NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74139984|dbj|BAE31827|]
View 

unnamed protein product [Mus musculus]

Protein Classification

radical SAM protein( domain architecture ID 11500009)

radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfer of a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 13-362 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


:

Pssm-ID: 212001  Cd Length: 347  Bit Score: 771.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    13 LLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEdgnSTQPTTPVSVNYHFTRQCNYKCGFCF 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEPTRKEEEED---PDQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    93 HTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGE 172
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   173 YLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 252
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   253 LIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEE 332
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 74139984   333 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 362
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 13-362 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 771.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    13 LLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEdgnSTQPTTPVSVNYHFTRQCNYKCGFCF 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEPTRKEEEED---PDQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    93 HTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGE 172
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   173 YLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 252
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   253 LIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEE 332
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 74139984   333 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 362
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 75-349 2.88e-100

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 297.92  E-value: 2.88e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   75 SVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQdrGEYLGKLVRFCK 145
Cdd:NF038283   3 VINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  146 EeLALpSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKN--HVENLQKLRRWCRDY--KVAFKI 221
Cdd:NF038283  81 E-LGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKLKI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  222 NSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENsgedalreaERFLISNEEFETFLERHKEV-SCLVPESNQKMKD 300
Cdd:NF038283 159 NTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDMTG 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74139984  301 SYLILDEYMRFL-NCTGGRK-DPSKSILDVGVEEAIKFSGFDEKMFLKRGG 349
Cdd:NF038283 230 SYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 79-283 3.14e-23

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: 95.86  E-value: 3.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  79 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKQAGLEKINFSGGEPFLQdrgEYLGKLVRFCKEELALPSVS 154
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLY---PELAELLRRLKKELPGFEIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984 155 IVSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNhvENLQKLRRWCRdYKVAFKINSVINRFNVD-E 232
Cdd:cd01335  79 IETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELRE-AGLGLSTTLLVGLGDEDeE 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74139984 233 DMNEHIKAL----SPVRWKVFQCLLIEGensgedALREAERFLISNEEFETFLER 283
Cdd:cd01335 156 DDLEELELLaefrSPDRVSLFRLLPEEG------TPLELAAPVVPAEKLLRLIAA 204
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 75-224 4.28e-20

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: 85.73  E-value: 4.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  75 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKQAGLEKINFSGGEPFLqdRgEYLGKLVRFCKEelALPS 152
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAKE--LGIR 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74139984 153 VSIVSNGSLIRE---RWFKDYGeyLDILAISCDSFDEQVNALIGRGQGKKNHV-ENLqklrRWCRDYKVAFKINSV 224
Cdd:COG0535  76 VNLSTNGTLLTEelaERLAEAG--LDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 80-210 2.67e-18

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: 81.03  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    80 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFcKEELALPSVSI 155
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLK-LELAEGIRITL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74139984   156 VSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRR 210
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE 135
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 78-256 3.54e-14

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: 70.89  E-value: 3.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984     78 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKQAG-----LEKINFSGGEPFLQDRgEYLGKLVRFCKEELAL 150
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSP-EQLEELLEAIREILGL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    151 P---SVSIVSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRwcrdykvAFKINsvin 226
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-------AGPIK---- 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 74139984    227 rFNVD-------------EDMNEHIKALSPVRWKVFQCLLIEG 256
Cdd:smart00729 153 -VSTDlivglpgeteedfEETLKLLKELGPDRVSIFPLSPRPG 194
moaA PRK00164
GTP 3',8-cyclase MoaA;
74-239 2.58e-08

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 54.76  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   74 VSVnyhfTRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKQA---GLEKINFSGGEPFL-QDrgeyLGKLVRFC 144
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  145 KEELALPSVSIVSNGSLIRER---WfKDYGeyLDILAISCDSFDEQVNALI-GRGqgkknhvenlqKLRRWCRDYKVAF- 219
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLARRaaaL-KDAG--LDRVNVSLDSLDPERFKAItGRD-----------RLDQVLAGIDAALa 155

                        170       180
                 ....*....|....*....|....*....
gi 74139984  220 ------KINSVINR-FNVDE--DMNEHIK 239
Cdd:PRK00164 156 agltpvKVNAVLMKgVNDDEipDLLEWAK 184
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 13-362 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 771.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    13 LLSLFQQQLGSLWSGLAILFCWLRIALGWLDPGKEQPQVRGEPEDTQETQEdgnSTQPTTPVSVNYHFTRQCNYKCGFCF 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEPTRKEEEED---PDQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    93 HTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGE 172
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   173 YLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 252
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   253 LIEGENSGEDALREAERFLISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSKSILDVGVEE 332
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 74139984   333 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 362
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 75-349 2.88e-100

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 297.92  E-value: 2.88e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   75 SVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQdrGEYLGKLVRFCK 145
Cdd:NF038283   3 VINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  146 EeLALpSVSIVSNGSLIRERWFKDYGEYLDILAISCDSFDEQVNALIGRGQGKKN--HVENLQKLRRWCRDY--KVAFKI 221
Cdd:NF038283  81 E-LGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKLKI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  222 NSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENsgedalreaERFLISNEEFETFLERHKEV-SCLVPESNQKMKD 300
Cdd:NF038283 159 NTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDMTG 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74139984  301 SYLILDEYMRFL-NCTGGRK-DPSKSILDVGVEEAIKFSGFDEKMFLKRGG 349
Cdd:NF038283 230 SYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 79-283 3.14e-23

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: 95.86  E-value: 3.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  79 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKQAGLEKINFSGGEPFLQdrgEYLGKLVRFCKEELALPSVS 154
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLY---PELAELLRRLKKELPGFEIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984 155 IVSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNhvENLQKLRRWCRdYKVAFKINSVINRFNVD-E 232
Cdd:cd01335  79 IETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELRE-AGLGLSTTLLVGLGDEDeE 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74139984 233 DMNEHIKAL----SPVRWKVFQCLLIEGensgedALREAERFLISNEEFETFLER 283
Cdd:cd01335 156 DDLEELELLaefrSPDRVSLFRLLPEEG------TPLELAAPVVPAEKLLRLIAA 204
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 75-224 4.28e-20

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: 85.73  E-value: 4.28e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  75 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKQAGLEKINFSGGEPFLqdRgEYLGKLVRFCKEelALPS 152
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAKE--LGIR 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74139984 153 VSIVSNGSLIRE---RWFKDYGeyLDILAISCDSFDEQVNALIGRGQGKKNHV-ENLqklrRWCRDYKVAFKINSV 224
Cdd:COG0535  76 VNLSTNGTLLTEelaERLAEAG--LDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 80-210 2.67e-18

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: 81.03  E-value: 2.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    80 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFcKEELALPSVSI 155
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLK-LELAEGIRITL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74139984   156 VSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRR 210
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE 135
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 78-256 3.54e-14

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: 70.89  E-value: 3.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984     78 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKQAG-----LEKINFSGGEPFLQDRgEYLGKLVRFCKEELAL 150
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSP-EQLEELLEAIREILGL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    151 P---SVSIVSNGSLIRERWFKDYGEY-LDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRwcrdykvAFKINsvin 226
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-------AGPIK---- 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 74139984    227 rFNVD-------------EDMNEHIKALSPVRWKVFQCLLIEG 256
Cdd:smart00729 153 -VSTDlivglpgeteedfEETLKLLKELGPDRVSIFPLSPRPG 194
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 81-283 2.08e-10

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 61.16  E-value: 2.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  81 TRQCNYKCGFCF---HTAKTSFVLPLEEAKRGLLLLKQAGLE----KINFSGGEPFLqdRGEYLGKLVRFCKEELALP-- 151
Cdd:COG0641   8 TSRCNLRCSYCYyseGDEGSRRRMSEETAEKAIDFLIESSGPgkelTITFFGGEPLL--NFDFIKEIVEYARKYAKKGkk 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984 152 -SVSIVSNGSLIRERW---FKDYGeylDILAISCDSfDEQVNAL--IGRGqGKKNH---VENLQKLrrwcRDYKVAFKIN 222
Cdd:COG0641  86 iRFSIQTNGTLLDDEWidfLKENG---FSVGISLDG-PKEIHDRnrVTKN-GKGSFdrvMRNIKLL----KEHGVEVNIR 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74139984 223 SVINRFNVD--EDMNEHIKALspvRWKVFQCLLIEGENSGEDALREAE--RFLIsnEEFETFLER 283
Cdd:COG0641 157 CTVTRENLDdpEELYDFLKEL---GFRSIQFNPVVEEGEADYSLTPEDygEFLI--ELFDEWLER 216
moaA PRK00164
GTP 3',8-cyclase MoaA;
74-239 2.58e-08

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 54.76  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   74 VSVnyhfTRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKQA---GLEKINFSGGEPFL-QDrgeyLGKLVRFC 144
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  145 KEELALPSVSIVSNGSLIRER---WfKDYGeyLDILAISCDSFDEQVNALI-GRGqgkknhvenlqKLRRWCRDYKVAF- 219
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLARRaaaL-KDAG--LDRVNVSLDSLDPERFKAItGRD-----------RLDQVLAGIDAALa 155

                        170       180
                 ....*....|....*....|....*....
gi 74139984  220 ------KINSVINR-FNVDE--DMNEHIK 239
Cdd:PRK00164 156 agltpvKVNAVLMKgVNDDEipDLLEWAK 184
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 74-239 6.28e-08

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 53.53  E-value: 6.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  74 VSVnyhfTRQCNYKCGFC-----FHTAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQdRGeyLGKLVRFCKEEL 148
Cdd:COG2896  18 ISV----TDRCNFRCTYCmpeegYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR-KD--LPELIARLAALP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984 149 ALPSVSIVSNGSLIRER--WFKDYGeyLDILAISCDSFDEQVNALIGRGqGKKNHV-ENLQKLRrwcrdyKVAF---KIN 222
Cdd:COG2896  91 GIEDLALTTNGSLLARYaeALKAAG--LDRVNVSLDSLDPERFRRITRR-DDLDKVlAGIDAAL------AAGLtpvKIN 161

                       170       180
                ....*....|....*....|
gi 74139984 223 SVINR-FNVDE--DMNEHIK 239
Cdd:COG2896 162 AVVMRgVNDDEilDLLEFAK 181
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 80-245 6.89e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 49.80  E-value: 6.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  80 FTRQCNYKCGFCfH---------TAKTSFVLP---LEEAKRGLLLLKQAGleKINFSGGEPFLQdrGEYLGKLVRFCKEE 147
Cdd:COG1180  27 FTQGCNLRCPYC-HnpeisqgrpDAAGRELSPeelVEEALKDRGFLDSCG--GVTFSGGEPTLQ--PEFLLDLAKLAKEL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984 148 -LAlpsVSIVSNGSLIRERwFKDYGEYLDILAISCDSFDEQV-NALIGRGQgkKNHVENLQKLRR-----WCRdykvafk 220
Cdd:COG1180 102 gLH---TALDTNGYIPEEA-LEELLPYLDAVNIDLKAFDDEFyRKLTGVSL--EPVLENLELLAEsgvhvEIR------- 168

                       170       180
                ....*....|....*....|....*....
gi 74139984 221 iNSVINRFNVDED----MNEHIKALSPVR 245
Cdd:COG1180 169 -TLVIPGLNDSEEeleaIARFIAELGDVI 196
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 72-232 1.45e-06

SynChlorMet cassette radical SAM/SPASM protein ScmE; 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 closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 49.47  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    72 TPVSVNYHFTRQCNYKCGFCFH---TAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQ-DRGEYLGKLV----RF 143
Cdd:TIGR04250   1 TPRSVDIDITGRCNLRCRYCSHfssAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRsDFREIIDGIVknrmRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   144 ckeelalpsvSIVSNGSLIRErwfkdygEYLDILAIS--CDSFDEQVNALIG------RGQGK-KNHVENLQKLRRwcrd 214
Cdd:TIGR04250  81 ----------SILSNGTLITD-------AIASFLAATrrCDYVQVSIDGSTPgthdrlRGTGSfLQAVEGIELLRK---- 139

                         170
                  ....*....|....*...
gi 74139984   215 YKVAFKINSVINRFNVDE 232
Cdd:TIGR04250 140 HAIPVVVRVTIHRWNVDD 157
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 83-213 8.10e-06

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 46.72  E-value: 8.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  83 QCNYKCGFC------FHTAKTSFVLPLEEAKRGLL-LLKQAGLEKIN-----FSG-GEPFLQdrgEYLGKLVRFCKEELA 149
Cdd:COG0731  33 TCNFDCVYCqrgrttDLTRERREFDDPEEILEELIeFLRKLPEEAREpdhitFSGsGEPTLY---PNLGELIEEIKKLRG 109

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74139984 150 LPsVSIVSNGSLI-RERWFKDYGEyLDILAISCDSFDEQVNALIGRGQGK---KNHVENLQKLRRWCR 213
Cdd:COG0731 110 IK-TALLTNGSLLhRPEVREELLK-ADQVYPSLDAADEETFRKINRPHPGlswERIIEGLELFRKLYK 175
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 26-232 1.47e-05

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 46.29  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   26 SGLAILFCWLrialgwldpGKEQPQVRGEPEDTQETQEDGNSTQPTTPVSVNYH----------FTRQCNYKCGFCFHTA 95
Cdd:PLN02951   9 LGFRSSSFQL---------QEPGSSIFSASSSYAADQVDPEASNPVSDMLVDSFgrrhnylrisLTERCNLRCQYCMPEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   96 -----KTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRgeyLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDY 170
Cdd:PLN02951  80 gveltPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKD---IEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74139984  171 GEYLDILAISCDSFDEQVNALIGRgqgKKNHVENLQKLRRWCRDYKVAFKINSVINR-FNVDE 232
Cdd:PLN02951 157 EAGLTSLNISLDTLVPAKFEFLTR---RKGHDRVLESIDTAIELGYNPVKVNCVVMRgFNDDE 216
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 84-177 2.38e-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: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    84 CNYKCGFCFHTA----KTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDrgEYLGKLVRFCKEELALPSVsIVSNG 159
Cdd:pfam13353  15 CNHHCKGCFNPEtwdfKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNA--EALLELVKRVREECPEKDI-WLWTG 91

                          90       100
                  ....*....|....*....|.
gi 74139984   160 SL---IRERWFKDYGEYLDIL 177
Cdd:pfam13353  92 YTfeeLQSKDQLELLKLIDVL 112
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
 75-131 6.41e-04

radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain protein are predicted peptide maturases, similar to PqqE, AlbA, the mycofactocin radical SAM maturase, and many others that share the peptide modification radical SAM protein C-terminal additional 4Fe4S-binding domain (TIGR04085). Members co-occur with a protein of unknown function that may be a chaperone or immunity protein and with a peptide that may have twelve or more cysteines occurring regularly spaced every fourth residue. These Cys residues tend to be flanked by residues with small side chains that provide minimal steric hindrance to crosslink formation by the radical SAM enzyme as in the subtilosin A system.


Pssm-ID: 200366 [Multi-domain]  Cd Length: 359  Bit Score: 41.41  E-value: 6.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74139984    75 SVNYHFTRQCNYKCGFCFHTAKTSF-VLPLEEAKRG--LLLLKQAGLEK----INFSGGEPFLQ 131
Cdd:TIGR04115   3 SITFIVTDDCQLACKYCYQTGKNKNkRMSFETAKKAvdYILSGNKGFGEpsviWDFIGGEPLLE 66
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
 84-283 2.02e-03

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 39.90  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984   84 CNYKCGFCFH-------TAKTSFVLPLE--EAKRGLLLLKQAGLEKINFSGGEPFLQDRgEYLGKLVRFCKE----ELAL 150
Cdd:PRK13758  15 CNLKCTYCFYhslsdnrNVKSYGIMRDEvlESMVKRVLNEAEGHCSFAFQGGEPTLAGL-EFFEELMELQRKhnykNLKI 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  151 PSvSIVSNGSLIRERWFKDYGEYLDILAISCDSFDE--QVNALIGRGQGKKNHVENLQKLrrwCRDYKVAFKINSVINRf 228
Cdd:PRK13758  94 YN-SLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEihNLNRKDCCGLDTFSKVERAAEL---FKKYKVEFNILCVVTS- 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74139984  229 NVDEDMNEHIKALSPVRWKVFQ---CLliegensgeDAL---REAERFLISNEEFETFLER 283
Cdd:PRK13758 169 NTARHVNKIYKYFKEKDFKFLQfinCL---------DPLyeeKGKYNYSLKPKDYTKFLKN 220
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 84-180 9.68e-03

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: 37.04  E-value: 9.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984  84 CNYKCGFC-----FHTAKTSFvLPLEEAkrgLLLLKQAGLEKINFSGGEPFLQDRGEYLgkLVRFCKEELalpSVSIVSN 158
Cdd:COG0602  30 CNLRCSWCdtkyaWDGEGGKR-MSAEEI---LEEVAALGARHVVITGGEPLLQDDLAEL--LEALKDAGY---EVALETN 100

                        90       100
                ....*....|....*....|..
gi 74139984 159 GSLIRErwfkdygEYLDILAIS 180
Cdd:COG0602 101 GTLPIP-------AGIDWVTVS 115
Fer4_14 pfam13394
4Fe-4S single cluster domain;
84-178 9.92e-03

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 35.42  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74139984    84 CNYKCGFCFH------TAKTSFVLPLEEAKRGLLLLKQAGLEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVS 157
Cdd:pfam13394   6 CNHSCPGCDNketwkfNYGEPFTEELEDQIIADLKDSYIKRQGLVLTGGEPLHPWNLPVLLKLLKRVKEEYPSKDIWLET 85

                          90       100
                  ....*....|....*....|.
gi 74139984   158 NGSLIRERWFKDYGEYLDILA 178
Cdd:pfam13394  86 GYTLAIDFEYPDTEEQLFTLS 106
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH