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Conserved domains on  [gi|15596172|ref|NP_249666|]
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radical activating enzyme [Pseudomonas aeruginosa PAO1]

Protein Classification

7-carboxy-7-deazaguanine synthase QueE( domain architecture ID 11500103)

7-carboxy-7-deazaguanine synthase QueE is a radical SAM protein that catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a common step in the biosynthesis of all 7-deazapurine-containing compounds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rSAM_QueE_gams TIGR04349
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; ...
 54-264 1.44e-158

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365.


:

Pssm-ID: 275145 [Multi-domain]  Cd Length: 210  Bit Score: 438.58  E-value: 1.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    54 LRITEIFYSLQGETRTAGLPTVFVRLTGCPLRCHYCDTAYAFSGGDVVSLDAIFERVAAYKPRYICVTGGEPLAQPNCIS 133
Cdd:TIGR04349   1 LRITEIFYSLQGETSTVGLPTVFVRLTGCPLRCVYCDTAYAFSGGERMSLDDILAQVASYGARYVTVTGGEPLAQPACLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172   134 LLERLCDAGYEVSLETSGALDVSRVDPRVSKVLDLKTPGSGEVGRNRYENIPLLTDNDQVKFVVCSREDYDWAVSKLIEY 213
Cdd:TIGR04349  81 LLTALCDAGYEVSLETSGALDISGVDPRVVKVMDLKTPGSGEVARNLWENLALLTPHDQIKFVLCDRADYDWARQKLREH 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15596172   214 RLDQRAgEVLFSPSHHQVSARELADWIVADNLPVRLQLQLHKILWNDEPGH 264
Cdd:TIGR04349 161 ALAERC-EVLFSPVYGQLAPADLAEWILADRLPVRFQLQLHKLLWGDAPGR 210
 
Name Accession Description Interval E-value
rSAM_QueE_gams TIGR04349
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; ...
 54-264 1.44e-158

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365.


Pssm-ID: 275145 [Multi-domain]  Cd Length: 210  Bit Score: 438.58  E-value: 1.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    54 LRITEIFYSLQGETRTAGLPTVFVRLTGCPLRCHYCDTAYAFSGGDVVSLDAIFERVAAYKPRYICVTGGEPLAQPNCIS 133
Cdd:TIGR04349   1 LRITEIFYSLQGETSTVGLPTVFVRLTGCPLRCVYCDTAYAFSGGERMSLDDILAQVASYGARYVTVTGGEPLAQPACLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172   134 LLERLCDAGYEVSLETSGALDVSRVDPRVSKVLDLKTPGSGEVGRNRYENIPLLTDNDQVKFVVCSREDYDWAVSKLIEY 213
Cdd:TIGR04349  81 LLTALCDAGYEVSLETSGALDISGVDPRVVKVMDLKTPGSGEVARNLWENLALLTPHDQIKFVLCDRADYDWARQKLREH 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15596172   214 RLDQRAgEVLFSPSHHQVSARELADWIVADNLPVRLQLQLHKILWNDEPGH 264
Cdd:TIGR04349 161 ALAERC-EVLFSPVYGQLAPADLAEWILADRLPVRFQLQLHKLLWGDAPGR 210
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 53-257 4.66e-92

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 270.08  E-value: 4.66e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  53 TLRITEIFYSLQGETRTAGLPTVFVRLTGCPLRCHYCDTAYAFSG--GDVVSLDAIFERVAAYKPRYICVTGGEPLAQPN 130
Cdd:COG0602   1 TLPIVEIFYSIQGEGALAGRPAVFVRLAGCNLRCSWCDTKYAWDGegGKRMSAEEILEEVAALGARHVVITGGEPLLQDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172 131 CISLLERLCDAGYEVSLETSGALDVSRVDPRVSkvLDLKTPGSGEVGRNRyENIPLLTDNDQVKFVVCSREDYDWAVSKL 210
Cdd:COG0602  81 LAELLEALKDAGYEVALETNGTLPIPAGIDWVT--VSPKLPSSGEEEDNR-ENLEVLRRADELKFVVADETDLEEAEELL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15596172 211 IEYRLDqraGEVLFSPSHHQ---VSARELADWIVADNlPVRLQLQLHKIL 257
Cdd:COG0602 158 ARLDFR---CPVYLQPVWGNkleENTELLAEWCLAHP-NVRLSPQLHKLL 203
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 81-216 8.52e-13

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 64.47  E-value: 8.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    81 GCPLRCHYCDTAYAFSGGD--VVSLDAIFERVAAYKP---RYICVTGGEPLAQPNCISLLERLC----DAGYEVSLETSG 151
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKgrELSPEEILEEAKELKRlgvEVVILGGGEPLLLPDLVELLERLLklelAEGIRITLETNG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596172   152 aldvSRVDPRVSKVLDlktpgsgEVGRNRYeNIPLLTDNDQVKFVVCSREDYDW---AVSKLIEYRLD 216
Cdd:pfam04055  84 ----TLLDEELLELLK-------EAGLDRV-SIGLESGDDEVLKLINRGHTFEEvleALELLREAGIP 139
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 80-153 4.25e-08

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 52.34  E-value: 4.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  80 TGCPLRCHYCdTAYAFSGGDVVSLDAIFE---RVAAYKPRY---ICVTGGEPLAQPNCISLLERLCD--AGYEVSLETSG 151
Cdd:cd01335   5 RGCNLNCGFC-SNPASKGRGPESPPEIEEildIVLEAKERGvevVILTGGEPLLYPELAELLRRLKKelPGFEISIETNG 83


                ..
gi 15596172 152 AL 153
Cdd:cd01335  84 TL 85
pflA PRK11145
pyruvate formate lyase 1-activating protein;
79-167 5.92e-06

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 46.17  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172   79 LTGCPLRCHYC---DTaYAFSGGDVVSLDAIFERVAAYKPRY------ICVTGGEPLAQPNCISLLERLCDA-GYEVSLE 148
Cdd:PRK11145  27 FQGCLMRCLYChnrDT-WDTHGGKEVTVEELMKEVVTYRHFMnasgggVTASGGEAILQAEFVRDWFRACKKeGIHTCLD 105

                         90
                 ....*....|....*....
gi 15596172  149 TSGAldVSRVDPRVSKVLD 167
Cdd:PRK11145 106 TNGF--VRRYDPVIDELLD 122
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 81-213 5.25e-03

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 37.38  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172     81 GCPLRCHYCDTAYAFSGGDVVSLDAIFERVAAYKPRY--------ICVTGGEPLAQPncISLLERLCDA---------GY 143
Cdd:smart00729  10 GCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGekeglvgtVFIGGGTPTLLS--PEQLEELLEAireilglakDV 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596172    144 EVSLETsgalDVSRVDPRVSKVLdlktpgsGEVGRNRYeNIPLLTDNDQVKFVVC---SREDYDWAVSKLIEY 213
Cdd:smart00729  88 EITIET----RPDTLTEELLEAL-------KEAGVNRV-SLGVQSGDDEVLKAINrghTVEDVLEAVELLREA 148
 
Name Accession Description Interval E-value
rSAM_QueE_gams TIGR04349
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; ...
 54-264 1.44e-158

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365.


Pssm-ID: 275145 [Multi-domain]  Cd Length: 210  Bit Score: 438.58  E-value: 1.44e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    54 LRITEIFYSLQGETRTAGLPTVFVRLTGCPLRCHYCDTAYAFSGGDVVSLDAIFERVAAYKPRYICVTGGEPLAQPNCIS 133
Cdd:TIGR04349   1 LRITEIFYSLQGETSTVGLPTVFVRLTGCPLRCVYCDTAYAFSGGERMSLDDILAQVASYGARYVTVTGGEPLAQPACLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172   134 LLERLCDAGYEVSLETSGALDVSRVDPRVSKVLDLKTPGSGEVGRNRYENIPLLTDNDQVKFVVCSREDYDWAVSKLIEY 213
Cdd:TIGR04349  81 LLTALCDAGYEVSLETSGALDISGVDPRVVKVMDLKTPGSGEVARNLWENLALLTPHDQIKFVLCDRADYDWARQKLREH 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15596172   214 RLDQRAgEVLFSPSHHQVSARELADWIVADNLPVRLQLQLHKILWNDEPGH 264
Cdd:TIGR04349 161 ALAERC-EVLFSPVYGQLAPADLAEWILADRLPVRFQLQLHKLLWGDAPGR 210
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 53-257 4.66e-92

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 270.08  E-value: 4.66e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  53 TLRITEIFYSLQGETRTAGLPTVFVRLTGCPLRCHYCDTAYAFSG--GDVVSLDAIFERVAAYKPRYICVTGGEPLAQPN 130
Cdd:COG0602   1 TLPIVEIFYSIQGEGALAGRPAVFVRLAGCNLRCSWCDTKYAWDGegGKRMSAEEILEEVAALGARHVVITGGEPLLQDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172 131 CISLLERLCDAGYEVSLETSGALDVSRVDPRVSkvLDLKTPGSGEVGRNRyENIPLLTDNDQVKFVVCSREDYDWAVSKL 210
Cdd:COG0602  81 LAELLEALKDAGYEVALETNGTLPIPAGIDWVT--VSPKLPSSGEEEDNR-ENLEVLRRADELKFVVADETDLEEAEELL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15596172 211 IEYRLDqraGEVLFSPSHHQ---VSARELADWIVADNlPVRLQLQLHKIL 257
Cdd:COG0602 158 ARLDFR---CPVYLQPVWGNkleENTELLAEWCLAHP-NVRLSPQLHKLL 203
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 65-168 1.05e-14

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 71.37  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  65 GETRTaglpTVFvrLTGCPLRCHYC---DTAYA--FSGGDVVSLDAIFERVAAYKPRY-----ICVTGGEPLAQP-NCIS 133
Cdd:COG1180  20 GSIRL----SVF--TQGCNLRCPYChnpEISQGrpDAAGRELSPEELVEEALKDRGFLdscggVTFSGGEPTLQPeFLLD 93

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15596172 134 LLERLCDAGYEVSLETSGALDVSRVDpRVSKVLDL 168
Cdd:COG1180  94 LAKLAKELGLHTALDTNGYIPEEALE-ELLPYLDA 127
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 81-216 8.52e-13

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 64.47  E-value: 8.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    81 GCPLRCHYCDTAYAFSGGD--VVSLDAIFERVAAYKP---RYICVTGGEPLAQPNCISLLERLC----DAGYEVSLETSG 151
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKgrELSPEEILEEAKELKRlgvEVVILGGGEPLLLPDLVELLERLLklelAEGIRITLETNG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596172   152 aldvSRVDPRVSKVLDlktpgsgEVGRNRYeNIPLLTDNDQVKFVVCSREDYDW---AVSKLIEYRLD 216
Cdd:pfam04055  84 ----TLLDEELLELLK-------EAGLDRV-SIGLESGDDEVLKLINRGHTFEEvleALELLREAGIP 139
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
 74-168 1.10e-11

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 62.77  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    74 TVFvrLTGCPLRCHYC---DTaYAFSGGDVVSLDAIFERVAAYKPRY------ICVTGGEPLAQPNCISLLERLC-DAGY 143
Cdd:TIGR02493  19 VVF--MQGCPLRCQYChnpDT-WDLKGGTEVTPEELIKEVGSYKDFFkasgggVTFSGGEPLLQPEFLSELFKACkELGI 95

                          90       100
                  ....*....|....*....|....*.
gi 15596172   144 EVSLETSGAL-DVSRVDPRVSKVLDL 168
Cdd:TIGR02493  96 HTCLDTSGFLgGCTEAADELLEYTDL 121
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 74-153 1.88e-10

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 57.99  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  74 TVFVRLTG-CPLRCHYCDTAYAFSGGDVVSLD---AIFERVAAYKPRYICVTGGEPLAQPNCISLLERLCDAGYEVSLET 149
Cdd:COG0535   1 RLQIELTNrCNLRCKHCYADAGPKRPGELSTEeakRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLST 80


                ....
gi 15596172 150 SGAL 153
Cdd:COG0535  81 NGTL 84
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 80-153 4.25e-08

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 52.34  E-value: 4.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  80 TGCPLRCHYCdTAYAFSGGDVVSLDAIFE---RVAAYKPRY---ICVTGGEPLAQPNCISLLERLCD--AGYEVSLETSG 151
Cdd:cd01335   5 RGCNLNCGFC-SNPASKGRGPESPPEIEEildIVLEAKERGvevVILTGGEPLLYPELAELLRRLKKelPGFEISIETNG 83


                ..
gi 15596172 152 AL 153
Cdd:cd01335  84 TL 85
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 71-151 1.44e-07

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 50.44  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    71 GLPTVFVRLTGCPLRCHYCDTAY--AFSGGDVVSLDAIFERVAAYKP--RYICVTGGEPLAQPNCISLLERLCDAGYEVS 146
Cdd:TIGR02495  15 GKLAFTIFLQGCNLKCPYCHNPLliPRRGSGEIEVEELLEFLRRRRGllDGVVITGGEPTLQAGLPDFLREVRELGFEVK 94


                  ....*
gi 15596172   147 LETSG 151
Cdd:TIGR02495  95 LDTNG 99
pflA PRK11145
pyruvate formate lyase 1-activating protein;
79-167 5.92e-06

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 46.17  E-value: 5.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172   79 LTGCPLRCHYC---DTaYAFSGGDVVSLDAIFERVAAYKPRY------ICVTGGEPLAQPNCISLLERLCDA-GYEVSLE 148
Cdd:PRK11145  27 FQGCLMRCLYChnrDT-WDTHGGKEVTVEELMKEVVTYRHFMnasgggVTASGGEAILQAEFVRDWFRACKKeGIHTCLD 105

                         90
                 ....*....|....*....
gi 15596172  149 TSGAldVSRVDPRVSKVLD 167
Cdd:PRK11145 106 TNGF--VRRYDPVIDELLD 122
Fer4_14 pfam13394
4Fe-4S single cluster domain;
75-161 6.03e-06

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 44.28  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    75 VFVrlTGCPLRCHYCD--TAYAFSGGDVVS---LDAIFERVAA--YKPRYICVTGGEPLA---QPNCISLLERL---CDa 141
Cdd:pfam13394   1 LFV--SGCNHSCPGCDnkETWKFNYGEPFTeelEDQIIADLKDsyIKRQGLVLTGGEPLHpwnLPVLLKLLKRVkeeYP- 77

                          90       100
                  ....*....|....*....|
gi 15596172   142 GYEVSLETSGALDVSRVDPR 161
Cdd:pfam13394  78 SKDIWLETGYTLAIDFEYPD 97
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 63-138 1.78e-04

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 40.62  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    63 LQGE-TRTaglpTVFVrlTGCPLRCHYCdtaYA-----FSGGDVVSLDAIFERVAAYKPRYI---CVTGGEPLAQ-PNCI 132
Cdd:pfam13353   1 VNGPgVRC----SLFV--SGCNHHCKGC---FNpetwdFKYGKPFTEELEDEIIEDLAKPYIqglTLSGGEPLLNaEALL 71


                  ....*.
gi 15596172   133 SLLERL 138
Cdd:pfam13353  72 ELVKRV 77
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 82-153 3.81e-04

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 41.13  E-value: 3.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  82 CPLRCHYCdtaYAFSGGDVVS-----------LDAIFERVAAYKPRYICVTGGEPLAQP----NCISLLERLCDAG--YE 144
Cdd:COG0641  11 CNLRCSYC---YYSEGDEGSRrrmseetaekaIDFLIESSGPGKELTITFFGGEPLLNFdfikEIVEYARKYAKKGkkIR 87


                ....*....
gi 15596172 145 VSLETSGAL 153
Cdd:COG0641  88 FSIQTNGTL 96
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 81-153 3.88e-04

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 40.74  E-value: 3.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  81 GCPLRCHYC----DTAYAFSGGDVVSLDAIFERV----AAYKPRYICVTGGEP-LAQPNCISLLERLCDAGYEVSLETSG 151
Cdd:COG5014  49 GCNLRCGFCwswrFRDFPLTIGKFYSPEEVAERLieiaRERGYRQVRLSGGEPtIGFEHLLKVLELFSERGLTFILETNG 128


                ..
gi 15596172 152 AL 153
Cdd:COG5014 129 IL 130
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 72-167 8.17e-04

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 40.21  E-value: 8.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172    72 LPTVFVRLT-GCPLRCHYC--DTAYAFSGGDVVSLD-----AIFERVAAYKPRYICVTGGEPLAQPNCISLLERLCDAGY 143
Cdd:TIGR04251   3 LHQIYFYLTeGCNLKCRHCwiDPKYQGEGEQHPSLDpslfrSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENNL 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15596172   144 EVSLETSGAL---DVSRV-----DPRVSKVLD 167
Cdd:TIGR04251  83 QLSVETNGLLctpQTARDlasceTPFVSVSLD 114
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 82-138 1.07e-03

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 39.90  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596172    82 CPLRCHYC---DTAYAFSGG-DVVSLDAIFERVAAY------KPRYicvTGGEPLAQPNCISLLERL 138
Cdd:TIGR02666  20 CNLRCVYCmpeGGGLDFLPKeELLTFEEIERLVRAFvglgvrKVRL---TGGEPLLRKDLVELVARL 83
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 81-213 5.25e-03

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 37.38  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172     81 GCPLRCHYCDTAYAFSGGDVVSLDAIFERVAAYKPRY--------ICVTGGEPLAQPncISLLERLCDA---------GY 143
Cdd:smart00729  10 GCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGekeglvgtVFIGGGTPTLLS--PEQLEELLEAireilglakDV 87

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596172    144 EVSLETsgalDVSRVDPRVSKVLdlktpgsGEVGRNRYeNIPLLTDNDQVKFVVC---SREDYDWAVSKLIEY 213
Cdd:smart00729  88 EITIET----RPDTLTEELLEAL-------KEAGVNRV-SLGVQSGDDEVLKAINrghTVEDVLEAVELLREA 148
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
74-153 8.33e-03

Uncharacterized radical SAM domain-containing protein [Function unknown];


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 37.25  E-value: 8.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596172  74 TVFVrlTG-CPLRCHYCDTAYAFSGGDVV--------SLDAIFERVAAYKPRYICVTGGEPLAQP----NCISLLERLCD 140
Cdd:COG2108  30 VLFI--TGlCNRNCFYCPLSEERKGKDVIyanerpveSDEDVIEEARRMGALGAGITGGEPLLVLdrtlEYIRLLKEEFG 107

                        90
                ....*....|...
gi 15596172 141 AGYEVSLETSGAL 153
Cdd:COG2108 108 PDHHIHLYTNGIL 120
 
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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