NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74724033|sp|Q8WXG1|]
View 

RecName: Full=S-adenosylmethionine-dependent nucleotide dehydratase RSAD2; Short=SAND; AltName: Full=Cytomegalovirus-induced gene 5 protein; AltName: Full=Radical S-adenosyl methionine domain-containing protein 2; AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible; Short=Viperin

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, ...
13-361 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: 798.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    13 LLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLvlRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFH 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQL--RGEPTRKEEEEDPDQPTTPTSVNYHFTRQCNYKCGFCFH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    93 TAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEY 172
Cdd:TIGR04278  79 TAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   173 LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLL 252
Cdd:TIGR04278 159 LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   253 IEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEA 332
Cdd:TIGR04278 239 IEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEEA 318
                         330       340
                  ....*....|....*....|....*....
gi 74724033   333 IKFSGFDEKMFLKRGGKYIWSKADLKLDW 361
Cdd:TIGR04278 319 IKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
13-361 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: 798.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    13 LLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLvlRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFH 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQL--RGEPTRKEEEEDPDQPTTPTSVNYHFTRQCNYKCGFCFH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    93 TAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEY 172
Cdd:TIGR04278  79 TAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   173 LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLL 252
Cdd:TIGR04278 159 LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   253 IEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEA 332
Cdd:TIGR04278 239 IEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEEA 318
                         330       340
                  ....*....|....*....|....*....
gi 74724033   333 IKFSGFDEKMFLKRGGKYIWSKADLKLDW 361
Cdd:TIGR04278 319 IKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
72-348 1.49e-101

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: 301.01  E-value: 1.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   72 PTSVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQdrGEYLGKLVRF 142
Cdd:NF038283   1 ELVINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  143 CKvELRLpSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKN--HVENLQKLRRWCRDY--RVAF 218
Cdd:NF038283  79 AK-ELGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  219 KINSVINRFNVEEDMTEQIKALNPVRWKVFQCLLIEGENcgedalreaERFVIGDEEFERFLERHKEV-SCLVPESNQKM 297
Cdd:NF038283 157 KINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDM 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74724033  298 KDSYLILDEYMRFL-NCRKGRK-DPSKSILDVGVEEAIKFSGFDEKMFLKRGG 348
Cdd:NF038283 228 TGSYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
78-262 1.44e-21

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: 91.24  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  78 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKEAGMEKINFSGGEPFLQ-DRGEYLGKLVRfckvELRLPSV 152
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLYpELAELLRRLKK----ELPGFEI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033 153 SIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNhvENLQKLRRWcRDYRVAFKINSVINR-FNVE 230
Cdd:cd01335  78 SIETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKEL-REAGLGLSTTLLVGLgDEDE 154
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74724033 231 EDMTEQIKALNPV----RWKVFQCLLIEGENCGEDA 262
Cdd:cd01335 155 EDDLEELELLAEFrspdRVSLFRLLPEEGTPLELAA 190
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
74-223 7.06e-19

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: 82.64  E-value: 7.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  74 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKEAGMEKINFSGGEPFLqdRgEYLGKLVRFCKvELRLPs 151
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAK-ELGIR- 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74724033 152 VSIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHV-ENLqklrRWCRDYRVAFKINSV 223
Cdd:COG0535  76 VNLSTNGTLLTEELAERLAEAgLDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-209 1.68e-17

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: 78.72  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    79 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPsVSI 154
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIR-ITL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74724033   155 VSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRR 209
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE 135
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
77-255 1.35e-12

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: 66.27  E-value: 1.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033     77 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKEAG-----MEKINFSGGEPFLQDRG--EYLGKLVRFCKVEL 147
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSPEqlEELLEAIREILGLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    148 RLPSVSIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRwcrdyRVAFKINS-VIN 225
Cdd:smart00729  85 KDVEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-----AGPIKVSTdLIV 159
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 74724033    226 RFNVE-----EDMTEQIKALNPVRWKVFQCLLIEG 255
Cdd:smart00729 160 GLPGEteedfEETLKLLKELGPDRVSIFPLSPRPG 194
moaA PRK00164
GTP 3',8-cyclase MoaA;
80-187 3.16e-05

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 45.13  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   80 TRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKEA---GMEKINFSGGEPFL-QDrgeyLGKLVRFCKVELRLP 150
Cdd:PRK00164  24 TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAALAALPGIR 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 74724033  151 SVSIVSNGSLIRER---WFQNyGeyLDILAISCDSFDEEV 187
Cdd:PRK00164  97 DLALTTNGYLLARRaaaLKDA-G--LDRVNVSLDSLDPER 133
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
13-361 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: 798.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    13 LLSVFRQPLSSLWRSLVPLFCWLRATFWLLATKRRKQQLvlRGPDETKEEEEDPPLPTTPTSVNYHFTRQCNYKCGFCFH 92
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQL--RGEPTRKEEEEDPDQPTTPTSVNYHFTRQCNYKCGFCFH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    93 TAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPSVSIVSNGSLIRERWFQNYGEY 172
Cdd:TIGR04278  79 TAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGEY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   173 LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRWCRDYRVAFKINSVINRFNVEEDMTEQIKALNPVRWKVFQCLL 252
Cdd:TIGR04278 159 LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCLL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   253 IEGENCGEDALREAERFVIGDEEFERFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCRKGRKDPSKSILDVGVEEA 332
Cdd:TIGR04278 239 IEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEEA 318
                         330       340
                  ....*....|....*....|....*....
gi 74724033   333 IKFSGFDEKMFLKRGGKYIWSKADLKLDW 361
Cdd:TIGR04278 319 IKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
72-348 1.49e-101

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: 301.01  E-value: 1.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   72 PTSVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQdrGEYLGKLVRF 142
Cdd:NF038283   1 ELVINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  143 CKvELRLpSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGKKN--HVENLQKLRRWCRDY--RVAF 218
Cdd:NF038283  79 AK-ELGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  219 KINSVINRFNVEEDMTEQIKALNPVRWKVFQCLLIEGENcgedalreaERFVIGDEEFERFLERHKEV-SCLVPESNQKM 297
Cdd:NF038283 157 KINTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDM 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74724033  298 KDSYLILDEYMRFL-NCRKGRK-DPSKSILDVGVEEAIKFSGFDEKMFLKRGG 348
Cdd:NF038283 228 TGSYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
78-262 1.44e-21

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: 91.24  E-value: 1.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  78 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKEAGMEKINFSGGEPFLQ-DRGEYLGKLVRfckvELRLPSV 152
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLYpELAELLRRLKK----ELPGFEI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033 153 SIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNhvENLQKLRRWcRDYRVAFKINSVINR-FNVE 230
Cdd:cd01335  78 SIETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKEL-REAGLGLSTTLLVGLgDEDE 154
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 74724033 231 EDMTEQIKALNPV----RWKVFQCLLIEGENCGEDA 262
Cdd:cd01335 155 EDDLEELELLAEFrspdRVSLFRLLPEEGTPLELAA 190
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
74-223 7.06e-19

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: 82.64  E-value: 7.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  74 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKEAGMEKINFSGGEPFLqdRgEYLGKLVRFCKvELRLPs 151
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAK-ELGIR- 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74724033 152 VSIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHV-ENLqklrRWCRDYRVAFKINSV 223
Cdd:COG0535  76 VNLSTNGTLLTEELAERLAEAgLDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-209 1.68e-17

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: 78.72  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    79 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRGEYLGKLVRFCKVELRLPsVSI 154
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIR-ITL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74724033   155 VSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRR 209
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE 135
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
77-255 1.35e-12

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: 66.27  E-value: 1.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033     77 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKEAG-----MEKINFSGGEPFLQDRG--EYLGKLVRFCKVEL 147
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSPEqlEELLEAIREILGLA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    148 RLPSVSIVSNGSLIRERWFQNYGEY-LDILAISCDSFDEEVNVLIGRGQGKKNHVENLQKLRRwcrdyRVAFKINS-VIN 225
Cdd:smart00729  85 KDVEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-----AGPIKVSTdLIV 159
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 74724033    226 RFNVE-----EDMTEQIKALNPVRWKVFQCLLIEG 255
Cdd:smart00729 160 GLPGEteedfEETLKLLKELGPDRVSIFPLSPRPG 194
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
80-282 1.34e-09

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 58.84  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  80 TRQCNYKCGFCF---HTAKTSFVLPLEEAKRGLLLLKEAGME----KINFSGGEPFLqdRGEYLGKLVRFCKVELRLP-- 150
Cdd:COG0641   8 TSRCNLRCSYCYyseGDEGSRRRMSEETAEKAIDFLIESSGPgkelTITFFGGEPLL--NFDFIKEIVEYARKYAKKGkk 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033 151 -SVSIVSNGSLIRERWfqnygeyLDILA-------ISCDSfDEEVN----VLIGrgqGKKNH---VENLQKLrrwcRDYR 215
Cdd:COG0641  86 iRFSIQTNGTLLDDEW-------IDFLKengfsvgISLDG-PKEIHdrnrVTKN---GKGSFdrvMRNIKLL----KEHG 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74724033 216 VAFKINSVINRFNVeEDMTEQIKALNPVRWKVFQCLLIEGENCGEDALREaerfvigdEEFERFLER 282
Cdd:COG0641 151 VEVNIRCTVTRENL-DDPEELYDFLKELGFRSIQFNPVVEEGEADYSLTP--------EDYGEFLIE 208
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
71-231 8.22e-07

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: 50.24  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    71 TPTSVNYHFTRQCNYKCGFCFH---TAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQ-DRGEYLGKLVRfckVE 146
Cdd:TIGR04250   1 TPRSVDIDITGRCNLRCRYCSHfssAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRsDFREIIDGIVK---NR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   147 LRLpsvSIVSNGSLIRERW--FQNYGEYLDILAISCD-SFDEEVNVLIGRGQGKKNhVENLQKLRRwcrdYRVAFKINSV 223
Cdd:TIGR04250  78 MRF---SILSNGTLITDAIasFLAATRRCDYVQVSIDgSTPGTHDRLRGTGSFLQA-VEGIELLRK----HAIPVVVRVT 149

                  ....*...
gi 74724033   224 INRFNVEE 231
Cdd:TIGR04250 150 IHRWNVDD 157
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
82-212 1.30e-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: 49.03  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  82 QCNYKCGFC-------FHTAKTSFVLP---LEEAKRGLLLLKEAGME--KINFSG-GEPFLQdrgEYLGKLVRFCKvELR 148
Cdd:COG0731  33 TCNFDCVYCqrgrttdLTRERREFDDPeeiLEELIEFLRKLPEEAREpdHITFSGsGEPTLY---PNLGELIEEIK-KLR 108
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74724033 149 LPSVSIVSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRGQGK---KNHVENLQKLRRWCR 212
Cdd:COG0731 109 GIKTALLTNGSLLHRPEVREELLKADQVYPSLDAADEETFRKINRPHPGlswERIIEGLELFRKLYK 175
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
79-186 1.91e-06

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 48.26  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  79 FTRQCNYKCGFCfH---------TAKTSFVLP---LEEAKRGLLLLKEAGMekINFSGGEPFLQdrGEYLGKLVRFCKvE 146
Cdd:COG1180  27 FTQGCNLRCPYC-HnpeisqgrpDAAGRELSPeelVEEALKDRGFLDSCGG--VTFSGGEPTLQ--PEFLLDLAKLAK-E 100
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 74724033 147 LRLpSVSIVSNGSLIRERwFQNYGEYLDILAISCDSFDEE 186
Cdd:COG1180 101 LGL-HTALDTNGYIPEEA-LEELLPYLDAVNIDLKAFDDE 138
moaA PRK00164
GTP 3',8-cyclase MoaA;
80-187 3.16e-05

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 45.13  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   80 TRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKEA---GMEKINFSGGEPFL-QDrgeyLGKLVRFCKVELRLP 150
Cdd:PRK00164  24 TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAALAALPGIR 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 74724033  151 SVSIVSNGSLIRER---WFQNyGeyLDILAISCDSFDEEV 187
Cdd:PRK00164  97 DLALTTNGYLLARRaaaLKDA-G--LDRVNVSLDSLDPER 133
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
80-284 3.30e-05

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: 45.05  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033  80 TRQCNYKCGFC-----FHTAKTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQdRGeyLGKLVRFCKVELRLPSVSI 154
Cdd:COG2896  21 TDRCNFRCTYCmpeegYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR-KD--LPELIARLAALPGIEDLAL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033 155 VSNGSLIrerwfqnyGEYLDILA--------ISCDSFDEEVNVLIGRGqGKKNHV-ENLQKLRrwcrdyRVAF---KINS 222
Cdd:COG2896  98 TTNGSLL--------ARYAEALKaagldrvnVSLDSLDPERFRRITRR-DDLDKVlAGIDAAL------AAGLtpvKINA 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033 223 VINR-FNVEE--DMTEQIKALN-PVRwkvfqclLIE----GENCGEDalreAERFVIGDEEFERFLERHK 284
Cdd:COG2896 163 VVMRgVNDDEilDLLEFAKERGiDLR-------FIElmplGEGGGWR----RDQVVSAAEILERLEARFP 221
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
74-130 3.75e-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: 42.18  E-value: 3.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74724033    74 SVNYHFTRQCNYKCGFCFHTAKTSF-VLPLEEAKRG--LLLLKEAGMEK----INFSGGEPFLQ 130
Cdd:TIGR04115   3 SITFIVTDDCQLACKYCYQTGKNKNkRMSFETAKKAvdYILSGNKGFGEpsviWDFIGGEPLLE 66
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
83-176 2.45e-03

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: 37.92  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033    83 CNYKCGFCFHTA----KTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDrgEYLGKLVRfcKVELRLPSVSIVS-N 157
Cdd:pfam13353  15 CNHHCKGCFNPEtwdfKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNA--EALLELVK--RVREECPEKDIWLwT 90
                          90       100
                  ....*....|....*....|..
gi 74724033   158 GSL---IRERWFQNYGEYLDIL 176
Cdd:pfam13353  91 GYTfeeLQSKDQLELLKLIDVL 112
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
80-231 3.60e-03

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 38.97  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74724033   80 TRQCNYKCGFCFHTA-----KTSFVLPLEEAKRGLLLLKEAGMEKINFSGGEPFLQDRgeyLGKLVRFCKVELRLPSVSI 154
Cdd:PLN02951  65 TERCNLRCQYCMPEEgveltPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKD---IEDICLQLSSLKGLKTLAM 141
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74724033  155 VSNGSLIRERWFQNYGEYLDILAISCDSFDEEVNVLIGRgqgKKNHVENLQKLRRWCRDYRVAFKINSVINR-FNVEE 231
Cdd:PLN02951 142 TTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTR---RKGHDRVLESIDTAIELGYNPVKVNCVVMRgFNDDE 216
 
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