
gi 495053574  333 EH-PLLDEHIDWAIAQQ 348
Cdd:TIGR00276 321 DPsPLVREHAAWALGQL 337
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 6-352 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: 554.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574   6 DLNQLAQKIKQWGAELGFQQVGITDTD-LSASEGALQAWLDKQYHGEMEWMARHGMLRARPHELLPGTLRVISVRMNYLP 84
Cdd:COG1600    3 DLMELKEEIKAWARELGFDLVGIAPADpLPEAEERLEEWLAAGYHGEMGYMERHIEKRADPRELLPGAKSVISLALNYLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  85 ANAAfastlKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDSAPILERPLAEKAGLGWTGKHSLIL 164
Cdd:COG1600   83 EEEV-----SDPDRGKISRYAWGRDYHKVLRKRLKKLAEFLEEEGPGVGYRVFVDTAPVLERALAERAGLGWIGKNTNLI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574 165 SRDAGSFFFLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVEPYTVDARRCISYLTIELEGAIPEEFRPLMGNRIY 244
Cdd:COG1600  158 TPEFGSWFFLGEILTDLELPPDEPVEDHCGSCTRCLDACPTGAIVAPYVLDARRCISYLTIELKGPIPEELRPKMGNRIY 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574 245 GCDDCQLICPWNRFSQLTDEADFSPRKSLHAPKLIELFSWSEAHFLKVTEGSAIRRIGHLRWLRNIAVALGNAPwDEANI 324
Cdd:COG1600  238 GCDDCQDVCPWNRFAQPTREPDFQPRPELAAPDLEELLALDEAEFRERFGGSAIRRIGRERLLRNAAIALGNSG-DPAAV 316

                        330       340
                 ....*....|....*....|....*....
gi 495053574 325 TALRQRKG-EHPLLDEHIDWAIAQQTDKR 352
Cdd:COG1600  317 PALEALLDdPSPLVREHAAWALGRLGGRE 345
QueG_DUF1730 pfam08331
Epoxyqueuosine reductase QueG, DUF1730; This domain of unknown function occurs in ...
 62-140 9.27e-32

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: 114.94  E-value: 9.27e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495053574   62 RARPHELLPGTLRVISVRMNYLPANAAFAstLKDPSLGYVSRYALGRDYHKLLRNRLKKLGETLQQHCASLNFRPFVDS 140
Cdd:pfam08331   1 RADPRLLLPGARSVISLALNYYPPKDPPA--LLDPDRGKISRYAWGRDYHDVLKKRLKALAAWLEAEVPGGEYRVFVDT 77
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
193-256 8.58e-30

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 109.12  E-value: 8.58e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495053574  193 CGRCVACMTICPTGAIVEP-YTVDARRCISYLTIELEGAIPEEFRPLMGNRIYGCDDCQLICPWN 256
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPeGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
RDH TIGR02486
reductive dehalogenase; This model represents a family of corrin and 8-iron Fe-S ...
 125-256 9.90e-07

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: 50.13  E-value: 9.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574  125 LQQHCASLNFRPFV---DSAPILERPLAEKAGLGWTGKH-SLILSRDAGSFFFLGE-LLVDLPLPVDKPVEEG----CGR 195
Cdd:TIGR02486 130 LQQFIRNLGYNAVPsgnGNGLGSSVAFAVLAGLGEHGRMgQAIISPEYGPRVRIAKvILTDLPLVPTKPIDAGmakfCET 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495053574  196 CVACMTICPTGAIVE--PYTVDARR--------CISYLTIELEGAIPEEFRPlMGNRIYGCDDCQLICPWN 256
Cdd:TIGR02486 210 CGKCADECPSGAISKggEPTWDPEDsngdppgeNNPGLKWQYDGWRCLLFRC-YNEGGGGCGVCQAVCPFN 279
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 190-258 2.05e-04

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


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 2.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495053574 190 EEGCGRCVACMTICPTGAIV----EPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICPWNRF 258
Cdd:cd10549   77 EEKCIGCGLCVKVCPVDAITledeLEIVIDKEKCI------------------------GCGICAEVCPVNAI 125
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 192-254 2.83e-04

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.88  E-value: 2.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495053574 192 GCGRCVAcmtICPTGAIV---EPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICP 254
Cdd:COG2221   19 GCGLCVA---VCPTGAISlddGKLVIDEEKCI------------------------GCGACIRVCP 57
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
189-254 7.22e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 37.79  E-value: 7.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495053574 189 VEEGCGRCVACMTICPTGAIV---EPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICP 254
Cdd:COG2768    9 DEEKCIGCGACVKVCPVGAISiedGKAVIDPEKCI------------------------GCGACIEVCP 53
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 190-254 8.60e-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: 37.40  E-value: 8.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495053574 190 EEGCGRCVACMTICPTGAIV----EPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICP 254
Cdd:COG1149   10 EEKCIGCGLCVEVCPEGAIKlddgGAPVVDPDLCT------------------------GCGACVGVCP 54
NapF COG1145
Ferredoxin [Energy production and conversion];
171-256 1.36e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 40.09  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495053574 171 FFFLGELLVDLPLPVDKPVEEGCGRCVACMTICPTGAIVE-----PYTVDARRCIsyltielegaipeefrplmgnriyG 245
Cdd:COG1145  162 KKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLkdgkpQIVVDPDKCI------------------------G 217

                         90
                 ....*....|.
gi 495053574 246 CDDCQLICPWN 256
Cdd:COG1145  218 CGACVKVCPVG 228
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 192-256 2.43e-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: 2.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495053574  192 GCGRCVAcmtICPTGAIvepytvdarrcisylTIELEGAIPEEFRPLMGNRI-YGCDDCQLICPWN 256
Cdd:pfam12838   3 GCGACVA---ACPVGAI---------------TLDEVGEKKGTKTVVIDPERcVGCGACVAVCPTG 50
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 190-254 4.62e-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: 4.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495053574 190 EEGCGRCVACMTICPTGAI-------VEPYTVDARRCIsyltielegaipeefrplmgnriyGCDDCQLICP 254
Cdd:COG1143    1 EDKCIGCGLCVRVCPVDAItiedgepGKVYVIDPDKCI------------------------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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